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(3b,4a,5a)-4,14-dimethylcholest-8-en-3-ol + [reduced NADPH-hemoprotein reductase] + O2
? + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
good substrate, 67% of activity compared to obtusifoliol
-
-
?
(3beta,4alpha,5alpha)-4,14-dimethylcholest-8-en-3-ol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
r
14alpha-methyl-24,28-dihydrofecosterol + [reduced NADPH-hemoprotein reductase] + O2
? + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
50% of activity compared to obtusifoliol
-
-
?
14alpha-methylzymosterol + [reduced NADPH-hemoprotein reductase] + O2
?
2-phenylimidazole + [reduced NADPH-hemoprotein reductase] + O2
?
-
2-phenylimidazole binding causes thermally induced alterations in CYP51 active site structure and/or binding modes for the small ligand
-
-
?
24(28)-methylene-24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
(3beta,5alpha)-4,4-dimethylcholesta-8,14-dien-3-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
24,25-dihydro-4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
24,28-dihydroobtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
24-methylene-24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
14alpha-demethyl-24-methylene-4alpha-methyl-5alpha-ergosta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
24-methylene-24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
24-methylenedihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
24-methylenedihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
preferred substrate
-
-
?
7-lanosten-3beta-ol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethylcholesta-7,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
very low activity
-
-
?
7-lanostene-3beta,32-diol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethylcholesta-7,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
very low activity
-
-
?
8-lanostene-3beta,32-diol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethylcholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
eburicol + O2 + [reduced NADPH-hemoprotein reductase] + O2
2-(3-hydroxy-4,4,10,13-tetramethyl-2,3,4,5,6,7,10,11,12,13,16,17-dodecahydro-1H-cyclopenta[a]phenanthren-17-yl)-6-methyl-5-methylene-heptanoic acid + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
eburicol + [reduced NADPH-hemoprotein reductase] + O2
?
eburicol + [reduced NADPH-hemoprotein reductase] + O2
? + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
estriol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
estriol + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
lanosterol + NADPH + O2
4,4-dimethylcholesta-8,14,24-trien-3-ol + NADP+ + H2O
artificial fused enzymes have comparable activity to the reconstituted system. Reduction of CYP51 both in the fused enzyme and the reconstituted system is biphasic and consisted of an initial fast phase followed by a slow phase
-
-
?
lanosterol + O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14,24-triene-3beta-ol + formate + NADP+ + H2O
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethylcholesta-8,14,24-trien-3-ol + [oxidized NADPH-hemoprotein reductase] + H2O
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethylcholesta-8,14,24-trienol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethylzymosterol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
norlanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
?
additional information
?
-
14alpha-methylzymosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
14alpha-methylzymosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
(3beta,5alpha)-4,4-dimethylcholesta-8,14-dien-3-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
(3beta,5alpha)-4,4-dimethylcholesta-8,14-dien-3-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
(3beta,5alpha)-4,4-dimethylcholesta-8,14-dien-3-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
8-lanosta-3beta-ol
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
DHL
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
8-lanosten-3beta-ol
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
4,4,14alpha-trimethyl-5alpha-cholesta-8-en-3beta-ol
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
8-lanosta-3beta-ol
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
DHL
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
8-lanosten-3beta-ol
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
4,4,14alpha-trimethyl-5alpha-cholesta-8-en-3beta-ol
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
8-lanosta-3beta-ol
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
DHL
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
8-lanosten-3beta-ol
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
4,4,14alpha-trimethyl-5alpha-cholesta-8-en-3beta-ol
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
8-lanosta-3beta-ol
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
DHL
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
8-lanosten-3beta-ol
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
4,4,14alpha-trimethyl-5alpha-cholesta-8-en-3beta-ol
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
8-lanosta-3beta-ol
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
DHL
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
8-lanosten-3beta-ol
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
4,4,14alpha-trimethyl-5alpha-cholesta-8-en-3beta-ol
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
not the natural substrate
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
8-lanosta-3beta-ol
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
DHL
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
8-lanosten-3beta-ol
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
4,4,14alpha-trimethyl-5alpha-cholesta-8-en-3beta-ol
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
the enzyme is involved in ergosterol and cholesterol biosynthesis
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
the enzyme is involved in ergosterol and cholesterol biosynthesis
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
i.e. anosta-8-en-3ebta-ol
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
the enzyme is involved in ergosterol and cholesterol biosynthesis
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
the enzyme is involved in ergosterol and cholesterol biosynthesis
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
the enzyme is involved in ergosterol and cholesterol biosynthesis
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
24,28-dihydroobtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
good substrate, 75% of activity to obtusifoliol
-
-
?
24,28-dihydroobtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
DHO
-
-
?
24,28-dihydroobtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
4alpha,14alpha-dimethyl-5alpha-ergosta-8-en-3beta-ol
-
-
?
24,28-dihydroobtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
very poor substrate, about 10% of obtusifoliol demethylation, activity disappears in the presence of same concentration of lanosterol, 24-methylene-24,25-dihydrolanosterol, obtusifoliol or 24,25-dihydrolanosterol
-
-
?
24,28-dihydroobtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
DHO
-
-
?
24,28-dihydroobtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
4alpha,14alpha-dimethyl-5alpha-ergosta-8-en-3beta-ol
-
-
?
24,28-dihydroobtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
good substrate, 75% of activity to obtusifoliol
-
-
?
24,28-dihydroobtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
DHO
-
-
?
24,28-dihydroobtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
4alpha,14alpha-dimethyl-5alpha-ergosta-8-en-3beta-ol
-
-
?
24-methylene-24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
poorest substrate, catalyzes 14alpha-demethylation of 24-methylene-DHL, but activity is considerably lower than that for lanosterol and for 24,25-dihydrolanosterol, DHL
-
-
?
24-methylene-24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
4,4,14alpha-trimethylergosta-8,24(28)-dien-3beta-ol
-
-
?
24-methylene-24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
24-methylenelanost-8-en-3beta-ol, 24-methylene-DHL
-
-
?
24-methylene-24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
good substrate
-
-
?
24-methylene-24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
4,4,14alpha-trimethylergosta-8,24(28)-dien-3beta-ol
-
-
?
24-methylene-24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
activity for 24-methylene-DHL is considerably higher, 4fold, than that for 24,25-dihydrolanosterol, DHL
-
-
?
24-methylene-24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
24-methylenelanost-8-en-3beta-ol, 24-methylene-DHL
-
-
?
24-methylene-24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
about 60% activity to that of lanosterol
-
-
?
24-methylenedihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
24-methylenedihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
24-methylenedihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
24-methylenedihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis
-
-
?
24-methylenedihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
24-methylenedihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
24-methylenedihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
24-methylenedihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis
-
-
?
24-methylenedihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
24-methylenedihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis
-
-
?
eburicol + [reduced NADPH-hemoprotein reductase] + O2
?
-
isozymes CYP51A and CYP51B
-
-
?
eburicol + [reduced NADPH-hemoprotein reductase] + O2
?
-
isozymes CYP51A and CYP51B
-
-
?
eburicol + [reduced NADPH-hemoprotein reductase] + O2
?
i.e. 24-methylenelanosta-8-en-3beta-ol
-
-
?
eburicol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
eburicol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
eburicol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
eburicol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
eburicol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
eburicol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
estriol + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
estriol + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
lanosterol + O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14,24-triene-3beta-ol + formate + NADP+ + H2O
-
-
-
-
?
lanosterol + O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14,24-triene-3beta-ol + formate + NADP+ + H2O
-
-
-
?
lanosterol + O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14,24-triene-3beta-ol + formate + NADP+ + H2O
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
lanosta-8,24-dien-3beta-ol
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
4,4,14alpha-trimethyl-5alpha-cholesta-8,24-dien-3beta-ol
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
lanosta-8,24-dien-3beta-ol
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
4,4,14alpha-trimethyl-5alpha-cholesta-8,24-dien-3beta-ol
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
lanosta-8,24-dien-3beta-ol
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
4,4,14alpha-trimethyl-5alpha-cholesta-8,24-dien-3beta-ol
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
best substrate
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
natural substrate
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
lanosta-8,24-dien-3beta-ol
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
lanosta-8,24-dien-3beta-ol
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
4,4,14alpha-trimethyl-5alpha-cholesta-8,24-dien-3beta-ol
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
4,4,14alpha-trimethyl-5alpha-cholesta-8,24-dien-3beta-ol
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
best substrate
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
natural substrate
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
lanosta-8,24-dien-3beta-ol
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
4,4,14alpha-trimethyl-5alpha-cholesta-8,24-dien-3beta-ol
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
P-45014DM catalyzes all three oxygenation steps from lanosterol to dimethylcholestratrienol
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
ergosterol synthesis in yeast involves oxidative removal of the 14alpha-methyl group, C-32, of lanosterol
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
lanosta-8,24-dien-3beta-ol
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
4,4,14alpha-trimethyl-5alpha-cholesta-8,24-dien-3beta-ol
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethylcholesta-8,14,24-trien-3-ol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethylcholesta-8,14,24-trien-3-ol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethylcholesta-8,14,24-trien-3-ol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethylcholesta-8,14,24-trien-3-ol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethylcholesta-8,14,24-trien-3-ol + [oxidized NADPH-hemoprotein reductase] + H2O
i.e. lanosta-8,24-dien-3beta-ol
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethylcholesta-8,14,24-trien-3-ol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethylcholesta-8,14,24-trien-3-ol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethylcholesta-8,14,24-trien-3-ol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethylcholesta-8,14,24-trien-3-ol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethylcholesta-8,14,24-trienol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethylcholesta-8,14,24-trienol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
deletion of the enzyme is lethal
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethylcholesta-8,14,24-trienol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethylcholesta-8,14,24-trienol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
deletion of the enzyme is lethal
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethylcholesta-8,14,24-trienol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethylcholesta-8,14,24-trienol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
isozymes CYP51A and CYP51B
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
isozymes CYP51A and CYP51B
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
production of follicular fluid-meiosis activating steroid by lanosterol demethylation
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
the enzyme is involved in ergosterol and cholesterol biosynthesis
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
production of follicular fluid-meiosis activating steroid by lanosterol demethylation
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
CYP51 responds to cholesterol feedback regulation, being upregulated in sterol limiting conditions and downregulated in cholesterol rich conditions, regulation involves the sterol regulatory elements SRE in the promoter of the gene which bind sterol regulatory element binding protein, SREBP, the CYP51 promoter also contains a cAMP regulatory element, CRE, binding cAMP regulatory proteins CREB/CREM, overview
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
the enzyme is involved in ergosterol and cholesterol biosynthesis
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
the enzyme is regulated by cholesterol feedback regulation through sterol regulatory element binding proteins, i.e. SREBPs, regulation mechanisms of enzyme expression, overview
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
the enzyme is involved in ergosterol and cholesterol biosynthesis
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
the enzyme is involved in ergosterol and cholesterol biosynthesis
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
the enzyme is involved in ergosterol and cholesterol biosynthesis
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
the enzyme is involved in ergosterol and cholesterol biosynthesis
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
active site contains an isoleucine, lanosterol is the preferred substrate
-
-
?
norlanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
norlanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
norlanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
norlanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
i.e. 4alpha,14alpha-dimethylcholesta-8,24-dien-3beta-ol
-
-
?
norlanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
norlanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis
-
-
?
norlanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
norlanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
norlanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis
-
-
?
norlanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
low activity
-
-
?
norlanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
i.e. 4alpha,4alpha-dimethylcholesta-8,24-dien-3beta-ol
-
-
?
norlanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
low activity
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
low activity
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
preferred substrate
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
low activity
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
low activity
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
low activity
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
preferred substrate
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
preferred substrate
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
the enzyme is involved in biosynthesis of sitosterol and brassinosteroids, pathways overview
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
low activity
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
low activity
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
preferred substrate
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
4alpha,14alpha-dimethyl-24-methylene-5alpha-cholesta-8-en-3beta-ol
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
catalyzes 14alpha-demethylation of obtusifoliol
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
4alpha,14alpha-dimethyl-5alpha-ergosta-8,24(28)-dien-3beta-ol
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
i.e. 4alpha,14alpha-dimethyl-5'-ergosta-8,24(24')-dien-3beta-ol
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
4alpha,14alpha-dimethyl-24-methylene-5alpha-cholesta-8-en-3beta-ol
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
catalyzes 14alpha-demethylation of obtusifoliol
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
4alpha,14alpha-dimethyl-5alpha-ergosta-8,24(28)-dien-3beta-ol
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
4alpha,14alpha-dimethyl-24-methylene-5alpha-cholesta-8-en-3beta-ol
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
catalyzes 14alpha-demethylation of obtusifoliol
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
4alpha,14alpha-dimethyl-5alpha-ergosta-8,24(28)-dien-3beta-ol
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
presence of the large phenylalanine side chain in the active site seems to lead to preferred processing of obtusifoliol
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
best substrate
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
4alpha,14alpha-dimethyl-24-methylene-5alpha-cholesta-8-en-3beta-ol
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
catalyzes 14alpha-demethylation of obtusifoliol
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
4alpha,14alpha-dimethyl-5alpha-ergosta-8,24(28)-dien-3beta-ol
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
additional information
?
-
-
azole binding properties of purified CYP51A and CYP51B, overview
-
-
?
additional information
?
-
-
azole binding properties of purified CYP51A and CYP51B, overview
-
-
?
additional information
?
-
-
enzyme of sterol biosynthesis, sterol 14-demethylation occurs in all organism exhibiting de novo sterol biosynthesis
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
the regio- and stereospecific 14alpha-demethylation CYP51 reaction proceeds in three steps, each requiring one molecule of oxygen and two NADPH-derived reducing equivalents, via 14alpha-carboxyalcohol and 14alpha-carboxyaldehyde intermediates, cleavage of the the C-C bond by radical or Bayer-Villiger mechanism, DELTA14,15 double bond introduction into the sterol core
-
-
?
additional information
?
-
-
enzyme of sterol biosynthesis, sterol 14-demethylation occurs in all organism exhibiting de novo sterol biosynthesis
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
substrate specificity
-
-
?
additional information
?
-
-
substrate specificity
-
-
?
additional information
?
-
-
can not catalyze demethylation of sterols having 4beta-methyl group, favorably interacts with sterols having saturated side chain
-
-
?
additional information
?
-
-
yeast enzyme poorly metabolizes sterols having saturated side chain, plant enzyme shows considerable activity for such sterols
-
-
?
additional information
?
-
-
substrate for 14alpha-demethylation reaction in plants is different from that in animals and fungi
-
-
?
additional information
?
-
-
narrow substrate selectivity
-
-
?
additional information
?
-
-
substrate recognition
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
14alpha-demethylation is a key step of sterol biosynthesis in eukaryotes
-
-
?
additional information
?
-
-
enzyme of plant sterol, phytosterol, biosynthesis
-
-
?
additional information
?
-
-
housekeeping enzyme essential for viability of mammals, essential step in cholesterol biosynthesis
-
-
?
additional information
?
-
-
enzyme of sterol biosynthesis, sterol 14-demethylation occurs in all organism exhibiting de novo sterol biosynthesis
-
-
?
additional information
?
-
-
enzyme of cholesterol biosynthesis
-
-
?
additional information
?
-
-
there is a possibility that P45014DM participates not only in sterol biogenesis but also in production of biosignal substance regulating meiosis of mammalian oocytes
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
analysis of active site by stectroscopic titration, resonance Raman spectroscopy and EPR
-
-
?
additional information
?
-
-
CYP51 plays a key role in fertilization by producing intermediates that could serve as ligands for nuclear receptors
-
-
?
additional information
?
-
-
enzyme inhibition may result in endocrine disruption since follicular fluid-meiosis activating steroid, the direct product of lanosterol demethylation, is involved in the control of meiosis
-
-
?
additional information
?
-
-
the regio- and stereospecific 14alpha-demethylation CYP51 reaction proceeds in three steps, each requiring one molecule of oxygen and two NADPH-derived reducing equivalents, via 14alpha-carboxyalcohol and 14alpha-carboxyaldehyde intermediates, cleavage of the the C-C bond by radical or Bayer-Villiger mechanism, DELTA14,15 double bond introduction into the sterol core
-
-
?
additional information
?
