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1-hydroxy-2-naphthoate + NADH + 2 H+ + O2
?
-
137% of the activity with salicylate
-
-
?
1-hydroxy-2-naphthoate + NADH + H+ + O2
?
1-hydroxy-2-naphthoate + NADH + O2
1,2-dihydroxynaphthalene + CO2 + H2O + NAD+
-
-
-
-
?
2,3-dihydroxybenzoate + NADH + 2 H+ + O2
pyrogallol + NAD+ + H2O + CO2
2,3-dihydroxybenzoate + NADH + O2
pyrogallol + CO2 + H2O + NAD+
2,4,6,8,10,12-hexanitro-2,4,6,8,10,12-hexaazaisowurzitane + NADH
NO2- + N2O + formate + NH4+
-
the enzyme catalyzes two oxygen-sensitive single-electron transfer steps necessary to release two nitrite ions from 2,4,6,8,10,12-hexanitro-2,4,6,8,10,12-hexaazaisowurzitane and this is followed by the secondary decomposition of this energetic chemical
N2O is abiotically produced from NO2-NH2
-
?
2,4-dihydroxybenzoate + NAD(P)H + O2
benzene-1,2,4-triol + CO2 + H2O + NAD(P)+
-
-
-
?
2,4-dihydroxybenzoate + NADH + 2 H+ + O2
1,2,4-trihydroxybenzene + NAD+ + H2O + CO2
-
91% of the activity with salicylate
-
-
?
2,4-dihydroxybenzoate + NADPH + H+ + O2
benzene-1,2,4-triol + NAD+ + H2O + CO2
-
-
-
-
r
2,5-dihydroxybenzoate + NADH + O2
benzene-1,2,5-triol + CO2 + H2O + NAD+
2,5-dihydroxybenzoic acid + NADH + H+ + O2
2,5-dihydroxyphenol + NAD+ + H2O + CO2
146% activity compared to salicylate
-
-
?
2,6-dihydroxybenzoate + NADH + 2 H+ + O2
1,2,3-trihydroxybenzene + NAD+ + H2O + CO2
-
70% of the activity with salicylate
-
-
?
2,6-dihydroxybenzoate + NADH + O2
pyrogallol + CO2 + H2O + NAD+
2-hydroxy-1-naphthoate + NADH + 2 H+ + O2
?
-
160% of the activity with salicylate
-
-
?
3,5-dinitrosalicylate + NADH + O2
? + NAD+ + H2O + CO2
3-aminosalicylate + NADH + H+ + O2
3-aminobenzene-1,2-diol + NAD+ + H2O + CO2
3-chlorosalicylate + NADH + H+ + O2
3-chlorobenzene-1,2-diol + NAD+ + H2O + CO2
3-chlorosalicylate + NADH + H+ + O2
3-chlorocatechol + NAD+ + H2O + CO2
-
-
-
?
3-methylsalicylate + NADH + 2 H+ + O2
3-methylcatechol + NAD+ + H2O + CO2
3-methylsalicylate + NADH + H+ + O2
3-methylbenzene-1,2-diol + NAD+ + H2O + CO2
3-methylsalicylate + NADH + H+ + O2
3-methylcatechol + NAD+ + H2O + CO2
-
-
-
?
3-methylsalicylate + NADH + O2
1,2-dihydroxy-3-methylbenzene + CO2 + NAD+ + H2O
3-methylsalicylate + NADH + O2
1,2-dihydroxy-3-methylbenzene + NAD+ + H2O + CO2
4-(3-benzothiazol-2-yl-4-cyano-2-oxo-2H-chromen-7-yloxymethyl)-2-hydroxy-benzoic acid + O2 + NADH + 2 H+
?
-
i.e. SHLF, two-step synthesis of a long-wavelength latent fluorogenic substrate SHLF. In the presence of NADH and under aerobic conditions, SHL catalyzes the decarboxylative hydroxylation of SHLF followed by a quinonemethide-type rearrangement reaction concomitant with the ejection of a fluorescence coumarin 2, which is spontaneous and irreversible at physiological temperatures in aqueous media. The fluorescence signal generated by this process is specific and, in the near red spectral region with an emission maximum at 595 nm, is suppressed by salicylic acid
-
-
?
4-aminosalicylate + NADH + 2 H+ + O2
4-aminocatechol + NAD+ + H2O + CO2
4-aminosalicylate + NADH + H+ + O2
4-aminobenzene-1,2-diol + NAD+ + H2O + CO2
4-aminosalicylate + NADH + O2
4-aminocatechol + CO2 + NAD+ + H2O
4-chlorosalicylate + NADH + H+ + O2
4-chlorobenzene-1,2-diol + NAD+ + H2O + CO2
4-chlorosalicylate + NADH + H+ + O2
4-chlorocatechol + NAD+ + H2O + CO2
-
-
-
?
4-chlorosalicylate + NADH + O2
1,2-dihydroxy-4-chlorobenzene + CO2 + NAD+ + H2O
4-chlorosalicylate + NADH + O2
4-chlorocatechol + NAD+ + H2O + CO2
-
-
-
-
?