-
-
the enzyme catalyzes a step in the cholesterol biosynthesis via the mevalonate pathway, overview
-
-
?
additional information
?
-
-
structure-activity relationship study of enzyme-ligand binding, pyridine binds within the heme binding pocket in an analogy with azoles, overview
-
-
?
additional information
?
-
-
CYP51 participates in biosynthesis of cholesterol
-
-
?
additional information
?
-
-
the regio- and stereospecific 14alpha-demethylation CYP51 reaction proceeds in three steps, each requiring one molecule of oxygen and two NADPH-derived reducing equivalents, via 14alpha-carboxyalcohol and 14alpha-carboxyaldehyde intermediates, cleavage of the the C-C bond by radical or Bayer-Villiger mechanism, DELTA14,15 double bond introduction into the sterol core
-
-
?
additional information
?
-
the enzyme is a demethylation inhibitor fungicide resistance determinant in Monilinia fructicola field isolates
-
-
?
additional information
?
-
-
the enzyme is a demethylation inhibitor fungicide resistance determinant in Monilinia fructicola field isolates
-
-
?
additional information
?
-
-
involved in fertilization
-
-
?
additional information
?
-
-
the enzyme is involved in follicle-stimulating hormone-induced mouse oocyte maturation and follicle-stimulating hormone-induced oocyte meiotic resumption, regulation, overview. The enzyme is involved in CREB phosphorylation
-
-
?
additional information
?
-
analysis of active site by spectroscopic titration, resonance Raman spectroscopy and EPR
-
-
?
additional information
?
-
-
analysis of active site by spectroscopic titration, resonance Raman spectroscopy and EPR
-
-
?
additional information
?
-
-
P420 formation process with protonation of Cys394 and structure by binding of CO to P450, overview
-
-
?
additional information
?
-
-
the regio- and stereospecific 14alpha-demethylation CYP51 reaction proceeds in three steps, each requiring one molecule of oxygen and two NADPH-derived reducing equivalents, via 14alpha-carboxyalcohol and 14alpha-carboxyaldehyde intermediates, cleavage of the the C-C bond by radical or Bayer-Villiger mechanism, DELTA14,15 double bond introduction into the sterol core
-
-
?
additional information
?
-
CYP51 is a major checkpoint in membrane sterol biosynthesis, is a key target for fungal antibiotic therapy
-
-
?
additional information
?
-
-
CYP51 is a major checkpoint in membrane sterol biosynthesis, is a key target for fungal antibiotic therapy
-
-
?
additional information
?
-
-
CYP51b1 shows activity with coumarin derivatives as substrates, e.g. with 7-ethoxycoumarin, 4-methyl-7-hydroxycoumarin, 4-methyl-7-aminocoumarin, and 7-aminocoumarin-4-acetic acid, that are competitive to lanosterol. In the model system for assay of CYP51b1 activity, a flavin domain of the cytochrome P450BM-3, BMR, from Bacillus megaterium may serve as the electron donor, overview
-
-
?
additional information
?
-
analysis of active site by spectroscopic titration, resonance Raman spectroscopy and EPR
-
-
?
additional information
?
-
CYP51 is a major checkpoint in membrane sterol biosynthesis, is a key target for fungal antibiotic therapy
-
-
?
additional information
?
-
-
the regio- and stereospecific 14alpha-demethylation CYP51 reaction proceeds in three steps, each requiring one molecule of oxygen and two NADPH-derived reducing equivalents, via 14alpha-carboxyalcohol and 14alpha-carboxyaldehyde intermediates, cleavage of the the C-C bond by radical or Bayer-Villiger mechanism, DELTA14,15 double bond introduction into the sterol core
-
-
?
additional information
?
-
CYP51 is one of the key enzymes of sterol biosynthesis in biological kingdoms and is a prime target of antifungal drugs
-
-
?
additional information
?
-
-
CYP51 is one of the key enzymes of sterol biosynthesis in biological kingdoms and is a prime target of antifungal drugs
-
-
?
additional information
?
-
-
enzyme of sterol biosynthesis, sterol 14-demethylation occurs in all organism exhibiting de novo sterol biosynthesis
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
sterol composition of different species isolated from human lung, two distinct sterol compositional phenotypes occur, one, the wild-type, is characterized by DELTA7 C28- and C24 24-alkylsterols with only low proportions of higher molecular mass components, the other type, a mutant with 14alpha-demethylase deficiency, is dominated by high C31 and C32 24-alkylsterols, especially pneumocysterol, NMR sterol analysis, overview
-
-
?
additional information
?
-
-
substrate specificity
-
-
?
additional information
?
-
-
substrate specificity
-
-
?
additional information
?
-
-
housekeeping enzyme essential for viability of mammals, essential step in cholesterol biosynthesis
-
-
?
additional information
?
-
-
enzyme of sterol biosynthesis, sterol 14-demethylation occurs in all organism exhibiting de novo sterol biosynthesis
-
-
?
additional information
?
-
-
brain microsomes, existence of sterol biosynthetic pathway in brain, cholesterol is synthesized de novo in brain
-
-
?
additional information
?
-
-
removal of 14alpha-methyl group, C32, from 14alpha-methylated precursor sterols is an essential step of sterol biosynthesis in eukaryotes
-
-
?
additional information
?
-
-
enzyme of cholesterol biosynthesis
-
-
?
additional information
?
-
-
enzyme of cholesterol biosynthesis
-
-
?
additional information
?
-
enzyme of cholesterol biosynthesis
-
-
?
additional information
?
-
-
lanosterol 14-demethylation is situated at the root of sterol-biosynthetic branch of mevalonic acid pathway
-
-
?
additional information
?
-
enzyme for regulation of cholesterol biosynthesis
-
-
?
additional information
?
-
-
there is a possibility that P45014DM participates not only in sterol biogenesis but also in production of biosignal substance regulating meiosis of mammalian oocytes
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
the regio- and stereospecific 14alpha-demethylation CYP51 reaction proceeds in three steps, each requiring one molecule of oxygen and two NADPH-derived reducing equivalents, via 14alpha-carboxyalcohol and 14alpha-carboxyaldehyde intermediates, cleavage of the the C-C bond by radical or Bayer-Villiger mechanism, DELTA14,15 double bond introduction into the sterol core
-
-
?
additional information
?
-
-
substrate specificity
-
-
?
additional information
?
-
-
substrate specificity
-
-
?
additional information
?
-
-
substrate specificity
-
-
?
additional information
?
-
-
4beta-methyl group, C31, does not affect the activity of yeast P-45014DM, although removal reduces affinity for enzyme in some extent
-
-
?
additional information
?
-
-
8-double bond of lanosterol plays an important critical role in enzyme-substrate interaction of cytochrome P-45014DM
-
-
?
additional information
?
-
-
no activity with 6-lanostene-3beta,32-diol and lanostane-3beta,32-diol
-
-
?
additional information
?
-
-
yeast enzyme poorly metabolizes sterols having saturated side chain, plant enzyme shows considerable activity for such sterols
-
-
?
additional information
?
-
-
enzyme recognizes 8-lanostene structure and favourably interacts with 8-lanostene derivatives, can act also with substrates having 7-lanostene structure, utilizes them with lower efficiency than 8-lanostene derivatives
-
-
?
additional information
?
-
-
cycloartenol: not or very poor substrate
-
-
?
additional information
?
-
-
3-hydroxy group, the 8-lanostene conformation of sterol ring and the side-chain terminal, C25, C26, C27, are the essential structures of substrates for interacting with the yeast enzyme
-
-
?
additional information
?
-
-
narrow substrate selectivity
-
-
?
additional information
?
-
-
narrow substrate selectivity
-
-
?
additional information
?
-
-
substrate recognition
-
-
?
additional information
?
-
-
reaction reqires molecular oxygen, does not occur anaerobically
-
-
?
additional information
?
-
-
enzyme of sterol biosynthesis, sterol 14-demethylation occurs in all organism exhibiting de novo sterol biosynthesis
-
-
?
additional information
?
-
-
removal of 14alpha-methyl group, C32, from 14alpha-methylated precursor sterols is an essential step of sterol biosynthesis in eukaryotes
-
-
?
additional information
?
-
-
enzyme of ergosterol biosynthesis
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
14alpha-demethylation is a key step of sterol biosynthesis in eukaryotes
-
-
?
additional information
?
-
-
the regio- and stereospecific 14alpha-demethylation CYP51 reaction proceeds in three steps, each requiring one molecule of oxygen and two NADPH-derived reducing equivalents, via 14alpha-carboxyalcohol and 14alpha-carboxyaldehyde intermediates, cleavage of the the C-C bond by radical or Bayer-Villiger mechanism, DELTA14,15 double bond introduction into the sterol core
-
-
?
additional information
?
-
-
enzyme of sterol biosynthesis, sterol 14-demethylation occurs in all organism exhibiting de novo sterol biosynthesis
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
substrate specificity
-
-
?
additional information
?
-
-
substrate specificity
-
-
?
additional information
?
-
-
substrate binding spectra
-
-
?
additional information
?
-
-
substrate binding spectra
-
-
?
additional information
?
-
-
biosynthetic enzyme with very narrow substrate specificity
-
-
?
additional information
?
-
-
biosynthetic enzyme with very narrow substrate specificity
-
-
?
additional information
?
-
-
no activity with lanosterol, campesterol, sitosterol, or stigmasterol
-
-
?
additional information
?
-
-
enzyme is a multifunctional cytochrome P450, which as the same active site catalyze demethylation in three consecutive NADPH- and O2-dependent hydroxylation reactions, resulting in the elimination of the methyl group as formic acid and the introduction of a double bond at the DELTA14 position
-
-
?
additional information
?
-
-
enzyme is a multifunctional cytochrome P450, which as the same active site catalyze demethylation in three consecutive NADPH- and O2-dependent hydroxylation reactions, resulting in the elimination of the methyl group as formic acid and the introduction of a double bond at the DELTA14 position
-
-
?
additional information
?
-
-
substrate for 14alpha-demethylation reaction in plants is different from that in animals and fungi
-
-
?
additional information
?
-
-
plant sterol 14alpha-demethylase have high substrate specificity
-
-
?
additional information
?
-
-
plant sterol 14alpha-demethylase have high substrate specificity
-
-
?
additional information
?
-
-
catalyzes an essential step in sterol biosynthesis as evidenced by the absence of a 14alpha-methyl group in all known functional sterols, removal of the 14alpha-methyl group is essential
-
-
?
additional information
?
-
-
key enzyme in plant sterol, phytosterol, biosynthesis
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
enzyme of plant sterol, phytosterol, biosynthesis
-
-
?
additional information
?
-
-
poor activity with lanosterol, 24,25-dihydrolanosterol, and 24-methylenedihydrolanosterol, the regio- and stereospecific 14alpha-demethylation CYP51 reaction proceeds in three steps, each requiring one molecule of oxygen and two NADPH-derived reducing equivalents, via 14alpha-carboxyalcohol and 14alpha-carboxyaldehyde intermediates, cleavage of the the C-C bond by radical or Bayer-Villiger mechanism, DELTA14,15 double bond introduction into the sterol core
-
-
?
additional information
?
-
-
no substrate: lanosterol
-
-
?
additional information
?
-
-
poor activity with lanosterol, 24,25-dihydrolanosterol, and 24-methylenedihydrolanosterol, the regio- and stereospecific 14alpha-demethylation CYP51 reaction proceeds in three steps, each requiring one molecule of oxygen and two NADPH-derived reducing equivalents, via 14alpha-carboxyalcohol and 14alpha-carboxyaldehyde intermediates, cleavage of the the C-C bond by radical or Bayer-Villiger mechanism, DELTA14,15 double bond introduction into the sterol core
-
-
?
additional information
?
-
-
the organism can specifically regulate gene expression, e.g. for the sterol C14-demethylase, in response to derangements in its cellular functions
-
-
?
additional information
?
-
substrate specificity, the Trypanosoma cruzi enzyme prefers C4-dimethylsterols substrates, overview
-
-
?
additional information
?
-
-
substrate specificity, the Trypanosoma cruzi enzyme prefers C4-dimethylsterols substrates, overview
-
-
?
additional information
?
-
-
the regio- and stereospecific 14alpha-demethylation CYP51 reaction proceeds in three steps, each requiring one molecule of oxygen and two NADPH-derived reducing equivalents, via 14alpha-carboxyalcohol and 14alpha-carboxyaldehyde intermediates, cleavage of the the C-C bond by radical or Bayer-Villiger mechanism, DELTA14,15 double bond introduction into the sterol core
-
-
?
additional information
?
-
-
enzyme of sterol biosynthesis, sterol 14-demethylation occurs in all organism exhibiting de novo sterol biosynthesis
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
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-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
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-
the regio- and stereospecific 14alpha-demethylation CYP51 reaction proceeds in three steps, each requiring one molecule of oxygen and two NADPH-derived reducing equivalents, via 14alpha-carboxyalcohol and 14alpha-carboxyaldehyde intermediates, cleavage of the the C-C bond by radical or Bayer-Villiger mechanism, DELTA14,15 double bond introduction into the sterol core
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-
?
additional information
?
-
-
substrate specificity
-
-
?
additional information
?
-
-
substrate specificity
-
-
?
additional information
?
-
-
no activity with 31-norlanosterol, cycloeucalenol, 4alpha,14alpha-dimethyl-5alpha-ergost-9(11)-en-3beta-ol, 4alpha,14alpha-dimethyl-5alpha-ergost-7-en-3beta-ol, 8(9),24(25)-tetrahydro-31-norlanosterol, 24-methylenelanosterol, 24,28-dihydro-4beta-methyl-30-norobtusifoliol, 24,25-dihydrolanosterol, lanosterol, obtusifoliyl-3beta-methoxy, obtusifoliyl-3beta-acetoxy, obtusifoliyl-3beta-amino
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-
?
additional information
?
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-
biosynthetic enzyme with very narrow substrate specificity
-
-
?
additional information
?
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-
biosynthetic enzyme with very narrow substrate specificity
-
-
?
additional information
?
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P-450OBT 14DM has probably a specific apolar binding site for the side chain. DELTA8-double bond is absolute required for substrate demethylation and the 3-hydroxy group plays a critical role in enzyme-substrate interaction
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-
?
additional information
?
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-
enzyme with high degree of substrate and product specificity
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-
?
additional information
?
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-
plant sterol 14alpha-demethylase have high substrate specificity
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?
additional information
?
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-
plant sterol 14alpha-demethylase have high substrate specificity
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-
?
additional information
?
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-
narrow substrate selectivity
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-
?
additional information
?
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enzyme of sterol biosynthetic pathway
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?
additional information
?
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enzyme of sterol biosynthetic pathway
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-
?
additional information
?
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-
enzyme of plant sterol, phytosterol, biosynthesis
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-
?
additional information
?
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-
enzyme of plant sterol, phytosterol, biosynthesis
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-
?
additional information
?
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-
substrate specificity
-
-
?
additional information
?
-
-
no activity with 31-norlanosterol, cycloeucalenol, 4alpha,14alpha-dimethyl-5alpha-ergost-9(11)-en-3beta-ol, 4alpha,14alpha-dimethyl-5alpha-ergost-7-en-3beta-ol, 8(9),24(25)-tetrahydro-31-norlanosterol, 24-methylenelanosterol, 24,28-dihydro-4beta-methyl-30-norobtusifoliol, 24,25-dihydrolanosterol, lanosterol, obtusifoliyl-3beta-methoxy, obtusifoliyl-3beta-acetoxy, obtusifoliyl-3beta-amino
-
-
?
additional information
?
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-
biosynthetic enzyme with very narrow substrate specificity
-
-
?
additional information
?
-
-
P-450OBT 14DM has probably a specific apolar binding site for the side chain. DELTA8-double bond is absolute required for substrate demethylation and the 3-hydroxy group plays a critical role in enzyme-substrate interaction
-
-
?
additional information
?
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-
enzyme with high degree of substrate and product specificity
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-
?
additional information
?
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residues Ile381 and Leu321 are involved in substrate recognition
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?
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14alpha-methylzymosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
(3beta,5alpha)-4,4-dimethylcholesta-8,14-dien-3-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
24,25-dihydro-4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
24-methylenedihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
eburicol + [reduced NADPH-hemoprotein reductase] + O2
?
eburicol + [reduced NADPH-hemoprotein reductase] + O2
? + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
lanosterol + O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14,24-triene-3beta-ol + formate + NADP+ + H2O
-
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethylcholesta-8,14,24-trien-3-ol + [oxidized NADPH-hemoprotein reductase] + H2O
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethylcholesta-8,14,24-trienol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethylzymosterol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
norlanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
additional information
?
-
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
(3beta,5alpha)-4,4-dimethylcholesta-8,14-dien-3-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
(3beta,5alpha)-4,4-dimethylcholesta-8,14-dien-3-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
(3beta,5alpha)-4,4-dimethylcholesta-8,14-dien-3-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
8-lanosta-3beta-ol
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
DHL
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
8-lanosten-3beta-ol
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
4,4,14alpha-trimethyl-5alpha-cholesta-8-en-3beta-ol
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
8-lanosta-3beta-ol
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
DHL
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
8-lanosten-3beta-ol
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
4,4,14alpha-trimethyl-5alpha-cholesta-8-en-3beta-ol
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
not the natural substrate
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
the enzyme is involved in ergosterol and cholesterol biosynthesis
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
the enzyme is involved in ergosterol and cholesterol biosynthesis
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
the enzyme is involved in ergosterol and cholesterol biosynthesis
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
the enzyme is involved in ergosterol and cholesterol biosynthesis
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
the enzyme is involved in ergosterol and cholesterol biosynthesis
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
24-methylenedihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis
-
-
?
24-methylenedihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
24-methylenedihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis
-
-
?
24-methylenedihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis
-
-
?
eburicol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
eburicol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
lanosta-8,24-dien-3beta-ol
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
4,4,14alpha-trimethyl-5alpha-cholesta-8,24-dien-3beta-ol
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
natural substrate
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
lanosta-8,24-dien-3beta-ol
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
lanosta-8,24-dien-3beta-ol
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
4,4,14alpha-trimethyl-5alpha-cholesta-8,24-dien-3beta-ol
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
4,4,14alpha-trimethyl-5alpha-cholesta-8,24-dien-3beta-ol
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
natural substrate
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
lanosta-8,24-dien-3beta-ol
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
4,4,14alpha-trimethyl-5alpha-cholesta-8,24-dien-3beta-ol
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
P-45014DM catalyzes all three oxygenation steps from lanosterol to dimethylcholestratrienol
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
ergosterol synthesis in yeast involves oxidative removal of the 14alpha-methyl group, C-32, of lanosterol
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethylcholesta-8,14,24-trien-3-ol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethylcholesta-8,14,24-trien-3-ol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethylcholesta-8,14,24-trien-3-ol + [oxidized NADPH-hemoprotein reductase] + H2O
i.e. lanosta-8,24-dien-3beta-ol
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethylcholesta-8,14,24-trien-3-ol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethylcholesta-8,14,24-trien-3-ol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethylcholesta-8,14,24-trien-3-ol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethylcholesta-8,14,24-trien-3-ol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethylcholesta-8,14,24-trienol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
deletion of the enzyme is lethal
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethylcholesta-8,14,24-trienol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
deletion of the enzyme is lethal
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
production of follicular fluid-meiosis activating steroid by lanosterol demethylation
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
the enzyme is involved in ergosterol and cholesterol biosynthesis
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
production of follicular fluid-meiosis activating steroid by lanosterol demethylation
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
CYP51 responds to cholesterol feedback regulation, being upregulated in sterol limiting conditions and downregulated in cholesterol rich conditions, regulation involves the sterol regulatory elements SRE in the promoter of the gene which bind sterol regulatory element binding protein, SREBP, the CYP51 promoter also contains a cAMP regulatory element, CRE, binding cAMP regulatory proteins CREB/CREM, overview
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
the enzyme is involved in ergosterol and cholesterol biosynthesis
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
the enzyme is regulated by cholesterol feedback regulation through sterol regulatory element binding proteins, i.e. SREBPs, regulation mechanisms of enzyme expression, overview
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
the enzyme is involved in ergosterol and cholesterol biosynthesis
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
the enzyme is involved in ergosterol and cholesterol biosynthesis
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
the enzyme is involved in ergosterol and cholesterol biosynthesis
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
the enzyme is involved in ergosterol and cholesterol biosynthesis
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
norlanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
norlanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
i.e. 4alpha,14alpha-dimethylcholesta-8,24-dien-3beta-ol
-
-
?
norlanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
norlanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis
-
-
?
norlanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis
-
-
?
norlanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
i.e. 4alpha,4alpha-dimethylcholesta-8,24-dien-3beta-ol
-
-
?
norlanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
low activity
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
low activity
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
low activity
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
low activity
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
low activity
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
preferred substrate
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
the enzyme is involved in biosynthesis of sitosterol and brassinosteroids, pathways overview
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
low activity
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
preferred substrate
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
4alpha,14alpha-dimethyl-24-methylene-5alpha-cholesta-8-en-3beta-ol
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
4alpha,14alpha-dimethyl-5alpha-ergosta-8,24(28)-dien-3beta-ol
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
i.e. 4alpha,14alpha-dimethyl-5'-ergosta-8,24(24')-dien-3beta-ol
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
4alpha,14alpha-dimethyl-24-methylene-5alpha-cholesta-8-en-3beta-ol
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
4alpha,14alpha-dimethyl-5alpha-ergosta-8,24(28)-dien-3beta-ol
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
4alpha,14alpha-dimethyl-24-methylene-5alpha-cholesta-8-en-3beta-ol
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
4alpha,14alpha-dimethyl-5alpha-ergosta-8,24(28)-dien-3beta-ol
-
-
?
additional information
?
-
-
enzyme of sterol biosynthesis, sterol 14-demethylation occurs in all organism exhibiting de novo sterol biosynthesis
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
enzyme of sterol biosynthesis, sterol 14-demethylation occurs in all organism exhibiting de novo sterol biosynthesis
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
14alpha-demethylation is a key step of sterol biosynthesis in eukaryotes
-
-
?
additional information
?
-
-
enzyme of plant sterol, phytosterol, biosynthesis
-
-
?
additional information
?
-
-
housekeeping enzyme essential for viability of mammals, essential step in cholesterol biosynthesis
-
-
?
additional information
?
-
-
enzyme of sterol biosynthesis, sterol 14-demethylation occurs in all organism exhibiting de novo sterol biosynthesis
-
-
?
additional information
?
-
-
enzyme of cholesterol biosynthesis
-
-
?
additional information
?
-
-
there is a possibility that P45014DM participates not only in sterol biogenesis but also in production of biosignal substance regulating meiosis of mammalian oocytes
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
CYP51 plays a key role in fertilization by producing intermediates that could serve as ligands for nuclear receptors
-
-
?
additional information
?
-
-
enzyme inhibition may result in endocrine disruption since follicular fluid-meiosis activating steroid, the direct product of lanosterol demethylation, is involved in the control of meiosis
-
-
?
additional information
?
-
-
the enzyme catalyzes a step in the cholesterol biosynthesis via the mevalonate pathway, overview
-
-
?
additional information
?
-
-
CYP51 participates in biosynthesis of cholesterol
-
-
?
additional information
?
-
the enzyme is a demethylation inhibitor fungicide resistance determinant in Monilinia fructicola field isolates
-
-
?
additional information
?
-
-
the enzyme is a demethylation inhibitor fungicide resistance determinant in Monilinia fructicola field isolates
-
-
?
additional information
?
-
-
involved in fertilization
-
-
?
additional information
?
-
-
the enzyme is involved in follicle-stimulating hormone-induced mouse oocyte maturation and follicle-stimulating hormone-induced oocyte meiotic resumption, regulation, overview. The enzyme is involved in CREB phosphorylation
-
-
?
additional information
?
-
CYP51 is a major checkpoint in membrane sterol biosynthesis, is a key target for fungal antibiotic therapy
-
-
?
additional information
?
-
-
CYP51 is a major checkpoint in membrane sterol biosynthesis, is a key target for fungal antibiotic therapy
-
-
?
additional information
?
-
CYP51 is a major checkpoint in membrane sterol biosynthesis, is a key target for fungal antibiotic therapy
-
-
?
additional information
?
-
CYP51 is one of the key enzymes of sterol biosynthesis in biological kingdoms and is a prime target of antifungal drugs
-
-
?
additional information
?
-
-
CYP51 is one of the key enzymes of sterol biosynthesis in biological kingdoms and is a prime target of antifungal drugs
-
-
?
additional information
?
-
-
enzyme of sterol biosynthesis, sterol 14-demethylation occurs in all organism exhibiting de novo sterol biosynthesis
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
sterol composition of different species isolated from human lung, two distinct sterol compositional phenotypes occur, one, the wild-type, is characterized by DELTA7 C28- and C24 24-alkylsterols with only low proportions of higher molecular mass components, the other type, a mutant with 14alpha-demethylase deficiency, is dominated by high C31 and C32 24-alkylsterols, especially pneumocysterol, NMR sterol analysis, overview
-
-
?
additional information
?
-
-
housekeeping enzyme essential for viability of mammals, essential step in cholesterol biosynthesis
-
-
?
additional information
?
-
-
enzyme of sterol biosynthesis, sterol 14-demethylation occurs in all organism exhibiting de novo sterol biosynthesis
-
-
?
additional information
?
-
-
brain microsomes, existence of sterol biosynthetic pathway in brain, cholesterol is synthesized de novo in brain
-
-
?
additional information
?
-
-
removal of 14alpha-methyl group, C32, from 14alpha-methylated precursor sterols is an essential step of sterol biosynthesis in eukaryotes
-
-
?
additional information
?
-
-
enzyme of cholesterol biosynthesis
-
-
?
additional information
?
-
-
enzyme of cholesterol biosynthesis
-
-
?
additional information
?
-
enzyme of cholesterol biosynthesis
-
-
?
additional information
?
-
-
lanosterol 14-demethylation is situated at the root of sterol-biosynthetic branch of mevalonic acid pathway
-
-
?
additional information
?
-
enzyme for regulation of cholesterol biosynthesis
-
-
?
additional information
?
-
-
there is a possibility that P45014DM participates not only in sterol biogenesis but also in production of biosignal substance regulating meiosis of mammalian oocytes
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
enzyme of sterol biosynthesis, sterol 14-demethylation occurs in all organism exhibiting de novo sterol biosynthesis
-
-
?
additional information
?
-
-
removal of 14alpha-methyl group, C32, from 14alpha-methylated precursor sterols is an essential step of sterol biosynthesis in eukaryotes
-
-
?
additional information
?
-
-
enzyme of ergosterol biosynthesis
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
14alpha-demethylation is a key step of sterol biosynthesis in eukaryotes
-
-
?
additional information
?
-
-
enzyme of sterol biosynthesis, sterol 14-demethylation occurs in all organism exhibiting de novo sterol biosynthesis
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
biosynthetic enzyme with very narrow substrate specificity
-
-
?
additional information
?
-
-
biosynthetic enzyme with very narrow substrate specificity
-
-
?
additional information
?
-
-
enzyme is a multifunctional cytochrome P450, which as the same active site catalyze demethylation in three consecutive NADPH- and O2-dependent hydroxylation reactions, resulting in the elimination of the methyl group as formic acid and the introduction of a double bond at the DELTA14 position
-
-
?
additional information
?
-
-
enzyme is a multifunctional cytochrome P450, which as the same active site catalyze demethylation in three consecutive NADPH- and O2-dependent hydroxylation reactions, resulting in the elimination of the methyl group as formic acid and the introduction of a double bond at the DELTA14 position
-
-
?
additional information
?
-
-
catalyzes an essential step in sterol biosynthesis as evidenced by the absence of a 14alpha-methyl group in all known functional sterols, removal of the 14alpha-methyl group is essential
-
-
?
additional information
?
-
-
key enzyme in plant sterol, phytosterol, biosynthesis
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
enzyme of plant sterol, phytosterol, biosynthesis
-
-
?
additional information
?
-
-
the organism can specifically regulate gene expression, e.g. for the sterol C14-demethylase, in response to derangements in its cellular functions
-
-
?
additional information
?
-
-
enzyme of sterol biosynthesis, sterol 14-demethylation occurs in all organism exhibiting de novo sterol biosynthesis
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
enzyme of plant sterol, phytosterol, biosynthesis
-
-
?
additional information
?
-
-
enzyme of plant sterol, phytosterol, biosynthesis
-
-
?