4-methylsalicylate + NADH + 2 H+ + O2
4-methylcatechol + NAD+ + H2O + CO2
4-methylsalicylate + NADH + H+ + O2
4-methylbenzene-1,2-diol + NAD+ + H2O + CO2
4-methylsalicylate + NADH + O2
1,2-dihydroxy-4-methylbenzene + CO2 + NAD+ + H2O
-
-
-
-
?
5-aminosalicylate + NADH + 2 H+ + O2
5-aminocatechol + NAD+ + H2O + CO2
5-aminosalicylate + NADH + H+ + O2
5-aminobenzene-1,2-diol + NAD+ + H2O + CO2
5-aminosalicylate + NADH + O2
5-aminocatechol + CO2 + NAD+ + H2O
-
-
-
-
?
5-chlorosalicylate + NADH + 2 H+ + O2
4-chlorocatechol + NAD+ + H2O + CO2
-
46% of the activity with salicylate
-
-
?
5-chlorosalicylate + NADH + H+ + O2
5-chlorobenzene-1,2-diol + NAD+ + H2O + CO2
5-chlorosalicylate + NADH + H+ + O2
5-chlorocatechol + NAD+ + H2O + CO2
-
-
-
?
5-chlorosalicylate + NADH + O2
1,2-dihydroxy-5-chlorobenzene + CO2 + NAD+ + H2O
5-chlorosalicylate + NADH + O2
1,2-dihydroxy-5-chlorobenzene + NAD+ + H2O + CO2
5-fluorosalicylate + NADH + O2
1,2-dihydroxy-5-fluorobenzene + CO2 + NAD+ + H2O
-
-
-
-
?
5-hydroxysalicylate + NADH + H+ + O2
2,5-dihydroxyphenol + NAD+ + H2O + CO2
5-methoxysalicylate + NADH + O2
1,2-dihydroxy-5-methoxybenzene + CO2 + NAD+ + H2O
-
-
-
-
?
5-methylsalicylate + NADH + 2 H+ + O2
4-methylcatechol + NAD+ + H2O + CO2
-
68.5% of the activity with salicylate
-
-
?
5-methylsalicylate + NADH + 2 H+ + O2
5-methylcatechol + NAD+ + H2O + CO2
5-methylsalicylate + NADH + H+ + O2
1,2-dihydroxy-5-methylbenzene + CO2 + NAD+ + H2O
5-methylsalicylate + NADH + H+ + O2
4-methylbenzene-1,2-diol + NAD+ + H2O + CO2
5-nitrosalicylate + NADH + 2 H+ + O2
4-nitrocatechol + NAD+ + H2O + CO2
-
32% of the activity with salicylate
-
-
?
anthranilate + NADH + 2 H+ + O2
2-aminophenol + NAD+ + H2O + CO2
-
67% of the activity with salicylate
-
-
?
aspirin + NADH + O2
? + NAD+ + H2O + CO2
-
-
-
-
?
gentisate + NADH + 2 H+ + O2
?
-
99% of the activity with salicylate
-
-
?
gentisate + NADH + 2 H+ + O2
hydroxyquinol + NAD+ + H2O + CO2
-
93% activity compared to salicylate
-
-
?
m-hydroxybenzoate + NADH + O2
1,3-dihydroxybenzene + CO2 + NAD+ + H2O
-
6% of the reaction with salicylate
-
-
?
o-iodophenol + NADH + O2
catechol + iodide + NAD+
-
-
-
-
?
o-nitrophenol + NADH + O2
catechol + nitrite + NAD+
p-aminosalicylate + NADH + O2
1,2-dihydroxy-4-aminobenzene + NAD+ + CO2 + H2O
salicylaldehyde + NADH + O2
catechol + formate + NAD+
-
mechanism
-
-
?
salicylate + NADH + 2 H+ + O2
catechol + NAD+ + H2O + CO2
salicylate + NADH + H+ + O2
catechol + NAD+ + H2O + CO2
salicylate + O2 + NADH + 2 H+
catechol + CO2 + H2O + NAD+
salicylate + O2 + NADPH + 2 H+
catechol + CO2 + H2O + NADP+
sulfosalicylate + NADH + O2
? + NAD+ + H2O + CO2
-
-
-
-
?
additional information
?
-
1-hydroxy-2-naphthoate + NADH + H+ + O2
?
-
25% activity compared to salicylate
-
-
?
1-hydroxy-2-naphthoate + NADH + H+ + O2
?
-
25% activity compared to salicylate
-
-
?
1-hydroxy-2-naphthoate + NADH + H+ + O2
?
-
83% activity compared to salicylate
-
-
?
1-hydroxy-2-naphthoate + NADH + H+ + O2
?
-
83% activity compared to salicylate
-
-
?
2,3-dihydroxybenzoate + NADH + 2 H+ + O2
pyrogallol + NAD+ + H2O + CO2
-
82% activity compared to salicylate
-
-
?