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(R)-2-(2,4-difluorophenyl)-1,1-difluoro-3-(1H-tetrazol-1-yl)-1-(5-(4-(2,2,2-trifluoroethoxy)phenyl)pyridin-2-yl)propan-2-ol
i.e. oteseconazole, i.e. VT-1161. 98% inhibition, molar ratio of enzyme/inhibitor/lanosterol was 1:2:50
(R)-3-(1H-1,2,4-triazol-1-yl)butyl 2-chlorobenzoate
-
exhibits stronger binding activities than triadimefon but lower binding activities than diniconazole
(R)-3-(1H-1,2,4-triazol-1-yl)butyl 3-chlorobenzoate
-
affinity with purified CYP51 is very low, exhibits lower binding activities than triadimefon and diniconazole
(R)-3-(1H-1,2,4-triazol-1-yl)butyl 4-chlorobenzoate
-
exhibits stronger binding activities than triadimefon but lower binding activities than diniconazole
(R)-3-(1H-1,2,4-triazol-1-yl)butyl 4-methylbenzoate
-
affinity with purified CYP51 is very tight, shows the best binding activities, exhibits stronger binding activities than triadimefon but lower binding activities than diniconazole; no binding affinity with purified CYP51
(R)-3-(1H-1,2,4-triazol-1-yl)butyl benzoate
-
exhibits lower binding activities than triadimefon and diniconazole
(R)-4'-chloro-N-(1-(2,4-dichlorophenyl)-2-(1H-imidazol-1-yl)ethyl)biphenyl-4-carboxamide
VNF, complexes CYP51, binding structure, overview
(R)-N-(1-(2,4-dichlorophenyl)-2-(1H-imidazol-1-yl)ethyl)-4-(5-phenyl-1,3,4-oxadiazol-2-yl)-benzamide
-
(R)-N-(2-(1H-imidazol-1-yl)-1-phenylethyl)-4'-chlorobiphenyl-4-carboxamide
-
(R,S)-3-(1H-1,2,4-triazol-1-yl)butyl 2,4-dichlorobenzoate
-
exhibits binding activities than triadimefon but lower binding activities than diniconazole
(R,S)-3-(1H-1,2,4-triazol-1-yl)butyl 2-chlorobenzoate
-
exhibits lower binding activities than triadimefon and diniconazole
(R,S)-3-(1H-1,2,4-triazol-1-yl)butyl 3-chlorobenzoate
-
exhibits stronger binding activities than triadimefon but lower binding activities than diniconazole
(R,S)-3-(1H-1,2,4-triazol-1-yl)butyl 4-chlorobenzoate
-
exhibits lower binding activities than triadimefon and diniconazole
(R,S)-3-(1H-1,2,4-triazol-1-yl)butyl 4-methylbenzoate
-
affinity with purified CYP51 is very low, exhibits lower binding activities than triadimefon and diniconazole
(R,S)-3-(1H-1,2,4-triazol-1-yl)butyl benzoate
-
exhibits lower binding activities than triadimefon and diniconazole
(S)-3-(1H-1,2,4-triazol-1-yl)butyl 2,4-dichlorobenzoate
-
affinity with purified CYP51 is very tight, exhibits stronger binding activities than triadimefon but lower binding activities than diniconazole
(S)-3-(1H-1,2,4-triazol-1-yl)butyl 2-chlorobenzoate
-
exhibits stronger binding activities than triadimefon but lower binding activities than diniconazole
(S)-3-(1H-1,2,4-triazol-1-yl)butyl 3-chlorobenzoate
-
affinity with purified CYP51 is very tight, exhibits stronger binding activities than triadimefon but lower binding activities than diniconazole
(S)-3-(1H-1,2,4-triazol-1-yl)butyl 4-chlorobenzoate
-
exhibits binding activities than triadimefon but lower binding activities than diniconazole
(S)-3-(1H-1,2,4-triazol-1-yl)butyl benzoate
-
exhibits lower binding activities than triadimefon and diniconazole
(Z)-2,3-dihydro-3-(1H-imidazol-1-yl)-2-(1-butyl)-4H-1-benzopyran-4-one oxime
-
(Z)-trans-2,3-dihydro-3-(1H-imidazol-1-yl)-2-(1-pentyl)-4H-1-benzopyran-4-one oxime
-
1-(1H-1,2,4-triazol-1-yl)-2-(2,4-difluorophenyl)-3-[4-(2-fluoro-4-amino-phenyl)-piperazin-1-yl]-propan-2-ol
1-(1H-1,2,4-triazol-1-yl)-2-(2,4-difluorophenyl)-3-[4-(2-fluoro-4-nitrophenyl)-piperazin-1-yl]-propan-2-ol
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(2,4-dichlorobenzyl)-amino]-2-propanol
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(2-bromobenzyl)-amino]-2-propanol
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(2-chlorobenzyl)-amino]-2-propanol
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(2-fluorobenzyl)-amino]-2-propanol
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(2-methylbenzyl)-amino]-2-propanol
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(3-chlorobenzyl)-amino]-2-propanol
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(3-fluorobenzyl)-amino]-2-propanol
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-bromobenzyl)-amino]-2-propanol
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-chlorobenzyl)-amino]-2-propanol
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-ethylbenzyl)-amino]-2-propanol
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-fluorobenzyl)-amino]-2-propanol
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-methylbenzyl)-amino]-2-propanol
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-nitrobenzyl)-amino]-2-propanol
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-benzyl-amino]-2-propanol
1-(4-methyl-2-(4-(2-methylthiazol-4-yl)phenyl)thiazol-5-yl)ethanone
the compounds is predicted to be a non-competitive inhibitor of the enzyme by molecular docking study
1-(phenethyl(propyl)amino)-3-(pyridin-3-yloxy)propan-2-ol
-
-
1-phenylimidazole
-
heme iron-coordinating inhibitor
11-ketoestrone
type I binding mechanism
14alpha-aminomethyl-lanosterol derivatives
competitive
-
15-hydroxy-lanosterol
-
-
2,2-dimethyl-1,3-dichloropropane
2,4-dichloro-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
2,7-dihydroxy-9-fluorenone
type I binding mechanism
2-(2-(naphthalen-2-yl)ethyl](propyl)amino]-1-(pyridin-3-yl)ethanol dihydrobromide
-
-
2-(2-chlorophenethyl(propyl)amino)-1-(pyridin-4-yl)ethanol dihydrobromide
-
-
2-(3,4-dichlorophenethyl(methyl)amino)-1-(pyridin-3-yl)ethanol dihydrobromide
-
-
2-(3,4-dichlorophenethyl(methyl)amino)-1-(pyridin-4-yl)ethanol dihydrobromide
-
-
2-(3,4-dichlorophenethyl(propyl)amino)-1-(4-methylpyridin-2-yl)ethanol dihydrobromide
-
-
2-(3,4-dichlorophenethyl(propyl)amino)-1-(pyridin-3-yl)ethanol dihydrobromide
-
-
2-(3,4-dichlorophenethyl(propyl)amino)-1-phenylethanol
-
-
2-(3,4-difluorophenethyl(propyl)amino)-1-(pyridin-3-yl)ethanol dihydrobromide
-
-
2-(3,4-dimethoxyphenethyl(propyl)amino)-1-(pyridin-3-yl)ethanol dihydrobromide
-
-
2-(4-chlorophenethyl(propyl)amino)-1-(pyridin-4-yl)ethanol dihydrobromide
-
-
2-(4-nitrophenethyl(propyl)amino)-1-(pyridin-3-yl)ethanol dihydrobromide
-
-
2-(benzo[d]-2,1,3-thiadiazole-4-sulfonyl)-2-amino-2-phenyl-N-(pyridinyl-4)-acetamide
binding structure, overview
2-(methylamino)thiazol-4(5H)-one
-
2-(naphthalen-1-ylamino)thiazol-4(5H)-one
-
2-(phenethyl(propyl)amino)-1-(pyridin-3-yl) ethanol dihydrobromide
-
-
2-(propyl(2-(trifluoromethyl)phenethyl)amino)-1-(pyridin-3-yl)ethanol dihydrobromide
-
-
2-(propyl(4-(trifluoromethyl)phenethyl)amino)-1-(pyridin-3-yl)ethanol dihydrobromide
-
-
2-bromo-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
2-chloro-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
2-decyl-1,2,3,4-tetrahydroisoquinoline-6,7-diol
2-dodecyl-1,2,3,4-tetrahydroisoquinoline-6,7-diol
2-hydroxy-5-(2-(4-(2-methylthiazol-4-yl)phenyl)thiazol-4-yl)benzamide
the compounds is predicted to be a non-competitive inhibitor of the enzyme by molecular docking study
2-methyl-4-(4-(4-(naphthalen-1-yl)thiazol-2-yl)phenyl)-thiazole
the compounds is predicted to be a non-competitive inhibitor of the enzyme by molecular docking study
2-methyl-4-(4-(4-phenylthiazol-2-yl)phenyl)thiazole
the compounds is predicted to be a non-competitive inhibitors of the enzyme by molecular docking study
2-octyl-1,2,3,4-tetrahydroisoquinoline-6,7-diol
2-phenyl-N-pyridin-4-ylbutanamide
-
-
2-[1-[(4-chlorophenyl)carbonyl]-5-methoxy-2-methyl-1H-indol-3-yl]-N-(1-pyridin-4-ylethyl)acetamide
-
-
2-[1-[(4-chlorophenyl)carbonyl]-5-methoxy-2-methyl-1H-indol-3-yl]-N-(2-phenylpropyl)acetamide
-
most potent inhibitor, antiparasitic activities at concentrations less than 0.01 mM
2-[1-[(4-chlorophenyl)carbonyl]-5-methoxy-2-methyl-1H-indol-3-yl]-N-(2-pyridin-3-ylethyl)acetamide
-
-
2-[1-[(4-chlorophenyl)carbonyl]-5-methoxy-2-methyl-1H-indol-3-yl]-N-(pyridin-2-ylmethyl)acetamide
-
-
2-[1-[(4-chlorophenyl)carbonyl]-5-methoxy-2-methyl-1H-indol-3-yl]-N-(pyridin-4-ylmethyl)acetamide
-
-
2-[1-[(4-chlorophenyl)carbonyl]-5-methoxy-2-methyl-1H-indol-3-yl]-N-pyridin-2-ylacetamide
-
-
2-[1-[(4-chlorophenyl)carbonyl]-5-methoxy-2-methyl-1H-indol-3-yl]-N-pyridin-3-ylacetamide
-
-
2-[1-[(4-chlorophenyl)carbonyl]-5-methoxy-2-methyl-1H-indol-3-yl]-N-pyrimidin-2-ylacetamide
-
-
2-[1-[(4-chlorophenyl)carbonyl]-5-methoxy-2-methyl-1H-indol-3-yl]-N-[(6-chloropyridin-3-yl)methyl]acetamide
-
-
2-[1-[(4-chlorophenyl)carbonyl]-5-methoxy-2-methyl-1H-indol-3-yl]-N-[2-(3-chlorophenyl)ethyl]acetamide
-
most potent inhibitor, antiparasitic activities at concentrations less than 0.01 mM
2-[1-[(4-chlorophenyl)carbonyl]-5-methoxy-2-methyl-1H-indol-3-yl]-N-[[6-(trifluoromethyl)pyridin-3-yl]methyl]acetamide
-
-
2-{propyl[2-(pyridin-3-yl)ethyl]amino}-1-(pyridin-3-yl)ethanol
-
-
24-methylene-24,25-dihydrolanosterol
3-(1H-1,2,4-triazol-1-yl)butyl 4-fluorobenzoate
-
-
3-(1H-1,2,4-triazol-1-yl)butyl 4-methoxybenzoate
-
-
3-(2-furyl)-5,6-dihydroimidazo[2,1-b][1,3]thiazole
-
most potent inhibitor
3-(alpha-imidazolylbenzyl)indole
3-(alpha-triazolylbenzyl)indole
3-benzyl-1-pyridin-4-ylpyrrolidine-2,5-dione
-
-
3-bromo-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
3-chloro-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
3-methyl-4-nitro-N-pyridin-4-ylbenzamide
-
-
3-nitrophenyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazol-1-yl)-propyl]-amino)-methyl)-benzoate
3-oxo-N-pyridin-4-yl-3H-benzo[f]chromene-2-carboxamide
-
-
3-thien-2-yl-5,6-dihydroimidazo[2,1-b][1,3]thiazole
-
-
4,4'-dihydroxybenzophenone
binds at the active site via a type I mechanism targeting the flexible region, binding structure and kinetics, overview
4-(2-(2-hydroxy-2-(pyridin-3-yl)ethyl)(propyl)amino)ethylbenzene-1,2-diol dihydrobromide
-
-
4-(2-(4-(2-methylthiazol-4-yl)phenyl)thiazol-4-yl)-benzonitrile
the compounds is predicted to be a non-competitive inhibitor of the enzyme by molecular docking study
4-(4-chlorophenyl)-2-(4-(2-methylthiazol-4-yl)phenyl)-thiazole
the compounds is predicted to be a non-competitive inhibitor of the enzyme by molecular docking study
4-(4-methoxyphenyl)-2-(4-(2-methylthiazol-4-yl)-phenyl)thiazole
the compounds is predicted to be a non-competitive inhibitor of the enzyme by molecular docking study
4-(chloromethyl)-2-(4-(2-methylthiazol-4-yl)phenyl)-thiazole
the compounds is predicted to be a non-competitive inhibitor of the enzyme by molecular docking study
4-(propoxycarbonyl)-phenyl-[4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazol-1-yl)propyl]amino)methyl)]benzoate
4-butyl-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
4-chloro-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
4-chlorophenyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazol-1-yl)-propyl]-amino)-methyl)-benzoate
-
exhibits activity than fluconazole
4-nitrophenyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazol-1-yl)-propyl]-amino)-methyl)-benzoate
4-tert-butyl-N-(4-[4-[2-(2,4-difluorophenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
4-[5-(2,4-difluoro-phenyl)-5-imidazol-1-ylmethyl-tetrahydro-furan-3-yl]-1-isopropyl-butylamine
0.0001 mM, wild-type, 10% residual activity, mutant F145L, 35% residual activity, mutant Y132H, 60% residual activity
4-[5-(2,4-difluoro-phenyl)-5-[1,2,4]triazol-1-ylmethyl-tetrahydro-furan-3-yl]-1-isopropyl-butylamine
0.0001 mM, wild-type, 25% residual activity, mutant F145L, 75% residual activity, mutant Y132H, 75% residual activity
5-(2,4-dichlorobenzylidene)-2-(naphthalen-1-ylamino)thiazol-4(5H)-one
-
5-(4-nitrobenzylidene)-2-(phenylamino)thiazol-4(5H)-one
-
6-[5-(2,4-difluoro-phenyl)-5-imidazol-1-ylmethyl-tetrahydro-furan-3-yl]-2-methyl-hexan-3-one
0.0001 mM, wild-type, no residual activity, mutant F145L, 5% residual activity, mutant Y132H, 25% residual activity
6-[5-(2,4-difluoro-phenyl)-5-[1,2,4]triazol-1-ylmethyl-tetrahydro-furan-3-yl]-2-methyl-hexan-3-one
0.0001 mM, wild-type, no residual activity, mutant F145L, 15% residual activity, mutant Y132H, 55% residual activity
7-chloro-3-[(2R,3R)-3-(2,4-difluorophenyl)-3-hydroxy-4-(1H-1,2,4-triazol-1-yl)butan-2-yl]-4a,8a-dihydroquinazolin-4(3H)-one
-
albaconazole
lower interaction energies with CYP51 than those of voriconazole
alpha-ethyl-N-4-pyridinyl-benzeneacetamide
binds to the non-heme iron, binding structure involving residues H259 and Y76, overview
anti-P-45014DM antibodies
-
complete inhibition
-
azalanstat
specific inhibitor, IC50 less than 0.000002 mM
azole
-
the organism shows reduced azole-sensitivity
azole antifungal agents
-
butyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazole-1-yl)-propyl]-amino)-methyl)-benzoate
clomiphene
interacts with heme, is less potent than azoles
estriol
a substrate analogue
ethyl 2-(2-(4-(2-methylthiazol-4-yl)phenyl)thiazol-4-yl)acetate
the compounds is predicted to be a non-competitive inhibitor of the enzyme by molecular docking study
ethyl 4-methyl-2-(4-(2-methylthiazol-4-yl)phenyl)-thiazole-5-carboxylate
the compounds is predicted to be a non-competitive inhibitor of the enzyme by molecular docking study
ethyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazole-1-yl)-propyl]-amino)-methyl)-benzoate
fluquinconazole
whole-cell antifungal activity of both the R- and S-enantiomers of tebuconazole, prothioconazole, prothioconazole-desthio, and oxo-prothioconazole as well as for fluquinconazole, prochloraz and a racemic mixture of difenoconazole are determined. In vitro binding studies with the affinity purified enzyme are used to show tight type II binding to the yeast enzyme for all compounds tested except prothioconazole and oxo-prothioconazole. Comparison with CYP51 structures from fungal pathogens including Candida albicans, Candida glabrata and Aspergillus fumigatus provides strong evidence for a highly conserved CYP51 structure including the drug binding site
glafenine
interacts with heme, shows no potency which may arise from its hydrophilic nature which lower its up-take and capacity to reach the target enzyme
isobutyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazole-1-yl)-propyl]-amino)-methyl)-benzoate
isopropyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazole-1-yl)-propyl]-amino)-methyl)-benzoate
KG-501
-
the enzyme can be rescued by progesterone
menadione
-
0.125 mM: 62.1% inhibition
methyl-2-[4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazol-1-yl)-propyl]-amino)-methyl)-benzoyloxy]-benzoate
-
exhibits higher activity than fluconazole
methyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazole-1-yl)-propyl]-amino)-methyl)-benzoate
Metyrapone
-
strong inhibition, 0.1 mM: 57.3% inhibition
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-2,4-dimethyl-benzamide
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-2-methoxy-benzamide
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-2-nitro-benzamide
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-3,4,5-trimethoxy-benzamide
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-3,4-dimethoxy-benzamide
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-3,4-dimethyl-benzamide
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-3-methoxy-benzamide
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-3-methyl-benzamide
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-3-trifluoromethyl-benzamide
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-ethyl-benzamide
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-isopropyl-benzamide
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-methoxy-benzamide
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-methyl-benzamide
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-nitro-benzamide
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-pentyl-benzamide
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-propyl-benzamide
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-trifluoromethoxy-benzamide
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluorophenyl)-2-fluoro-benzamide
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluorophenyl)-2-methyl-benzamide
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluorophenyl)-4-fluoro-benzamide
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluorophenyl)-benzamide
N-pyridin-4-yl-9H-xanthene-9-carboxamide
-
strongest binding compound
N-{2-[4-(acetylamino)phenyl]ethyl}-2-[1-(4-chlorobenzoyl)-5-methoxy-2-methyl-1H-indol-3-yl]acetamide
interacts with heme
Nalpha-[(4-methylcyclohexyl)carbonyl]-N-pyridin-4-yltryptophanamide
-
strongest binding compound
nitric oxide
in Huh7 human hepatoma cells, treatment with nitric oxide donors causes rapid post-translational down-regulation of the enzyme
nitrogen
-
nitrogen atmosphere
obtusifoliol
-
24.4% inhibition of 24,25-dihydrolanosterol, DHL, demethylation, no inhibition of lanosterol and 24-methylene-24,25-dihydrolanosterol demethylation
oxo-prothioconazole
whole-cell antifungal activity of both the R- and S-enantiomers of tebuconazole, prothioconazole, prothioconazole-desthio, and oxo-prothioconazole as well as for fluquinconazole, prochloraz and a racemic mixture of difenoconazole are determined. In vitro binding studies with the affinity purified enzyme are used to show tight type II binding to the yeast enzyme for all compounds tested except prothioconazole and oxo-prothioconazole. Comparison with CYP51 structures from fungal pathogens including Candida albicans, Candida glabrata and Aspergillus fumigatus provides strong evidence for a highly conserved CYP51 structure including the drug binding site
pentyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazole-1-yl)-propyl]-amino)-methyl)-benzoate
phenyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazole-1-yl)-propyl]-amino)-methyl)-benzoate
-
exhibits higher activity than fluconazole
prothioconazole-desthio
whole-cell antifungal activity of both the R- and S-enantiomers of tebuconazole, prothioconazole, prothioconazole-desthio, and oxo-prothioconazole as well as for fluquinconazole, prochloraz and a racemic mixture of difenoconazole are determined. In vitro binding studies with the affinity purified enzyme are used to show tight type II binding to the yeast enzyme for all compounds tested except prothioconazole and oxo-prothioconazole. Comparison with CYP51 structures from fungal pathogens including Candida albicans, Candida glabrata and Aspergillus fumigatus provides strong evidence for a highly conserved CYP51 structure including the drug binding site
rottlerin
interacts with heme
RS21607
-
specific inhibition of CYP51, the enzyme can be rescued by progesterone
siRNA
-
administrated single dose of 10 microg CYP51-siRNAs for 48 h results in significantly depletion of CYP51 mRNA in liver of mice fed on normal diet (from 40 to 60%). Exerts inhibition in a dose dependent manner (from 26% in 5 microg to 40% in 20 microg). Most inhibitive effect from day 3 to day 6 (over 50%) after treatment. Six days after administration of 30 microg CYP51-siRNAs (20 microg on day 0 and 10 microg on day 3), CYP51 mRNA and protein levels are significantly knocked down in mice liver. Low-density lipoprotein receptor expression is significantly elevated compared with controls in hepatic cells after CYP51-siRNAs. As a consequence, about 50% of sera low-density lipoprotein cholesterol are significantly reduced. Effect on low-density lipoprotein receptor increase and low-density lipoprotein cholesterol reduction lasts 8 days after a single 20 microg CYP51-siRNAs injection. CYP51-siRNAs can not cause any fatty liver compared with buffer-group and do not interfere with mice ovulation
-
SKF-525A
-
potent inhibitor, 1.0 mM: 100% inhibition
SPSM1
interacts with heme
trans-2,3-dihydro-3-(1H-imidazol-1-yl)-2-(1-heptyl)-4H-1-benzopyran-4-one nitrate
-
trans-2,3-dihydro-3-(1H-imidazol-1-yl)-2-(1-hexyl)-4H-1-benzopyran-4-one nitrate
-
trans-2,3-dihydro-3-(1H-imidazol-1-yl)-2-(1-pentyl)-4H-1-benzopyran-4-one nitrate
-
(2R,4S)-ketoconazole
-
-
1-(1H-1,2,4-triazol-1-yl)-2-(2,4-difluorophenyl)-3-[4-(2-fluoro-4-amino-phenyl)-piperazin-1-yl]-propan-2-ol
-
-
1-(1H-1,2,4-triazol-1-yl)-2-(2,4-difluorophenyl)-3-[4-(2-fluoro-4-amino-phenyl)-piperazin-1-yl]-propan-2-ol
-
-
1-(1H-1,2,4-triazol-1-yl)-2-(2,4-difluorophenyl)-3-[4-(2-fluoro-4-amino-phenyl)-piperazin-1-yl]-propan-2-ol
-
-
1-(1H-1,2,4-triazol-1-yl)-2-(2,4-difluorophenyl)-3-[4-(2-fluoro-4-amino-phenyl)-piperazin-1-yl]-propan-2-ol
-
-
1-(1H-1,2,4-triazol-1-yl)-2-(2,4-difluorophenyl)-3-[4-(2-fluoro-4-amino-phenyl)-piperazin-1-yl]-propan-2-ol
-
-
1-(1H-1,2,4-triazol-1-yl)-2-(2,4-difluorophenyl)-3-[4-(2-fluoro-4-amino-phenyl)-piperazin-1-yl]-propan-2-ol
-
-
1-(1H-1,2,4-triazol-1-yl)-2-(2,4-difluorophenyl)-3-[4-(2-fluoro-4-amino-phenyl)-piperazin-1-yl]-propan-2-ol
-
-
1-(1H-1,2,4-triazol-1-yl)-2-(2,4-difluorophenyl)-3-[4-(2-fluoro-4-amino-phenyl)-piperazin-1-yl]-propan-2-ol
-
-
1-(1H-1,2,4-triazol-1-yl)-2-(2,4-difluorophenyl)-3-[4-(2-fluoro-4-nitrophenyl)-piperazin-1-yl]-propan-2-ol
-
-
1-(1H-1,2,4-triazol-1-yl)-2-(2,4-difluorophenyl)-3-[4-(2-fluoro-4-nitrophenyl)-piperazin-1-yl]-propan-2-ol
-
-
1-(1H-1,2,4-triazol-1-yl)-2-(2,4-difluorophenyl)-3-[4-(2-fluoro-4-nitrophenyl)-piperazin-1-yl]-propan-2-ol
-
-
1-(1H-1,2,4-triazol-1-yl)-2-(2,4-difluorophenyl)-3-[4-(2-fluoro-4-nitrophenyl)-piperazin-1-yl]-propan-2-ol
-
-
1-(1H-1,2,4-triazol-1-yl)-2-(2,4-difluorophenyl)-3-[4-(2-fluoro-4-nitrophenyl)-piperazin-1-yl]-propan-2-ol
-
-
1-(1H-1,2,4-triazol-1-yl)-2-(2,4-difluorophenyl)-3-[4-(2-fluoro-4-nitrophenyl)-piperazin-1-yl]-propan-2-ol
-
-
1-(1H-1,2,4-triazol-1-yl)-2-(2,4-difluorophenyl)-3-[4-(2-fluoro-4-nitrophenyl)-piperazin-1-yl]-propan-2-ol
-
-
1-(1H-1,2,4-triazol-1-yl)-2-(2,4-difluorophenyl)-3-[4-(2-fluoro-4-nitrophenyl)-piperazin-1-yl]-propan-2-ol
-
-
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(2,4-dichlorobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(2,4-dichlorobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(2,4-dichlorobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(2,4-dichlorobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(2-bromobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(2-bromobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(2-bromobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(2-bromobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(2-bromobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(2-bromobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(2-bromobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(2-chlorobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(2-chlorobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(2-chlorobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(2-chlorobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(2-chlorobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(2-chlorobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(2-chlorobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(2-fluorobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(2-fluorobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(2-fluorobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(2-fluorobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(2-fluorobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(2-fluorobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(2-fluorobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(2-methylbenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(2-methylbenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(2-methylbenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(2-methylbenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(2-methylbenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(2-methylbenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(2-methylbenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(3-chlorobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(3-chlorobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(3-chlorobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(3-chlorobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(3-chlorobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(3-chlorobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(3-chlorobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(3-fluorobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(3-fluorobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(3-fluorobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(3-fluorobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(3-fluorobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(3-fluorobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(3-fluorobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-bromobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-bromobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-bromobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-bromobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-bromobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-bromobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-bromobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-chlorobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-chlorobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-chlorobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-chlorobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-chlorobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-chlorobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-chlorobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-ethylbenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-ethylbenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-ethylbenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-ethylbenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-ethylbenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-ethylbenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-fluorobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-fluorobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-fluorobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-fluorobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-fluorobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-fluorobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-fluorobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-methylbenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-methylbenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-methylbenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-methylbenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-methylbenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-methylbenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-methylbenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-nitrobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-nitrobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-nitrobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-nitrobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-nitrobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-nitrobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-nitrobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-benzyl-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-benzyl-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-benzyl-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-benzyl-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-benzyl-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-benzyl-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-benzyl-amino]-2-propanol
-
exhibits higher activity than fluconazole
14alpha-amino-lanosterol
-
-
14alpha-amino-lanosterol
-
-
2,2-dimethyl-1,3-dichloropropane
i.e.D0870
2,2-dimethyl-1,3-dichloropropane
-
i.e.D0870
2,2-dimethyl-1,3-dichloropropane
-
i.e.D0870
2,4-dichloro-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
2,4-dichloro-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
2,4-dichloro-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
2,4-dichloro-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
2,4-dichloro-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
2,4-dichloro-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
2,4-dichloro-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
2,4-dichloro-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
2-bromo-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
2-bromo-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
2-bromo-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
2-bromo-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
2-bromo-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
2-bromo-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
2-bromo-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
2-bromo-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
2-chloro-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
2-chloro-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
2-chloro-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
2-chloro-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
2-chloro-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
2-chloro-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
2-chloro-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
2-chloro-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
2-decyl-1,2,3,4-tetrahydroisoquinoline-6,7-diol
-
-
2-decyl-1,2,3,4-tetrahydroisoquinoline-6,7-diol
-
-
2-decyl-1,2,3,4-tetrahydroisoquinoline-6,7-diol
-
-
2-decyl-1,2,3,4-tetrahydroisoquinoline-6,7-diol
-
-
2-decyl-1,2,3,4-tetrahydroisoquinoline-6,7-diol
-
-
2-decyl-1,2,3,4-tetrahydroisoquinoline-6,7-diol
-
-
2-dodecyl-1,2,3,4-tetrahydroisoquinoline-6,7-diol
-
-
2-dodecyl-1,2,3,4-tetrahydroisoquinoline-6,7-diol
-
-
2-dodecyl-1,2,3,4-tetrahydroisoquinoline-6,7-diol
-
-
2-dodecyl-1,2,3,4-tetrahydroisoquinoline-6,7-diol
-
-
2-dodecyl-1,2,3,4-tetrahydroisoquinoline-6,7-diol
-
-
2-dodecyl-1,2,3,4-tetrahydroisoquinoline-6,7-diol
-
-
2-octyl-1,2,3,4-tetrahydroisoquinoline-6,7-diol
-
-
2-octyl-1,2,3,4-tetrahydroisoquinoline-6,7-diol
-
-
2-octyl-1,2,3,4-tetrahydroisoquinoline-6,7-diol
-
-
2-octyl-1,2,3,4-tetrahydroisoquinoline-6,7-diol
-
-
2-octyl-1,2,3,4-tetrahydroisoquinoline-6,7-diol
-
-
2-octyl-1,2,3,4-tetrahydroisoquinoline-6,7-diol
-
-
2-phenylimidazole
-
Kd-value 9.1 mM, comparison of affinity and binding to human and Mycobacterium tuberculosis enzyme
2-phenylimidazole
Kd-value 2.1 mM, comparison of affinity and binding to human and Mycobacterium tuberculosis enzyme
24,25-dihydrolanosterol
-
8.3% inhibition of 24-methylene-24,25-dihydrolanosterol demethylation, no inhibition of lanosterol demethylation
24,25-dihydrolanosterol
-
16.4% inhibition of obtusifoliol 14alpha-demethylation
24-methylene-24,25-dihydrolanosterol
-
21.6% inhibition of lanosterol demethylation, 55.3% inhibition of 24,25-dihydrolanosterol demethylation
24-methylene-24,25-dihydrolanosterol
-
47.4% inhibition of obtusifoliol 14alpha-demethylation
3-(alpha-imidazolylbenzyl)indole
-
3-(alpha-imidazolylbenzyl)indole
-
-
3-(alpha-imidazolylbenzyl)indole
-
-
3-(alpha-triazolylbenzyl)indole
-
3-(alpha-triazolylbenzyl)indole
-
-
3-(alpha-triazolylbenzyl)indole
-
-
3-bromo-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
3-bromo-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
3-bromo-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
3-bromo-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
3-bromo-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
3-bromo-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
3-bromo-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
3-bromo-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
3-chloro-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
3-chloro-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
3-chloro-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
3-chloro-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
3-chloro-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
3-chloro-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
3-chloro-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
3-chloro-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
3-nitrophenyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazol-1-yl)-propyl]-amino)-methyl)-benzoate
-
exhibits higher activity than fluconazole
3-nitrophenyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazol-1-yl)-propyl]-amino)-methyl)-benzoate
-
-
4-(propoxycarbonyl)-phenyl-[4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazol-1-yl)propyl]amino)methyl)]benzoate
-
exhibits higher activity than fluconazole
4-(propoxycarbonyl)-phenyl-[4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazol-1-yl)propyl]amino)methyl)]benzoate
-
-
4-butyl-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
4-butyl-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
4-butyl-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
4-butyl-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
4-butyl-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
4-butyl-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
4-butyl-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
4-butyl-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
4-chloro-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
4-chloro-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
4-chloro-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
4-chloro-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
4-chloro-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
4-chloro-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
4-chloro-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
4-chloro-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
4-nitrophenyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazol-1-yl)-propyl]-amino)-methyl)-benzoate
-
exhibits higher activity than fluconazole
4-nitrophenyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazol-1-yl)-propyl]-amino)-methyl)-benzoate
-
exhibits activity than fluconazole
4-nitrophenyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazol-1-yl)-propyl]-amino)-methyl)-benzoate
-
exhibits higher activity than fluconazole
4-phenylimidazole
-
Kd-value 0.19 mM, comparison of affinity and binding to human and Mycobacterium tuberculosis enzyme
4-phenylimidazole
Kd-value 0.29 mM, comparison of affinity and binding to human and Mycobacterium tuberculosis enzyme
4-phenylimidazole
-
heme iron-coordinating inhibitor
4-tert-butyl-N-(4-[4-[2-(2,4-difluorophenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
4-tert-butyl-N-(4-[4-[2-(2,4-difluorophenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
4-tert-butyl-N-(4-[4-[2-(2,4-difluorophenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
4-tert-butyl-N-(4-[4-[2-(2,4-difluorophenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
4-tert-butyl-N-(4-[4-[2-(2,4-difluorophenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
4-tert-butyl-N-(4-[4-[2-(2,4-difluorophenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
4-tert-butyl-N-(4-[4-[2-(2,4-difluorophenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
4-tert-butyl-N-(4-[4-[2-(2,4-difluorophenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
Amphotericin B
-
-
azole antifungal agents
-
specific inhibitors
-
azole antifungal agents
-
specific inhibitors
-
azole antifungal agents
-
specific inhibitors
-
bifonazole
-
IC50: 300 nM
bifonazole
-
IC50: 0.0008 mM
bitertanol
-
IC50: 59 nM
bitertanol
-
IC50: 0.0013 mM
butyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazole-1-yl)-propyl]-amino)-methyl)-benzoate
-
exhibits higher activity than fluconazole
butyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazole-1-yl)-propyl]-amino)-methyl)-benzoate
-
exhibits higher activity than fluconazole
butyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazole-1-yl)-propyl]-amino)-methyl)-benzoate
-
exhibits higher activity than fluconazole
clotrimazole
-
IC50: 91 nM
clotrimazole
78% inhibition, molar ratio of enzyme/inhibitor/lanosterol was 1:2:50
clotrimazole
-
IC50: 0.0009 mM
CO
-
high partial pressure of CO, ratio CO:O2 of 95:5 causes 48% inhibition
CO
-
ratio CO:O2 of 90:10, 51.1% inhibition, ratio CO:O2 of 95:5, 100% inhibition
cyproconazole
-
IC50: 100 nM
cyproconazole
-
IC50: 0.0228 mM
difenoconazole
whole-cell antifungal activity of both the R- and S-enantiomers of tebuconazole, prothioconazole, prothioconazole-desthio, and oxo-prothioconazole as well as for fluquinconazole, prochloraz and a racemic mixture of difenoconazole are determined. In vitro binding studies with the affinity purified enzyme are used to show tight type II binding to the yeast enzyme for all compounds tested except prothioconazole and oxo-prothioconazole. Comparison with CYP51 structures from fungal pathogens including Candida albicans, Candida glabrata and Aspergillus fumigatus provides strong evidence for a highly conserved CYP51 structure including the drug binding site
difenoconazole
-
an azole inhibitor
diniconazole
homology modeling and docking model
diniconazole
-
is the most sensitive fungicide for CYP51, has a stronger affinity for CYP51 than the other fungicides
econazole
-
epoxiconazole
-
IC50: 220 nM
epoxiconazole
-
IC50: 0.0020 mM
ethyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazole-1-yl)-propyl]-amino)-methyl)-benzoate
-
exhibits higher activity than fluconazole
ethyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazole-1-yl)-propyl]-amino)-methyl)-benzoate
-
-
ethyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazole-1-yl)-propyl]-amino)-methyl)-benzoate
-
exhibits activity than fluconazole
ethyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazole-1-yl)-propyl]-amino)-methyl)-benzoate
-
exhibits higher activity than fluconazole
ethyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazole-1-yl)-propyl]-amino)-methyl)-benzoate
-
exhibits higher activity than fluconazole
fadrozole
-
IC50: 0.0322 mM, above
fadrozole
-
IC50: 0.10 mM, above
fluconazole
-
-
fluconazole
-
IC50: 51 nM, above
fluconazole
-
binds to the active site of CYP51 via coordination of the N atom of the triazole nucleus with iron of the heme group
fluconazole
54% inhibition, molar ratio of enzyme/inhibitor/lanosterol was 1:2:50
fluconazole
N136Y transformants show a reduced in vitro susceptibility to fluconazole compared to wild-type controls. The amino acid substitution N136Y in Candida albicans sterol 14alpha-demethylase is involved in fluconazole resistance
fluconazole
-
binds to the active site of CYP51 via coordination of the N atom of the triazole nucleus with iron of the heme group
fluconazole
-
binds to the active site of CYP51 via coordination of the N atom of the triazole nucleus with iron of the heme group
fluconazole
is bound to the active site of CYP51 through the formation of a coordination bond with the iron of the heme group (the P1 subsite). The difluorophenyl group of fluconazole points toward substrate access channel 1 (the BC loop) and forms a hydrophobic interaction with Met153 and the alkyl group of Lys157 (the P3 subsite). Another triazolyl ring of fluconazole attached to C-3 has a preferable orientation toward substrate access channel 2 (the FG loop) and forms indirect nonbonding interactions with the surrounding residues, lined with Leu134, Phe240, Met316, Ile386, and Ile529 (the P4 subsite). The hydroxyl group attached to C-2 is important for antifungal activity, but no interaction between this hydroxyl group and the active site of CYP51