2,3-dihydroxybenzoate + NADH + 2 H+ + O2
pyrogallol + NAD+ + H2O + CO2
-
82% activity compared to salicylate
-
-
?
2,3-dihydroxybenzoate + NADH + O2
pyrogallol + CO2 + H2O + NAD+
-
-
-
?
2,3-dihydroxybenzoate + NADH + O2
pyrogallol + CO2 + H2O + NAD+
-
-
-
-
?
2,3-dihydroxybenzoate + NADH + O2
pyrogallol + CO2 + H2O + NAD+
-
-
-
-
?
2,3-dihydroxybenzoate + NADH + O2
pyrogallol + CO2 + H2O + NAD+
-
-
-
?
2,3-dihydroxybenzoate + NADH + O2
pyrogallol + CO2 + H2O + NAD+
-
-
-
-
?
2,5-dihydroxybenzoate + NADH + O2
benzene-1,2,5-triol + CO2 + H2O + NAD+
-
or NADPH
-
?
2,5-dihydroxybenzoate + NADH + O2
benzene-1,2,5-triol + CO2 + H2O + NAD+
-
-
-
-
?
2,5-dihydroxybenzoate + NADH + O2
benzene-1,2,5-triol + CO2 + H2O + NAD+
-
-
-
-
?
2,5-dihydroxybenzoate + NADH + O2
benzene-1,2,5-triol + CO2 + H2O + NAD+
-
-
-
-
?
2,6-dihydroxybenzoate + NADH + O2
pyrogallol + CO2 + H2O + NAD+
-
-
-
?
2,6-dihydroxybenzoate + NADH + O2
pyrogallol + CO2 + H2O + NAD+
-
-
-
-
?
2,6-dihydroxybenzoate + NADH + O2
pyrogallol + CO2 + H2O + NAD+
-
-
-
-
?
2,6-dihydroxybenzoate + NADH + O2
pyrogallol + CO2 + H2O + NAD+
-
-
-
?
2,6-dihydroxybenzoate + NADH + O2
pyrogallol + CO2 + H2O + NAD+
-
-
-
-
?
3,5-dinitrosalicylate + NADH + O2
? + NAD+ + H2O + CO2
-
-
-
-
?
3,5-dinitrosalicylate + NADH + O2
? + NAD+ + H2O + CO2
-
-
-
-
?
3-aminosalicylate + NADH + H+ + O2
3-aminobenzene-1,2-diol + NAD+ + H2O + CO2
-
11% activity compared to salicylate
-
-
?
3-aminosalicylate + NADH + H+ + O2
3-aminobenzene-1,2-diol + NAD+ + H2O + CO2
-
11% activity compared to salicylate
-
-
?
3-aminosalicylate + NADH + H+ + O2
3-aminobenzene-1,2-diol + NAD+ + H2O + CO2
-
62% activity compared to salicylate
-
-
?
3-aminosalicylate + NADH + H+ + O2
3-aminobenzene-1,2-diol + NAD+ + H2O + CO2
-
62% activity compared to salicylate
-
-
?
3-chlorosalicylate + NADH + H+ + O2
3-chlorobenzene-1,2-diol + NAD+ + H2O + CO2
-
15% activity compared to salicylate
-
-
?
3-chlorosalicylate + NADH + H+ + O2
3-chlorobenzene-1,2-diol + NAD+ + H2O + CO2
-
15% activity compared to salicylate
-
-
?
3-chlorosalicylate + NADH + H+ + O2
3-chlorobenzene-1,2-diol + NAD+ + H2O + CO2
-
23% activity compared to salicylate
-
-
?
3-chlorosalicylate + NADH + H+ + O2
3-chlorobenzene-1,2-diol + NAD+ + H2O + CO2
-
23% activity compared to salicylate
-
-
?
3-methylsalicylate + NADH + 2 H+ + O2
3-methylcatechol + NAD+ + H2O + CO2
-
-
-
r
3-methylsalicylate + NADH + 2 H+ + O2
3-methylcatechol + NAD+ + H2O + CO2
-
-
-
r
3-methylsalicylate + NADH + 2 H+ + O2
3-methylcatechol + NAD+ + H2O + CO2
-
76% of the activity with salicylate
-
-
?
3-methylsalicylate + NADH + H+ + O2
3-methylbenzene-1,2-diol + NAD+ + H2O + CO2
-
47% activity compared to salicylate
-
-
?
3-methylsalicylate + NADH + H+ + O2
3-methylbenzene-1,2-diol + NAD+ + H2O + CO2
-
86% activity compared to salicylate
-
-
?
3-methylsalicylate + NADH + O2
1,2-dihydroxy-3-methylbenzene + CO2 + NAD+ + H2O
-
-
-
-
?
3-methylsalicylate + NADH + O2
1,2-dihydroxy-3-methylbenzene + CO2 + NAD+ + H2O
-
-
-
-
?
3-methylsalicylate + NADH + O2
1,2-dihydroxy-3-methylbenzene + NAD+ + H2O + CO2
-
-
-
-
?