fluconazole
-
binds to the active site of CYP51 via coordination of the N atom of the triazole nucleus with iron of the heme group
fluconazole
-
Kd-value 0.12 mM, comparison of affinity and binding to human and Mycobacterium tuberculosis enzyme
fluconazole
-
IC50: 0.030 mM, above
fluconazole
the inhibitor not only replaces the substrate in the enzyme active site but most likely displaces the CO from the iron coordination sphere
fluconazole
Kd-value 0.02 mM, comparison of affinity and binding to human and Mycobacterium tuberculosis enzyme
fluconazole
a clinical drug
fluconazole
-
binds to the active site of CYP51 via coordination of the N atom of the triazole nucleus with iron of the heme group
fluconazole
-
binds to the active site of CYP51 via coordination of the N atom of the triazole nucleus with iron of the heme group
fluconazole
-
binds to the active site of CYP51 via coordination of the N atom of the triazole nucleus with iron of the heme group
fluconazole
and analogues
fluconazole
complexes CYP51, binding structure, overview
flusilazole
-
IC50: 85 nM
flusilazole
-
IC50: 0.0034 mM
hexaconazole
-
IC50: 66 nM
hexaconazole
-
IC50: 0.0156 mM
imazalil
-
IC50: 82 nM
imazalil
-
IC50: 0.0361 mM
imidazole inhibitors
-
-
-
imidazole inhibitors
-
-
-
imidazole inhibitors
-
-
-
imidazole inhibitors
-
-
-
imidazole inhibitors
-
-
-
imidazole inhibitors
-
-
-
imidazole inhibitors
-
-
-
imidazole inhibitors
-
-
-
imidazole inhibitors
-
-
-
imidazole inhibitors
-
-
-
imidazole inhibitors
-
-
-
imidazoles
-
-
-
isobutyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazole-1-yl)-propyl]-amino)-methyl)-benzoate
-
exhibits higher activity than fluconazole
isobutyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazole-1-yl)-propyl]-amino)-methyl)-benzoate
-
exhibits higher activity than fluconazole
isobutyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazole-1-yl)-propyl]-amino)-methyl)-benzoate
-
exhibits higher activity than fluconazole
isobutyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazole-1-yl)-propyl]-amino)-methyl)-benzoate
-
exhibits higher activity than fluconazole
isopropyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazole-1-yl)-propyl]-amino)-methyl)-benzoate
-
exhibits higher activity than fluconazole
isopropyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazole-1-yl)-propyl]-amino)-methyl)-benzoate
-
exhibits higher activity than fluconazole
isopropyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazole-1-yl)-propyl]-amino)-methyl)-benzoate
-
exhibits higher activity than fluconazole
isopropyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazole-1-yl)-propyl]-amino)-methyl)-benzoate
-
exhibits higher activity than fluconazole
itraconazole
-
-
itraconazole
-
IC50: 39 nM
itraconazole
91% inhibition, molar ratio of enzyme/inhibitor/lanosterol was 1:2:50
itraconazole
lowest interaction energies with CYP51
itraconazole
-
IC50: 0.030 mM
itraconazole
a fungicide that targets CYP51 and as an inhibitor causes the accumulation of lanosterol and reduced ergosterol biosynthesis in fungi, also induces AcCYP51 expression after 24 h of treatment
itraconzole
-
-
ketoconazole
-
-
ketoconazole
-
IC50: 64 nM
ketoconazole
85% inhibition, molar ratio of enzyme/inhibitor/lanosterol was 1:2:50
ketoconazole
-
Kd-value 0.008 mM, comparison of affinity and binding to human and Mycobacterium tuberculosis enzyme
ketoconazole
-
IC50: 0.0004 mM
ketoconazole
Kd-value 0.019 mM, comparison of affinity and binding to human and Mycobacterium tuberculosis enzyme
ketoconazole
residues lining the ketoconazole pocket include Ala397 and Ala398, Arg389 and Arg393, Asp377, Glu308, Gly390, Ile401, Leu311 and Leu315, Lys312, Phe387, Pro386, Trp382 and Trp384
ketoconazole
-
potent inhibitor, 0.015 mM: complete inhibition
lanosterol
-
63% inhibition of 24-methylene-24,25-dihydrolanosterol demethylation, 74.9% inhibition of 24,25-dihydrolanosterol demethylation
lanosterol
-
53.1% inhibition of obtusifoliol 14alpha-demethylation
letrozole
-
IC50: 0.0133 mM, above
letrozole
-
IC50: 0.10 mM, above
meglumine antimoniate
-
meglumine antimoniate
-
-
meglumine antimoniate
-
-
methyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazole-1-yl)-propyl]-amino)-methyl)-benzoate
-
exhibits higher activity than fluconazole
methyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazole-1-yl)-propyl]-amino)-methyl)-benzoate
-
exhibits higher activity than fluconazole
methyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazole-1-yl)-propyl]-amino)-methyl)-benzoate
-
-
methyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazole-1-yl)-propyl]-amino)-methyl)-benzoate
-
exhibits higher activity than fluconazole
methyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazole-1-yl)-propyl]-amino)-methyl)-benzoate
-
exhibits higher activity than fluconazole
methyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazole-1-yl)-propyl]-amino)-methyl)-benzoate
-
exhibits higher activity than fluconazole
methyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazole-1-yl)-propyl]-amino)-methyl)-benzoate
-
exhibits higher activity than fluconazole
miconazole
-
IC50: 72 nM
miconazole
79% inhibition, molar ratio of enzyme/inhibitor/lanosterol was 1:2:50
miconazole
-
IC50: 0.00006 mM
myclobutanil
-
IC50: 140 nM
myclobutanil
-
IC50: 0.0290 mM
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-2,4-dimethyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-2,4-dimethyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-2,4-dimethyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-2,4-dimethyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-2,4-dimethyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-2,4-dimethyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-2,4-dimethyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-2,4-dimethyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-2-methoxy-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-2-methoxy-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-2-methoxy-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-2-methoxy-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-2-methoxy-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-2-methoxy-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-2-methoxy-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-2-methoxy-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-2-nitro-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-2-nitro-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-2-nitro-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-2-nitro-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-2-nitro-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-2-nitro-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-2-nitro-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-2-nitro-benzamide
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-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-3,4,5-trimethoxy-benzamide
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-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-3,4,5-trimethoxy-benzamide
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-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-3,4,5-trimethoxy-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-3,4,5-trimethoxy-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-3,4,5-trimethoxy-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-3,4,5-trimethoxy-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-3,4,5-trimethoxy-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-3,4,5-trimethoxy-benzamide
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-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-3,4-dimethoxy-benzamide
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-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-3,4-dimethoxy-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-3,4-dimethoxy-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-3,4-dimethoxy-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-3,4-dimethoxy-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-3,4-dimethoxy-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-3,4-dimethoxy-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-3,4-dimethoxy-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-3,4-dimethyl-benzamide
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-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-3,4-dimethyl-benzamide
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-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-3,4-dimethyl-benzamide
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-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-3,4-dimethyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-3,4-dimethyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-3,4-dimethyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-3,4-dimethyl-benzamide
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-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-3,4-dimethyl-benzamide
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-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-3-methoxy-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-3-methoxy-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-3-methoxy-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-3-methoxy-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-3-methoxy-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-3-methoxy-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-3-methoxy-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-3-methoxy-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-3-methyl-benzamide
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-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-3-methyl-benzamide
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-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-3-methyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-3-methyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-3-methyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-3-methyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-3-methyl-benzamide
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-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-3-methyl-benzamide
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-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-3-trifluoromethyl-benzamide
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-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-3-trifluoromethyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-3-trifluoromethyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-3-trifluoromethyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-3-trifluoromethyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-3-trifluoromethyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-3-trifluoromethyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-3-trifluoromethyl-benzamide
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-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-ethyl-benzamide
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-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-ethyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-ethyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-ethyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-ethyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-ethyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-ethyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-ethyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-isopropyl-benzamide
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-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-isopropyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-isopropyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-isopropyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-isopropyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-isopropyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-isopropyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-isopropyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-methoxy-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-methoxy-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-methoxy-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-methoxy-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-methoxy-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-methoxy-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-methoxy-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-methoxy-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-methyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-methyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-methyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-methyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-methyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-methyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-methyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-methyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-nitro-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-nitro-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-nitro-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-nitro-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-nitro-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-nitro-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-nitro-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-nitro-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-pentyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-pentyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-pentyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-pentyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-pentyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-pentyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-pentyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-pentyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-propyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-propyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-propyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-propyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-propyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-propyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-propyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-propyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-trifluoromethoxy-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-trifluoromethoxy-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-trifluoromethoxy-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-trifluoromethoxy-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-trifluoromethoxy-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-trifluoromethoxy-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-trifluoromethoxy-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-trifluoromethoxy-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluorophenyl)-2-fluoro-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluorophenyl)-2-fluoro-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluorophenyl)-2-fluoro-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluorophenyl)-2-fluoro-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluorophenyl)-2-fluoro-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluorophenyl)-2-fluoro-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluorophenyl)-2-fluoro-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluorophenyl)-2-fluoro-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluorophenyl)-2-methyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluorophenyl)-2-methyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluorophenyl)-2-methyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluorophenyl)-2-methyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluorophenyl)-2-methyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluorophenyl)-2-methyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluorophenyl)-2-methyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluorophenyl)-2-methyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluorophenyl)-4-fluoro-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluorophenyl)-4-fluoro-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluorophenyl)-4-fluoro-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluorophenyl)-4-fluoro-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluorophenyl)-4-fluoro-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluorophenyl)-4-fluoro-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluorophenyl)-4-fluoro-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluorophenyl)-4-fluoro-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluorophenyl)-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluorophenyl)-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluorophenyl)-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluorophenyl)-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluorophenyl)-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluorophenyl)-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluorophenyl)-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluorophenyl)-benzamide
-
-
penconazole
-
IC50: 76 nM
penconazole
-
IC50: 0.0193 mM
pentyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazole-1-yl)-propyl]-amino)-methyl)-benzoate
-
exhibits higher activity than fluconazole
pentyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazole-1-yl)-propyl]-amino)-methyl)-benzoate
-
exhibits higher activity than fluconazole
posaconazole
-
-
posaconazole
98% inhibition, molar ratio of enzyme/inhibitor/lanosterol was 1:2:50
posaconazole
lowest interaction energies with CYP51
posaconazole
complexes CYP51, binding structure, overview
Prochloraz
-
IC50: 98 nM
Prochloraz
-
IC50: 0.0050 mM
Prochloraz
whole-cell antifungal activity of both the R- and S-enantiomers of tebuconazole, prothioconazole, prothioconazole-desthio, and oxo-prothioconazole as well as for fluquinconazole, prochloraz and a racemic mixture of difenoconazole are determined. In vitro binding studies with the affinity purified enzyme are used to show tight type II binding to the yeast enzyme for all compounds tested except prothioconazole and oxo-prothioconazole. Comparison with CYP51 structures from fungal pathogens including Candida albicans, Candida glabrata and Aspergillus fumigatus provides strong evidence for a highly conserved CYP51 structure including the drug binding site
Propiconazole
-
-
Propiconazole
-
IC50: 150 nM
Propiconazole
-
IC50: 0.0083 mM
prothioconazole
whole-cell antifungal activity of both the R- and S-enantiomers of tebuconazole, prothioconazole, prothioconazole-desthio, and oxo-prothioconazole as well as for fluquinconazole, prochloraz and a racemic mixture of difenoconazole are determined. In vitro binding studies with the affinity purified enzyme are used to show tight type II binding to the yeast enzyme for all compounds tested except prothioconazole and oxo-prothioconazole. Comparison with CYP51 structures from fungal pathogens including Candida albicans, Candida glabrata and Aspergillus fumigatus provides strong evidence for a highly conserved CYP51 structure including the drug binding site