3-methylsalicylate + NADH + O2
1,2-dihydroxy-3-methylbenzene + NAD+ + H2O + CO2
-
-
-
-
?
4-aminosalicylate + NADH + 2 H+ + O2
4-aminocatechol + NAD+ + H2O + CO2
-
72% activity compared to salicylate
-
-
?
4-aminosalicylate + NADH + 2 H+ + O2
4-aminocatechol + NAD+ + H2O + CO2
-
72% activity compared to salicylate
-
-
?
4-aminosalicylate + NADH + H+ + O2
4-aminobenzene-1,2-diol + NAD+ + H2O + CO2
-
94% activity compared to salicylate
-
-
?
4-aminosalicylate + NADH + H+ + O2
4-aminobenzene-1,2-diol + NAD+ + H2O + CO2
-
130% activity compared to salicylate
-
-
?
4-aminosalicylate + NADH + O2
4-aminocatechol + CO2 + NAD+ + H2O
-
-
-
-
?
4-aminosalicylate + NADH + O2
4-aminocatechol + CO2 + NAD+ + H2O
-
-
-
-
?
4-aminosalicylate + NADH + O2
4-aminocatechol + CO2 + NAD+ + H2O
-
-
-
-
?
4-chlorosalicylate + NADH + H+ + O2
4-chlorobenzene-1,2-diol + NAD+ + H2O + CO2
-
43% activity compared to salicylate
-
-
?
4-chlorosalicylate + NADH + H+ + O2
4-chlorobenzene-1,2-diol + NAD+ + H2O + CO2
-
78% activity compared to salicylate
-
-
?
4-chlorosalicylate + NADH + O2
1,2-dihydroxy-4-chlorobenzene + CO2 + NAD+ + H2O
-
-
-
-
?
4-chlorosalicylate + NADH + O2
1,2-dihydroxy-4-chlorobenzene + CO2 + NAD+ + H2O
-
-
-
-
?
4-chlorosalicylate + NADH + O2
1,2-dihydroxy-4-chlorobenzene + CO2 + NAD+ + H2O
-
-
-
-
?
4-chlorosalicylate + NADH + O2
1,2-dihydroxy-4-chlorobenzene + CO2 + NAD+ + H2O
-
-
-
-
?
4-methylsalicylate + NADH + 2 H+ + O2
4-methylcatechol + NAD+ + H2O + CO2
-
-
-
?
4-methylsalicylate + NADH + 2 H+ + O2
4-methylcatechol + NAD+ + H2O + CO2
-
108% of the activity with salicylate
-
-
?
4-methylsalicylate + NADH + H+ + O2
4-methylbenzene-1,2-diol + NAD+ + H2O + CO2
-
166% activity compared to salicylate
-
-
?
4-methylsalicylate + NADH + H+ + O2
4-methylbenzene-1,2-diol + NAD+ + H2O + CO2
-
164% activity compared to salicylate
-
-
?
5-aminosalicylate + NADH + 2 H+ + O2
5-aminocatechol + NAD+ + H2O + CO2
-
-
-
r
5-aminosalicylate + NADH + 2 H+ + O2
5-aminocatechol + NAD+ + H2O + CO2
-
-
-
r
5-aminosalicylate + NADH + H+ + O2
5-aminobenzene-1,2-diol + NAD+ + H2O + CO2
-
80% activity compared to salicylate
-
-
?
5-aminosalicylate + NADH + H+ + O2
5-aminobenzene-1,2-diol + NAD+ + H2O + CO2
-
50% activity compared to salicylate
-
-
?
5-chlorosalicylate + NADH + H+ + O2
5-chlorobenzene-1,2-diol + NAD+ + H2O + CO2
-
14% activity compared to salicylate
-
-
?
5-chlorosalicylate + NADH + H+ + O2
5-chlorobenzene-1,2-diol + NAD+ + H2O + CO2
-
18% activity compared to salicylate
-
-
?
5-chlorosalicylate + NADH + O2
1,2-dihydroxy-5-chlorobenzene + CO2 + NAD+ + H2O
-
-
-
-
?
5-chlorosalicylate + NADH + O2
1,2-dihydroxy-5-chlorobenzene + CO2 + NAD+ + H2O
-
-
-
-
?
5-chlorosalicylate + NADH + O2
1,2-dihydroxy-5-chlorobenzene + CO2 + NAD+ + H2O
-
-
-
-
?
5-chlorosalicylate + NADH + O2
1,2-dihydroxy-5-chlorobenzene + NAD+ + H2O + CO2
-
-
-
-
?
5-chlorosalicylate + NADH + O2
1,2-dihydroxy-5-chlorobenzene + NAD+ + H2O + CO2
-
-
-
-
?
5-hydroxysalicylate + NADH + H+ + O2
2,5-dihydroxyphenol + NAD+ + H2O + CO2
-
132% activity compared to salicylate
-
-
?
5-hydroxysalicylate + NADH + H+ + O2
2,5-dihydroxyphenol + NAD+ + H2O + CO2
-
84% activity compared to salicylate
-
-
?
5-methylsalicylate + NADH + 2 H+ + O2
5-methylcatechol + NAD+ + H2O + CO2
-
-
-
r
5-methylsalicylate + NADH + 2 H+ + O2
5-methylcatechol + NAD+ + H2O + CO2
-
-
-
r
5-methylsalicylate + NADH + 2 H+ + O2
5-methylcatechol + NAD+ + H2O + CO2
-
-
-
?
5-methylsalicylate + NADH + H+ + O2
1,2-dihydroxy-5-methylbenzene + CO2 + NAD+ + H2O
-
-
-
-
?
5-methylsalicylate + NADH + H+ + O2
1,2-dihydroxy-5-methylbenzene + CO2 + NAD+ + H2O
-
-
-
-
?
5-methylsalicylate + NADH + H+ + O2
1,2-dihydroxy-5-methylbenzene + CO2 + NAD+ + H2O
-
-
-
-
?
5-methylsalicylate + NADH + H+ + O2
1,2-dihydroxy-5-methylbenzene + CO2 + NAD+ + H2O
-
-
-
-
?
5-methylsalicylate + NADH + H+ + O2
1,2-dihydroxy-5-methylbenzene + CO2 + NAD+ + H2O
-
-
-
-
?
5-methylsalicylate + NADH + H+ + O2
1,2-dihydroxy-5-methylbenzene + CO2 + NAD+ + H2O
-
-
-
-
?
5-methylsalicylate + NADH + H+ + O2
4-methylbenzene-1,2-diol + NAD+ + H2O + CO2
-
81% activity compared to salicylate
-
-
?
5-methylsalicylate + NADH + H+ + O2
4-methylbenzene-1,2-diol + NAD+ + H2O + CO2
-
40% activity compared to salicylate
-
-
?
o-nitrophenol + NADH + O2
catechol + nitrite + NAD+
-
-
-
-
?
o-nitrophenol + NADH + O2
catechol + nitrite + NAD+
-
-
-
-
?
p-aminosalicylate + NADH + O2
1,2-dihydroxy-4-aminobenzene + NAD+ + CO2 + H2O
-
-
-
-
?
p-aminosalicylate + NADH + O2
1,2-dihydroxy-4-aminobenzene + NAD+ + CO2 + H2O
-
-
-
-
?
salicylate + NADH + 2 H+ + O2
catechol + NAD+ + H2O + CO2
-
-
-
-
?
salicylate + NADH + 2 H+ + O2
catechol + NAD+ + H2O + CO2
-
best substrate, almost complete conversion
-
-
?
salicylate + NADH + 2 H+ + O2
catechol + NAD+ + H2O + CO2
-
-
-
-
?
salicylate + NADH + 2 H+ + O2
catechol + NAD+ + H2O + CO2
-
best substrate, almost complete conversion
-
-
?
salicylate + NADH + 2 H+ + O2
catechol + NAD+ + H2O + CO2
-
-
-
?
salicylate + NADH + 2 H+ + O2
catechol + NAD+ + H2O + CO2
-
-
-
?
salicylate + NADH + 2 H+ + O2
catechol + NAD+ + H2O + CO2
-
-
-
?
salicylate + NADH + 2 H+ + O2
catechol + NAD+ + H2O + CO2
-
-
-
?
salicylate + NADH + 2 H+ + O2
catechol + NAD+ + H2O + CO2
-
-
-
?
salicylate + NADH + 2 H+ + O2
catechol + NAD+ + H2O + CO2
-
-
-
?
salicylate + NADH + 2 H+ + O2
catechol + NAD+ + H2O + CO2
-
-
-
?
salicylate + NADH + 2 H+ + O2
catechol + NAD+ + H2O + CO2
-
-
-
r
salicylate + NADH + 2 H+ + O2
catechol + NAD+ + H2O + CO2
-
-
-
?
salicylate + NADH + 2 H+ + O2
catechol + NAD+ + H2O + CO2
-
-
-
?
salicylate + NADH + 2 H+ + O2
catechol + NAD+ + H2O + CO2
-
-
-
r
salicylate + NADH + 2 H+ + O2
catechol + NAD+ + H2O + CO2
-
-
-
?
salicylate + NADH + 2 H+ + O2
catechol + NAD+ + H2O + CO2
-
-
-
?
salicylate + NADH + 2 H+ + O2
catechol + NAD+ + H2O + CO2
-
-
-
-
?
salicylate + NADH + 2 H+ + O2
catechol + NAD+ + H2O + CO2
-
-
-
?
salicylate + NADH + 2 H+ + O2
catechol + NAD+ + H2O + CO2
-
-
-
?
salicylate + NADH + H+ + O2
catechol + NAD+ + H2O + CO2
-
-
-
-
?
salicylate + NADH + H+ + O2
catechol + NAD+ + H2O + CO2
-
-
-
-
?