ravuconazole
-
-
ravuconazole
thiazole ring interacts with the side chain of Tyr131, Leu134, and Ile389. Besides the hydrophobic interaction with Phe240, Met528, and Ile529, the 4-cyano-phenyl group of ravuconazole can also form a pi-pi stacking interaction with His133
tebuconazole
-
IC50: 350 nM
tebuconazole
-
IC50: 0.0036 mM
tebuconazole
whole-cell antifungal activity of both the R- and S-enantiomers of tebuconazole, prothioconazole, prothioconazole-desthio, and oxo-prothioconazole as well as for fluquinconazole, prochloraz and a racemic mixture of difenoconazole are determined. In vitro binding studies with the affinity purified enzyme are used to show tight type II binding to the yeast enzyme for all compounds tested except prothioconazole and oxo-prothioconazole. Comparison with CYP51 structures from fungal pathogens including Candida albicans, Candida glabrata and Aspergillus fumigatus provides strong evidence for a highly conserved CYP51 structure including the drug binding site
tebuconazole
-
an azole inhibitor
terbinafine
-
-
triadimefon
-
IC50: 130 nM
triadimefon
-
IC50: 0.010 mM
triadimefon
-
is the less sensitive fungicide for CYP51, affinity for CYP51 is the weakest
triadimenol
-
-
triadimenol
-
IC50: 330 nM
triadimenol
-
IC50: 0.0372 mM
triadimenol
-
hydrophobicity of triadimenol is reduced by the shortening of the carbon chain and the addition of a polar oxygen atom in comparison with tebuconazole, which may be the cause of the decrease in the affinity of triadimenol compared with tebuconazole
triazole
-
-
triazole
-
sensitive and resistant variants of CYP51A1, mutations lead to alterations in the enzyme as drug target, primary determinants of triazole resistance, overview
triazole inhibitors
-
-
-
triazole inhibitors
-
-
-
triazole inhibitors
-
-
-
triazole inhibitors
-
-
-
triazole inhibitors
-
-
-
triazole inhibitors
-
-
-
triazole inhibitors
-
-
-
triazole inhibitors
-
-
-
triazole inhibitors
-
-
-
triazole inhibitors
-
-
-
triazole inhibitors
-
-
-
triazoles
-
-
-
voriconazole
-
-
voriconazole
84% inhibition, molar ratio of enzyme/inhibitor/lanosterol was 1:2:50
voriconazole
shows higher affinity with CYP51 than fluconazole
voriconazole
displays the greatest specificity
voriconazole
-
displays the greatest specificity
additional information
-
in vivo inhibition study with different strains, overview
-
additional information
-
design of non-azole antifungal lead compounds based on the constructed three-dimensional model of CYP51by coupling structure-based de novo design, overview
-
additional information
-
inhibitory potency, antifungal activity in vivo, and structure-function analysis of 1-(1H-1,2,4-triazol-1-yl)-2-(2,4-difluorophenyl)-3-[(4-substituted phenyl)-piperazin-1-yl]-propan-2-ol derivatives, overview
-
additional information
-
is not inhibited by fluconazole, amphotericin B, 1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-benzyl-amino]-2-propanol, 1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(2-fluorobenzyl)-amino]-2-propanol, 1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(3-fluorobenzyl)-amino]-2-propanol, 1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-fluorobenzyl)-amino]-2-propanol, 1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(2-chlorobenzyl)-amino]-2-propanol, 1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(3-chlorobenzyl)-amino]-2-propanol, 1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-chlorobenzyl)-amino]-2-propanol, 1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(2-bromobenzyl)-amino]-2-propanol, 1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-bromobenzyl)-amino]-2-propanol, 1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(2-methylbenzyl)-amino]-2-propanol, 1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-methylbenzyl)-amino]-2-propanol, 1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-nitrobenzyl)-amino]-2-propanol, 1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-ethylbenzyl)-amino]-2-propanol, 1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(2,4-dichlorobenzyl)-amino]-2-propanol, methyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazole-1-yl)-propyl]-amino)-methyl)-benzoate, ethyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazole-1-yl)-propyl]-amino)-methyl)-benzoate, isopropyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazole-1-yl)-propyl]-amino)-methyl)-benzoate, isopropyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazole-1-yl)-propyl]-amino)-methyl)-benzoate, isobutyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazole-1-yl)-propyl]-amino)-methyl)-benzoate, pentyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazole-1-yl)-propyl]-amino)-methyl)-benzoate, phenyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazole-1-yl)-propyl]-amino)-methyl)-benzoate, 3-nitrophenyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazol-1-yl)-propyl]-amino)-methyl)-benzoate, 4-nitrophenyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazol-1-yl)-propyl]-amino)-methyl)-benzoate, 4-chlorophenyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazol-1-yl)-propyl]-amino)-methyl)-benzoate, methyl-2-[4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazol-1-yl)-propyl]-amino)-methyl)-benzoyloxy]-benzoate or 4-(propoxycarbonyl)-phenyl-[4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazol-1-yl)propyl]amino)methyl)]benzoate
-
additional information
-
the enzyme is highly resistant to triadimenol
-
additional information
-
design of non-azole antifungal lead compounds based on the constructed three-dimensional model of CYP51by coupling structure-based de novo design, overview
-
additional information
-
inhibitory potency, antifungal activity in vivo, and structure-function analysis of 1-(1H-1,2,4-triazol-1-yl)-2-(2,4-difluorophenyl)-3-[(4-substituted phenyl)-piperazin-1-yl]-propan-2-ol derivatives, overview
-
additional information
-
inhibitory potency of fungicides, antifungal drugs, and cytostatic drugs, overview
-
additional information
-
yeast cells are more sensitive to azole drugs than mammalian cells, yeast cells have lower P450 enzyme content and a higher IC50 value
-
additional information
-
inhibition of CYP51 involves a coordination bond with iron of the heme group, the hydrophilic H-bonding region, the hydrophobic region, and the narrow hydrophobic cleft
-
additional information
the enzyme constitutes an important biological target for the most popular class of antifungals. Inhibition of lanosterol 14alpha-demethylase leads to accumulation of 14-a-methylsterols on the fungal surface and alteration of the permeability and rigidity of the plasma membrane, which results in arrest of fungal growth. Because this enzyme is found in all eukaryotes (including humans) and because the azoles interact also with other cytochrome P450 dependent enzymes (CYP3A4), a selective inhibition towards the fungal CYP51A1 is essential for an increased therapeutic index
-
additional information
-
design of non-azole antifungal lead compounds based on the constructed three-dimensional model of CYP51by coupling structure-based de novo design, overview
-
additional information
-
inhibitory potency, antifungal activity in vivo, and structure-function analysis of 1-(1H-1,2,4-triazol-1-yl)-2-(2,4-difluorophenyl)-3-[(4-substituted phenyl)-piperazin-1-yl]-propan-2-ol derivatives, overview
-
additional information
-
inhibition of CYP51 involves a coordination bond with iron of the heme group, the hydrophilic H-bonding region, the hydrophobic region, and the narrow hydrophobic cleft
-
additional information
-
inhibitory potency, antifungal activity in vivo, and structure-function analysis of 1-(1H-1,2,4-triazol-1-yl)-2-(2,4-difluorophenyl)-3-[(4-substituted phenyl)-piperazin-1-yl]-propan-2-ol derivatives, overview
-
additional information
-
inhibition of CYP51 involves a coordination bond with iron of the heme group, the hydrophilic H-bonding region, the hydrophobic region, and the narrow hydrophobic cleft
-
additional information
-
design of non-azole antifungal lead compounds based on the constructed three-dimensional model of CYP51by coupling structure-based de novo design, overview
-
additional information
-
inhibitory potency, antifungal activity in vivo, and structure-function analysis of 1-(1H-1,2,4-triazol-1-yl)-2-(2,4-difluorophenyl)-3-[(4-substituted phenyl)-piperazin-1-yl]-propan-2-ol derivatives, overview
-
additional information
-
inhibition of CYP51 involves a coordination bond with iron of the heme group, the hydrophilic H-bonding region, the hydrophobic region, and the narrow hydrophobic cleft
-
additional information
-
inhibitory potency, antifungal activity in vivo, and structure-function analysis of 1-(1H-1,2,4-triazol-1-yl)-2-(2,4-difluorophenyl)-3-[(4-substituted phenyl)-piperazin-1-yl]-propan-2-ol derivatives, overview
-
additional information
-
14alpha-carboaldehyde reaction intermediates are effective in competitive enzyme inhibition and as hypocholesterolemic agents
-
additional information
-
inhibitory potency of fungicides, antifungal drugs, and cytostatic drugs, overview
-
additional information
-
structureactivity relationship study of enzyme-ligand binding, pyridine binds within the heme binding pocket in an analogy with azoles, overview
-
additional information
-
azole antifungals have higher IC50 values against the human CYP51 than against that of Candida albicans by a factor of ca. 30
-
additional information
humanized yeast strain as compared to the parental yeast strain shows up to 1000fold reduced susceptibility to the orally active azole drugs and reduced effectiveness for the topical drugs
-
additional information
-
humanized yeast strain as compared to the parental yeast strain shows up to 1000fold reduced susceptibility to the orally active azole drugs and reduced effectiveness for the topical drugs
-
additional information
-
design of non-azole antifungal lead compounds based on the constructed three-dimensional model of CYP51by coupling structure-based de novo design, overview
-
additional information
specific inhibitor screening
-
additional information
-
specific inhibitor screening
-
additional information
the aromatic moieties of drugs where aligning to phenylalanine and tyrosine residues that lines the hydrophobic part of the binding pocket which is itself generally hydrophobic
-
additional information
-
development of a simple, highly sensitive and accurate method for screening of sterol 14alpha-demethylase inhibitors, overview
-
additional information
-
inhibitory potency, antifungal activity in vivo, and structure-function analysis of 1-(1H-1,2,4-triazol-1-yl)-2-(2,4-difluorophenyl)-3-[(4-substituted phenyl)-piperazin-1-yl]-propan-2-ol derivatives, overview
-
additional information
-
inhibition of CYP51 involves a coordination bond with iron of the heme group, the hydrophilic H-bonding region, the hydrophobic region, and the narrow hydrophobic cleft
-
additional information
-
Oculimacula acuformis is intrinsically resistant to triazoles and sensitive to imidazoles
-
additional information
-
inhibition of CYP51 involves a coordination bond with iron of the heme group, the hydrophilic H-bonding region, the hydrophobic region, and the narrow hydrophobic cleft
-
additional information
-
affinity of the azoles for CYP51 is positively correlated with their hydrophobicity. Amino acid residues Tyr112, Phe120, Phe220, His308 and Phe497 of CYP51, forming a large hydrophobic cavity, are the key residues interacting with azole fungicides
-
additional information
-
no inhibition by 24,28-dihydroobtusifoliol
-
additional information
-
the parental yeast strain as compared to humanized yeast strain shows up to 1000fold higher susceptibility to the orally active azole drugs
-
additional information
-
design of non-azole antifungal lead compounds based on the constructed three-dimensional model of CYP51by coupling structure-based de novo design, overview
-
additional information
-
inhibitory potency, antifungal activity in vivo, and structure-function analysis of 1-(1H-1,2,4-triazol-1-yl)-2-(2,4-difluorophenyl)-3-[(4-substituted phenyl)-piperazin-1-yl]-propan-2-ol derivatives, overview
-
additional information
inhibition kinetics and mechanism
-
additional information
-
inhibition kinetics and mechanism
-
additional information
-
EC50 values, structure-function relationship of enzyme and inhibitor interactions, overview
-
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Bak, S.; Kahn, R.A.; Olsen, C.E.; Halkier, B.A.
Cloning and expression in Escherichia coli of the obtusifoliol 14alpha-demethylase of Sorghum bicolor (L.) Moench, a cytochrome P450 orthologous to the sterol 14alpha-demethylases (CYP51) from fungi and mammals
Plant J.
11
191-201
1997
Arabidopsis thaliana, Saccharomyces cerevisiae, Candida albicans, [Candida] glabrata, Candida tropicalis, Homo sapiens, Manihot esculenta, no activity in Escherichia coli, Penicillium italicum, Rattus norvegicus, Schizosaccharomyces pombe, Sinapis alba, Sorghum bicolor, Ustilago maydis, Zea mays, Sinapis alba L.
brenda
Aoyama, Y.; Yoshida, Y.
Different substrate specificities of lanosterol 14alpha-demethylase (P-45014DM) of Saccharomyces cerevisiae and rat liver for 24-methylene-24,25-dihydrolanosterol and 24,25-dihydrolanosterol
Biochem. Biophys. Res. Commun.
178
1064-1071
1991
Rattus norvegicus, Saccharomyces cerevisiae
brenda
Aoyama, Y.; Yoshida, Y.
The 4beta-methyl group of substrate does not affect the activity of lanosterol 14alpha-demethylase (P-45014DM) of yeast: Difference between the substrate recognition by yeast and plant sterol 14alpha-demethylases
Biochem. Biophys. Res. Commun.
183
1266-1272
1992
Saccharomyces cerevisiae, Embryophyta
brenda
Aoyama, Y.; Yoshida, Y.; Sonoda, Y.; Sato, Y.
Role of the 8-double bond of lanosterol in the enzyme-substrate interaction of cytochrome P-45014DM (lanosterol 14alpha-demethylase)
Biochim. Biophys. Acta
1001
196-200
1989
Saccharomyces cerevisiae
brenda
Aoyama, Y.; Funae, Y.; Noshiro, M.; Horiuchi, T.; Yoshida, Y.
Occurrence of a P450 showing high homology to yeast lanosterol 14-demethylase (P45014DM) in the rat liver
Biochem. Biophys. Res. Commun.
201
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Mycobacterium tuberculosis
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Saccharomyces cerevisiae, Candida albicans, Homo sapiens, Methylococcus capsulatus, Mycobacterium tuberculosis, Mycolicibacterium smegmatis, Rattus norvegicus, Sorghum bicolor, Trypanosoma brucei, Trypanosoma cruzi, Ustilago maydis
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Zhu, J.; Lu, J.; Zhou, Y.; Li, Y.; Cheng, J.; Zheng, C.
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Aspergillus fumigatus, Candida albicans, Candida parapsilosis, Cryptococcus neoformans, Trichophyton rubrum, Microsporum canis
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Cloning of chicken lanosterol 14alpha-demethylase (CYP51) cDNA: discovery of a testis-specific CYP51 transcript
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Gallus gallus (Q0KKP4), Gallus gallus (Q0KKP5)
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Fink, M.; Acimovic, J.; Rezen, T.; Tansek, N.; Rozman, D.
Cholesterogenic lanosterol 14alpha-demethylase (CYP51) is an immediate early response gene
Endocrinology
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Homo sapiens
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Synthesis of novel triazole derivatives as inhibitors of cytochrome P450 14alpha-demethylase (CYP51)
Eur. J. Med. Chem.
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Aspergillus fumigatus, Candida albicans, Candida parapsilosis, Candida tropicalis, Cryptococcus neoformans, Nannizzia gypsea, Trichophyton rubrum, Fonsecaea compacta
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Lepesheva, G.I.; Zaitseva, N.G.; Nes, W.D.; Zhou, W.; Arase, M.; Liu, J.; Hill, G.C.; Waterman, M.R.
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Trypanosoma cruzi
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Lipid signaling in plants. Cloning and expression analysis of the obtusifoliol 14alpha-demethylase from Solanum chacoense Bitt., a pollination- and fertilization-induced gene with both obtusifoliol and lanosterol demethylase activity
Plant Physiol.
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Solanum chacoense (Q673E9), Solanum chacoense
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Troesken, E.R.; Adamska, M.; Arand, M.; Zarn, J.A.; Patten, C.; Voelkel, W.; Lutz, W.K.
Comparison of lanosterol-14 alpha-demethylase (CYP51) of human and Candida albicans for inhibition by different antifungal azoles
Toxicology
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Candida albicans, Homo sapiens
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Podust, L.M.; von Kries, J.P.; Eddine, A.N.; Kim, Y.; Yermalitskaya, L.V.; Kuehne, R.; Ouellet, H.; Warrier, T.; Altekoester, M.; Lee, J.S.; Rademann, J.; Oschkinat, H.; Kaufmann, S.H.; Waterman, M.R.
Small-molecule scaffolds for CYP51 inhibitors identified by high-throughput screening and defined by X-ray crystallography
Antimicrob. Agents Chemother.
51
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Mycobacterium tuberculosis (P9WPP9), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WPP9)
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Luo, C.X.; Schnabel, G.
The cytochrome P450 lanosterol 14alpha-demethylase gene is a demethylation inhibitor fungicide resistance determinant in Monilinia fructicola field isolates from Georgia
Appl. Environ. Microbiol.
74
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Monilinia fructicola (A7LM25), Monilinia fructicola
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Seliskar, M.; Kosir, R.; Rozman, D.
Expression of microsomal lanosterol 14alpha-demethylase (CYP51) in an engineered soluble monomeric form
Biochem. Biophys. Res. Commun.
371
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Bos taurus (Q4PJW3), Bos taurus
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Shumyantseva, V.V.; Bulko, T.V.; Kuznetsova, G.P.; Lisitsa, A.V.; Ponomarenko, E.A.; Karuzina, I.I.; Archakov, A.I.
Electrochemical reduction of sterol-14alpha-demethylase from Mycobacterium tuberculosis (CYP51b1)
Biochemistry (Moscow)
72
658-663
2007
Mycobacterium tuberculosis
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Chen, S.H.; Sheng, C.Q.; Xu, X.H.; Jiang, Y.Y.; Zhang, W.N.; He, C.
Identification of Y118 amino acid residue in Candida albicans sterol 14alpha-demethylase associated with the enzyme activity and selective antifungal activity of azole analogues
Biol. Pharm. Bull.
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Candida albicans
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Korosec, T.; Acimovic, J.; Seliskar, M.; Kocjan, D.; Tacer, K.F.; Rozman, D.; Urleb, U.
Novel cholesterol biosynthesis inhibitors targeting human lanosterol 14alpha-demethylase (CYP51)
Bioorg. Med. Chem.
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Homo sapiens
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Zhao, L.; Liu, D.; Zhang, Q.; Zhang, S.; Wan, J.; Xiao, W.
Expression and homology modeling of sterol 14alpha-demethylase from Penicillium digitatum
FEMS Microbiol. Lett.