salicylate + NADH + H+ + O2
catechol + NAD+ + H2O + CO2
-
-
-
-
?
salicylate + NADH + H+ + O2
catechol + NAD+ + H2O + CO2
100% activity
-
-
?
salicylate + NADH + H+ + O2
catechol + NAD+ + H2O + CO2
-
bismuth salt of salicylate
-
-
?
salicylate + NADH + H+ + O2
catechol + NAD+ + H2O + CO2
-
bismuth salt of salicylate
-
-
?
salicylate + NADH + H+ + O2
catechol + NAD+ + H2O + CO2
-
-
-
-
?
salicylate + NADH + H+ + O2
catechol + NAD+ + H2O + CO2
-
-
-
-
?
salicylate + NADH + H+ + O2
catechol + NAD+ + H2O + CO2
-
-
-
-
?
salicylate + NADH + H+ + O2
catechol + NAD+ + H2O + CO2
-
-
-
-
?
salicylate + NADH + H+ + O2
catechol + NAD+ + H2O + CO2
-
100% activity
-
-
?
salicylate + NADH + H+ + O2
catechol + NAD+ + H2O + CO2
-
-
-
-
?
salicylate + NADH + H+ + O2
catechol + NAD+ + H2O + CO2
-
100% activity
-
-
?
salicylate + NADH + H+ + O2
catechol + NAD+ + H2O + CO2
-
-
389997, 389998, 390001, 390002, 390003, 390004, 390006, 390007, 390009, 390010, 390013, 390014, 390015, 390016, 390017, 741666, 741825, 742130 -
-
?
salicylate + NADH + H+ + O2
catechol + NAD+ + H2O + CO2
-
100% activity
-
-
?
salicylate + NADH + H+ + O2
catechol + NAD+ + H2O + CO2
-
-
-
-
?
salicylate + NADH + H+ + O2
catechol + NAD+ + H2O + CO2
-
-
-
-
?
salicylate + NADH + H+ + O2
catechol + NAD+ + H2O + CO2
-
100% activity
-
-
?
salicylate + NADH + H+ + O2
catechol + NAD+ + H2O + CO2
-
-
-
-
?
salicylate + NADH + H+ + O2
catechol + NAD+ + H2O + CO2
-
-
-
?
salicylate + NADH + H+ + O2
catechol + NAD+ + H2O + CO2
-
-
-
-
?
salicylate + NADH + H+ + O2
catechol + NAD+ + H2O + CO2
-
-
-
-
?
salicylate + NADH + H+ + O2
catechol + NAD+ + H2O + CO2
-
-
-
-
?
salicylate + NADH + H+ + O2
catechol + NAD+ + H2O + CO2
-
-
-
-
?
salicylate + NADH + H+ + O2
catechol + NAD+ + H2O + CO2
-
-
-
-
?
salicylate + O2 + NADH + 2 H+
catechol + CO2 + H2O + NAD+
-
-
-
-
?
salicylate + O2 + NADH + 2 H+
catechol + CO2 + H2O + NAD+
-
-
-
-
?
salicylate + O2 + NADH + 2 H+
catechol + CO2 + H2O + NAD+
-
-
-
-
?
salicylate + O2 + NADPH + 2 H+
catechol + CO2 + H2O + NADP+
-
-
-
-
?
salicylate + O2 + NADPH + 2 H+
catechol + CO2 + H2O + NADP+
-
-
-
-
?
additional information
?
-
terbinafine resistance mediated by salicylate 1-monooxygenase. Terbinafine, which has a naphthalene nucleus in its chemical structure, may be a substrate for a salicylate-like part of an aromatic compound degradation pathway in Aspergillus nidulans
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-
?
additional information
?
-
-
terbinafine resistance mediated by salicylate 1-monooxygenase. Terbinafine, which has a naphthalene nucleus in its chemical structure, may be a substrate for a salicylate-like part of an aromatic compound degradation pathway in Aspergillus nidulans
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-
?
additional information
?
-
-
incubation of salicylic acid by a combination of cell extracts from the shyA with the crcA or the hqdA overexpression strains results in the formation of cis,cis-muconic acid, demonstrating that the combination of these enzymes is sufficient for this biochemical conversion. The conversion is highly efficient. No activity with protocatechuate, vanillate, syringate, 3-hydroxybenzoate, 4-hydroxybenzoate, and benzoate. ShyA shows activity on o-hydroxylated benzoic acids, such as 4-aminosalicylic acid, 2,3-dihydroxybenzoic acid, and gentisic acid, but not on benzoic acid derivatives that are not o-hydroxylated. The enzyme also exhibits NADH oxidase activity besides the more rapid hydroxylase activity
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-
-
additional information
?
-
-
incubation of salicylic acid by a combination of cell extracts from the shyA with the crcA or the hqdA overexpression strains results in the formation of cis,cis-muconic acid, demonstrating that the combination of these enzymes is sufficient for this biochemical conversion. The conversion is highly efficient. No activity with protocatechuate, vanillate, syringate, 3-hydroxybenzoate, 4-hydroxybenzoate, and benzoate. ShyA shows activity on o-hydroxylated benzoic acids, such as 4-aminosalicylic acid, 2,3-dihydroxybenzoic acid, and gentisic acid, but not on benzoic acid derivatives that are not o-hydroxylated. The enzyme also exhibits NADH oxidase activity besides the more rapid hydroxylase activity
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-
-
additional information
?
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-
apoenzyme-flavin interaction
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-
?
additional information
?
-
-
no activity with 2,1,3-benzothiadiazole and 2,6-dichloroisonicotinic acid
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-
?
additional information
?
-
the ability of wild-type from strain 46422 and the FgshyC mutant to metabolize salicylate (SA) is tested. When SA is added to liquid cultures of either wild-type strain 46422 or the FgShyC mutant, it is degraded similarly. This demonstrates that Fusarium graminearum produces salicylate hydroxylases and argues against this role for FgShyC. In addition, recombinant FgShyC protein expressed in Escherichia coli does not convert SA to catechol in a colorimetric plate assay. Although FgShyC has sequence homology with salicylic hydroxylase genes, it does not function as a salicylate hydroxylase in our assays
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-
-
additional information
?
-
the ability of wild-type from strain 46422 and the FgshyC mutant to metabolize salicylate (SA) is tested. When SA is added to liquid cultures of either wild-type strain 46422 or the FgShyC mutant, it is degraded similarly. This demonstrates that Fusarium graminearum produces salicylate hydroxylases and argues against this role for FgShyC. In addition, recombinant FgShyC protein expressed in Escherichia coli does not convert SA to catechol in a colorimetric plate assay. Although FgShyC has sequence homology with salicylic hydroxylase genes, it does not function as a salicylate hydroxylase in our assays
-
-
-
additional information
?
-
-
the ability of wild-type from strain 46422 and the FgshyC mutant to metabolize salicylate (SA) is tested. When SA is added to liquid cultures of either wild-type strain 46422 or the FgShyC mutant, it is degraded similarly. This demonstrates that Fusarium graminearum produces salicylate hydroxylases and argues against this role for FgShyC. In addition, recombinant FgShyC protein expressed in Escherichia coli does not convert SA to catechol in a colorimetric plate assay. Although FgShyC has sequence homology with salicylic hydroxylase genes, it does not function as a salicylate hydroxylase in our assays
-
-
-
additional information
?
-
the ability of wild-type from strain 46422 and the FgshyC mutant to metabolize salicylate (SA) is tested. When SA is added to liquid cultures of either wild-type strain 46422 or the FgShyC mutant, it is degraded similarly. This demonstrates that Fusarium graminearum produces salicylate hydroxylases and argues against this role for FgShyC. In addition, recombinant FgShyC protein expressed in Escherichia coli does not convert SA to catechol in a colorimetric plate assay. Although FgShyC has sequence homology with salicylic hydroxylase genes, it does not function as a salicylate hydroxylase in our assays
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-
-
additional information
?
-
-
mechanism
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-
?
additional information
?
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-
mechanism
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?
additional information
?
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-
mechanism
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?
additional information
?
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-
mechanism
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?
additional information
?
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-
mechanism
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?
additional information
?
-
-
enzyme catalyzes formation of catechol from substrate analogues such as o-nitro-, o-amino-, o-iodo-, o-bromo- and o-chlorophenol by removing the ortho substituted groups
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-
?
additional information
?
-
-
enzyme catalyses hydroxylation and dehalogenation of o-halogenophenols and also denitrification of o-nitrophenol with unusual stoichiometry
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-
?
additional information
?
-
-
by chemical treatment of the enzyme with dicarbonyl reagents, such as glyoxal, the original oxygenase activity is converted to the salicylate-dependent NADH-dehydrogenase activity with free FAD as electron acceptor
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-
?
additional information
?
-
-
o-fluorophenol is not converted to catechol, though NADH oxidation is observed
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-
?
additional information
?
-
product identification by NMR
-
-
-
additional information
?
-
salicylate hydroxylase NahG has a single redox site in which FAD is reduced by NADH, the O2 is activated by the reduced flavin, and salicylate undergoes an oxidative decarboxylation by a C(4a)-hydroperoxyflavin intermediate to give catechol
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-
-
additional information
?
-
salicylate hydroxylase NahG has a single redox site in which FAD is reduced by NADH, the O2 is activated by the reduced flavin, and salicylate undergoes an oxidative decarboxylation by a C(4a)-hydroperoxyflavin intermediate to give catechol
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-
-
additional information
?
-
product identification by NMR
-
-
-
additional information
?
-
-
product identification by NMR
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-
-
additional information
?
-
-
mechanism
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-
?
additional information
?