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Penicillium digitatum (A1XG20), Penicillium digitatum
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Eddine, A.N.; von Kries, J.P.; Podust, M.V.; Warrier, T.; Kaufmann, S.H.; Podust, L.M.
X-ray structure of 4,4-dihydroxybenzophenone mimicking sterol substrate in the active site of sterol 14alpha-demethylase (CYP51)
J. Biol. Chem.
283
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2008
Mycobacterium tuberculosis (P9WPP9), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WPP9)
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Ning, G.; Ouyang, H.; Wang, S.; Chen, X.; Xu, B.; Yang, J.; Zhang, H.; Zhang, M.; Xia, G.
3,5-cyclic adenosine monophosphate response element binding protein up-regulated cytochrome P450 lanosterol 14alpha-demethylase expression involved in follicle-stimulating hormone-induced mouse oocyte maturation
Mol. Endocrinol.
22
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2008
Mus musculus
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Fraaije, B.A.; Cools, H.J.; Kim, S.; Motteram, J.; Clark, W.S.; Lucas, J.A.
A novel substitution 1381V in the sterol 14alpha-demethylase (CYP51) of Mycosphaerella graminicola is differentially selected by azole fungicides
Mol. Plant Pathol.
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Zymoseptoria tritici
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Buckner, F.S.
Sterol 14-demethylase inhibitors for Trypanosoma cruzi infections
Adv. Exp. Med. Biol.
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Candida albicans, Homo sapiens, Mycobacterium tuberculosis, Trypanosoma brucei, Trypanosoma cruzi (Q7Z1V1), Trypanosoma cruzi
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Maurice, H.; Tuarira, E.; Mwambete, K.
Virtual high screening throughput and design of 14alpha-lanosterol demethylase inhibitors against Mycobacterium tuberculosis
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Mycobacterium tuberculosis (P9WPP9), Mycobacterium tuberculosis H37Rv (P9WPP9)
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Parker, J.E.; Merkamm, M.; Manning, N.J.; Pompon, D.; Kelly, S.L.; Kelly, D.E.
Differential azole antifungal efficacies contrasted using a Saccharomyces cerevisiae strain humanized for sterol 14 alpha-demethylase at the homologous locus
Antimicrob. Agents Chemother.
52
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2008
Saccharomyces cerevisiae, Homo sapiens (Q16850), Homo sapiens, Saccharomyces cerevisiae BY4741
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Sheng, C.; Miao, Z.; Ji, H.; Yao, J.; Wang, W.; Che, X.; Dong, G.; Lue, J.; Guo, W.; Zhang, W.
Three-dimensional model of lanosterol 14 alpha-demethylase from Cryptococcus neoformans: active-site characterization and insights into azole binding
Antimicrob. Agents Chemother.
53
3487-3495
2009
Cryptococcus neoformans (Q870D1), Cryptococcus neoformans
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Xu, B.; Wang, C.; Yang, J.; Mao, G.; Zhang, C.; Liu, D.; Tai, P.; Zhou, B.; Xia, G.; Zhang, M.
Silencing of mouse hepatic lanosterol 14-alpha demethylase down-regulated plasma low-density lipoprotein cholesterol levels by short-term treatment of siRNA
Biol. Pharm. Bull.
31
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2008
Mus musculus
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Kitahama, Y.; Nakamura, M.; Yoshida, Y.; Aoyama, Y.
The construction and characterization of self-sufficient lanosterol 14-demethylase fusion proteins consisting of yeast CYP51 and its reductase
Biol. Pharm. Bull.
32
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Saccharomyces cerevisiae (P10614), Saccharomyces cerevisiae
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Ming, Z.H.; Xu, S.Z.; Zhou, L.; Ding, M.W.; Yang, J.Y.; Yang, S.; Xiao, W.J.
Organocatalytic synthesis and sterol 14alpha-demethylase binding interactions of enantioriched 3-(1H-1,2,4-triazol-1-yl)butyl benzoates
Bioorg. Med. Chem. Lett.
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2009
Penicillium digitatum
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Chai, X.; Zhang, J.; Hu, H.; Yu, S.; Sun, Q.; Dan, Z.; Jiang, Y.; Wu, Q.
Design, synthesis, and biological evaluation of novel triazole derivatives as inhibitors of cytochrome P450 14alpha-demethylase
Eur. J. Med. Chem.
44
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2009
Aspergillus fumigatus, Candida albicans, Pichia kudriavzevii, Candida parapsilosis, Candida tropicalis, Cryptococcus neoformans, Nannizzia gypsea, Trichophyton rubrum, Candida albicans ATCC 7661
brenda
Krishnan-Natesan, S.; Chandrasekar, P.H.; Alangaden, G.J.; Manavathu, E.K.
Molecular characterisation of cyp51A and cyp51B genes coding for P450 14alpha-lanosterol demethylases A (CYP51Ap) and B (CYP51Bp) from voriconazole-resistant laboratory isolates of Aspergillus flavus
Int. J. Antimicrob. Agents
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2008
Aspergillus flavus
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Konkle, M.E.; Hargrove, T.Y.; Kleshchenko, Y.Y.; von Kries, J.P.; Ridenour, W.; Uddin, M.J.; Caprioli, R.M.; Marnett, L.J.; Nes, W.D.; Villalta, F.; Waterman, M.R.; Lepesheva, G.I.
Indomethacin amides as a novel molecular scaffold for targeting Trypanosoma cruzi sterol 14alpha-demethylase
J. Med. Chem.
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2009
Trypanosoma cruzi
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Sen, K.; Hackett, J.C.
Molecular oxygen activation and proton transfer mechanisms in lanosterol 14alpha-demethylase catalysis
J. Phys. Chem. B
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2009
Mycobacterium tuberculosis (P9WPP9), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WPP9)
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Warrilow, A.; Ugochukwu, C.; Lamb, D.; Kelly, D.; Kelly, S.
Expression and characterization of CYP51, the ancient sterol 14-demethylase activity for cytochromes P450 (CYP), in the white-rot fungus Phanerochaete chrysosporium
Lipids
43
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2008
Phanerodontia chrysosporium (Q68HC3), Phanerodontia chrysosporium
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Yang, J.; Zhang, Q.; Liao, M.; Xiao, M.; Xiao, W.; Yang, S.; Wan, J.
Expression and homology modelling of sterol 14alpha-demethylase of Magnaporthe grisea and its interaction with azoles
Pest Manag. Sci.
65
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2009
Pyricularia grisea
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Song, X.; Tai, P.; Yan, J.; Xu, B.; Chen, X.; Ouyang, H.; Zhang, M.; Xia, G.
Expression and regulation of lanosterol 14alpha-demethylase in mouse embryo and uterus during the peri-implantation period
Reprod. Fertil. Dev.
20
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2008
Mus musculus
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Warrilow, A.G.; Melo, N.; Martel, C.M.; Parker, J.E.; Nes, W.D.; Kelly, S.L.; Kelly, D.E.
Expression, purification, and characterization of Aspergillus fumigatus sterol 14-alpha demethylase (CYP51) isoenzymes A and B
Antimicrob. Agents Chemother.
54
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Aspergillus fumigatus, Aspergillus fumigatus Af293
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Martel, C.M.; Parker, J.E.; Warrilow, A.G.; Rolley, N.J.; Kelly, S.L.; Kelly, D.E.
Complementation of a Saccharomyces cerevisiae ERG11/CYP51 (sterol 14alpha-demethylase) doxycycline-regulated mutant and screening of the azole sensitivity of Aspergillus fumigatus isoenzymes CYP51A and CYP51B
Antimicrob. Agents Chemother.
54
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2010
Aspergillus fumigatus
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Cools, H.J.; Parker, J.E.; Kelly, D.E.; Lucas, J.A.; Fraaije, B.A.; Kelly, S.L.
Heterologous expression of mutated eburicol 14alpha-demethylase (CYP51) proteins of Mycosphaerella graminicola to assess effects on azole fungicide sensitivity and intrinsic protein function
Appl. Environ. Microbiol.
76
2866-2872
2010
Zymoseptoria tritici, Zymoseptoria tritici IPO323
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Petushkova, N.; Lisitsa, A.; Pozdnev, V.; Karuzina, I.
A fluorometric method for determination of catalytic activity of CYP51b1 (sterol 14alpha-demethylase) with coumarin derivatives
Biochemistry (Moscow) Suppl. B
4
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2010
Mycobacterium tuberculosis
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Lee, C.H.; Hsu, K.H.; Wang, S.Y.; Chang, T.T.; Chu, F.H.; Shaw, J.F.
Cloning and characterization of the lanosterol 14alpha-demethylase gene from Antrodia cinnamomea
J. Agric. Food Chem.
58
4800-4807
2010
Taiwanofungus camphoratus (A8DBU6), Taiwanofungus camphoratus, Taiwanofungus camphoratus TFRIB 470 (A8DBU6)
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Lepesheva, G.I.; Hargrove, T.Y.; Anderson, S.; Kleshchenko, Y.; Furtak, V.; Wawrzak, Z.; Villalta, F.; Waterman, M.R.
Structural insights into inhibition of sterol 14alpha-demethylase in the human pathogen Trypanosoma cruzi
J. Biol. Chem.
285
25582-25590
2010
Trypanosoma cruzi (Q7Z1V1), Trypanosoma cruzi
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Cools, H.J.; Mullins, J.G.; Fraaije, B.A.; Parker, J.E.; Kelly, D.E.; Lucas, J.A.; Kelly, S.L.
Impact of recently emerged sterol 14alpha-demethylase (CYP51) variants of Mycosphaerella graminicola on azole fungicide sensitivity
Appl. Environ. Microbiol.
77
3830-3837
2011
Zymoseptoria tritici
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Park, H.G.; Lee, I.S.; Chun, Y.J.; Yun, C.H.; Johnston, J.B.; Montellano, P.R.; Kim, D.
Heterologous expression and characterization of the sterol 14alpha-demethylase CYP51F1 from Candida albicans
Arch. Biochem. Biophys.
509
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2011
Candida albicans (P10613), Candida albicans, Candida albicans ATCC MYA-2876 (P10613)
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Mukha, D.V.; Feranchuk, S.I.; Gilep, A.A.; Usanov, S.A.
Molecular modeling of human lanosterol 14alpha-demethylase complexes with substrates and their derivatives
Biochemistry
76
175-185
2011
Homo sapiens (Q16850), Homo sapiens
brenda
Yan, X.; Ma, W.; Li, Y.; Wang, H.; Que, Y.; Ma, Z.; Talbot, N.; Wang, Z.
A sterol 14alph-demethylase is required for conidiation, virulence and for mediating sensitivity to sterol demethylation inhibitors by the rice blast fungus Magnaporthe oryzae
Fungal Genet. Biol.
48
144-153
2011
Pyricularia oryzae, Pyricularia oryzae Guy11
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Hargrove, T.Y.; Wawrzak, Z.; Liu, J.; Nes, W.D.; Waterman, M.R.; Lepesheva, G.I.
Substrate preferences and catalytic parameters determined by structural characteristics of sterol 14alpha-demethylase (CYP51) from Leishmania infantum
J. Biol. Chem.
286
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2011
Leishmania infantum (A2TEF2), Leishmania infantum
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Emami, S.; Banipoulad, T.; Irannejad, H.; Foroumadi, A.; Falahati, M.; Ashrafi-Khozani, M.; Sharifynia, S.
Imidazolylchromanones containing alkyl side chain as lanosterol 14alpha-demethylase inhibitors: synthesis, antifungal activity and docking study
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29
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2014
Mycobacterium tuberculosis (P9WPP9), Mycobacterium tuberculosis H37Rv (P9WPP9)
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Alvarez-Rueda, N.; Fleury, A.; Morio, F.; Pagniez, F.; Gastinel, L.; Le Pape, P.
Amino acid substitutions at the major insertion loop of Candida albicans sterol 14alpha-demethylase are involved in fluconazole resistance
PLoS ONE
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2011
Candida albicans
brenda
Park, J.W.; Byrd, A.; Lee, C.M.; Morgan, E.T.
Nitric oxide stimulates cellular degradation of human CYP51A1, the highly conserved lanosterol 14alpha-demethylase
Biochem. J.
474
3241-3252
2017
Homo sapiens (Q16850), Homo sapiens
brenda
Morrison, A.; Goldstone, J.; Lamb, D.; Kubota, A.; Lemaire, B.; Stegeman, J.
Identification, modeling and ligand affinity of early deuterostome CYP51s, and functional characterization of recombinant zebrafish sterol 14alpha-demethylase
Biochim. Biophys. Acta
1840
1825-1836
2014
Danio rerio
brenda
Emami, S.; Tavangar, P.; Keighobadi, M.
An overview of azoles targeting sterol 14?-demethylase for antileishmanial therapy
Eur. J. Med. Chem.
135
241-259
2017
Leishmania major, Leishmania mexicana, Leishmania infantum (A2TEF2)
brenda
Borcea, A.; Marc, G.; Pirnau, A.; Vlase, L.; Ionut, I.; Tiperciuc, B.; Oniga, O.
Synthesis and molecular docking study of some new 1,4-phenylene-bisthiazoles as fungal lanosterol 14alpha-demethylase inhibitors
Farmacia
65
683-689
2017
Candida albicans SC5314 (P10613)
-
brenda
Stana, A.; Vodnar, D.C.; Tamaian, R.; Pirn?u, A.; Vlase, L.; Ionu?, I.; Oniga, O.; Tiperciuc, B.
Design, synthesis and antifungal activity evaluation of new thiazolin-4-ones as potential lanosterol 14alpha-demethylase inhibitors
Int. J. Mol. Sci.
18
E177
2017
Candida albicans SC5314 (P10613)
brenda
Hargrove, T.Y.; Friggeri, L.; Wawrzak, Z.; Qi, A.; Hoekstra, W.J.; Schotzinger, R.J.; York, J.D.; Guengerich, F.P.; Lepesheva, G.I.
Structural analyses of Candida albicans sterol 14alpha-demethylase complexed with azole drugs address the molecular basis of azole-mediated inhibition of fungal sterol biosynthesis
J. Biol. Chem.
292
6728-6743
2017
Candida albicans (Q9P4W0), Candida albicans
brenda
Friggeri, L.; Hargrove, T.Y.; Rachakonda, G.; Williams, A.D.; Wawrzak, Z.; Di Santo, R.; De Vita, D.; Waterman, M.R.; Tortorella, S.; Villalta, F.; Lepesheva, G.I.
Structural basis for rational design of inhibitors targeting Trypanosoma cruzi sterol 14alpha-demethylase two regions of the enzyme molecule potentiate its inhibition
J. Med. Chem.
57
6704-6717
2014
Trypanosoma cruzi (Q7Z1V1), Trypanosoma cruzi, Trypanosoma cruzi CL Brener (Q7Z1V1)
brenda
Alvarez-Rueda, N.; Fleury, A.; Loge, C.; Pagniez, F.; Robert, E.; Morio, F.; Le Pape, P.
The amino acid substitution N136Y in Candida albicans sterol 14alpha-demethylase is involved in fluconazole resistance
Med. Mycol.
54
764-775
2016
Candida albicans (C8XRD8), Candida albicans
brenda
Tyndall, J.D.; Sabherwal, M.; Sagatova, A.A.; Keniya, M.V.; Negroni, J.; Wilson, R.K.; Woods, M.A.; Tietjen, K.; Monk, B.C.
Structural and functional elucidation of yeast lanosterol 14alpha-demethylase in complex with agrochemical antifungals
PLoS ONE
11
e0167485
2016
Saccharomyces cerevisiae (A6ZSR0), Saccharomyces cerevisiae, Saccharomyces cerevisiae YJM789 (A6ZSR0)
brenda
Warrilow, A.G.; Price, C.L.; Parker, J.E.; Rolley, N.J.; Smyrniotis, C.J.; Hughes, D.D.; Thoss, V.; Nes, W.D.; Kelly, D.E.; Holman, T.R.; Kelly, S.L.
Azole antifungal sensitivity of sterol 14alpha-demethylase (CYP51) and CYP5218 from Malassezia globosa
Sci. Rep.
6
27690
2016
Malassezia globosa (A8Q3I7), Malassezia globosa, Malassezia globosa CBS 7966 (A8Q3I7)
brenda