-
the recombinant SlSA1H enzyme shows high substrate specificity. Poor activity with 6-methylsalicylate, no activity with 3-hydroxybenzoate, 4-hydroxybenzoate, 2-methoxybenzoate, 2-coumarate, gallate, shikimate, 2,3-dihydroxybenzoate, 2,4-dihydroxybenzoate, 2,5-dihydroxybenzoate, 2,6-dihydroxybenzoate, 3,4-dihydroxybenzoate, 3,5-dihydroxybenzoate, 3-methylsalicylate, 4-methylsalicylate, and 5-methylsalicylate
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-
-
additional information
?
-
-
the recombinant SlSA1H enzyme shows high substrate specificity. Poor activity with 6-methylsalicylate, no activity with 3-hydroxybenzoate, 4-hydroxybenzoate, 2-methoxybenzoate, 2-coumarate, gallate, shikimate, 2,3-dihydroxybenzoate, 2,4-dihydroxybenzoate, 2,5-dihydroxybenzoate, 2,6-dihydroxybenzoate, 3,4-dihydroxybenzoate, 3,5-dihydroxybenzoate, 3-methylsalicylate, 4-methylsalicylate, and 5-methylsalicylate
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-
-
additional information
?
-
-
1-hydroxy-2-naphthoate, which is an intermediate in phenanthrene degradation, is not hydroxylated by PhnII, but it induces a high rate of uncoupled oxidation of NADH
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-
?
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evolution
phylogenetic analysis and tree, salicylate hydroxylase homologue FgShy1 is most closely related to NahG from Pseudomonas putida and Shy1 from Ustilago maydis
evolution
phylogenetic analysis and tree, salicylate hydroxylase homologue FgShyC is unique to the North American population 2 (NA2), FgShyC is present only in NA2 strains
evolution
the enzyme reaction links the upper and lower pathways of naphthalene degradation by soil pseudomonads, a bacterial genus encompassing many species that can use naphthalene or salicylate as sole carbon sources. NahG hydroxylates and decarboxylates the substrate at the same aromatic carbon atom (ipso substitution), an exquisite feature that is remarkable from a synthetic perspective. NahG is one of the few examples of a flavin enzyme that catalyzes an ortho hydroxylation relative to the substrate's phenol group, which is usually required for efficient catalysis. Other monooxygenases exhibit different regioselectivities. Enzyme structure comparisons, overview. The aromatic residues F85,W87, F230, F243, and W293 are positioned on the antiparallel beta-sheet opposite from the FAD isoalloxazine ring and likely form a hydrophobic environment facing the salicylate. In addition, a number of nonpolar amino acid residues, including A190, M194, M219, L221, L228, and V241, also compose the substrate-binding pocket, whereas the charged residues D224, H226, R247, H322, E381, and R383 are distinctly grouped near the active site, laterally positioned on the re-side of the isoalloxazine and leading to the solvent-accessible protein surface
evolution
the NahG homologue from tomato (SlSA1H) belongs to the FAD/NAD(P)-binding oxidoreductase family and is capable of catalyzing the oxidative decarboxylation (i.e. 1-hydroxylation) of SA to catechol both in vitro and in planta. Phylogenetic tree, overview
evolution
-
phylogenetic analysis and tree, salicylate hydroxylase homologue FgShy1 is most closely related to NahG from Pseudomonas putida and Shy1 from Ustilago maydis
-
evolution
-
phylogenetic analysis and tree, salicylate hydroxylase homologue FgShyC is unique to the North American population 2 (NA2), FgShyC is present only in NA2 strains
-
evolution
-
the enzyme reaction links the upper and lower pathways of naphthalene degradation by soil pseudomonads, a bacterial genus encompassing many species that can use naphthalene or salicylate as sole carbon sources. NahG hydroxylates and decarboxylates the substrate at the same aromatic carbon atom (ipso substitution), an exquisite feature that is remarkable from a synthetic perspective. NahG is one of the few examples of a flavin enzyme that catalyzes an ortho hydroxylation relative to the substrate's phenol group, which is usually required for efficient catalysis. Other monooxygenases exhibit different regioselectivities. Enzyme structure comparisons, overview. The aromatic residues F85,W87, F230, F243, and W293 are positioned on the antiparallel beta-sheet opposite from the FAD isoalloxazine ring and likely form a hydrophobic environment facing the salicylate. In addition, a number of nonpolar amino acid residues, including A190, M194, M219, L221, L228, and V241, also compose the substrate-binding pocket, whereas the charged residues D224, H226, R247, H322, E381, and R383 are distinctly grouped near the active site, laterally positioned on the re-side of the isoalloxazine and leading to the solvent-accessible protein surface
-
evolution
-
phylogenetic analysis and tree, salicylate hydroxylase homologue FgShy1 is most closely related to NahG from Pseudomonas putida and Shy1 from Ustilago maydis
-
evolution
-
phylogenetic analysis and tree, salicylate hydroxylase homologue FgShy1 is most closely related to NahG from Pseudomonas putida and Shy1 from Ustilago maydis
-
evolution
-
phylogenetic analysis and tree, salicylate hydroxylase homologue FgShy1 is most closely related to NahG from Pseudomonas putida and Shy1 from Ustilago maydis
-
evolution
-
phylogenetic analysis and tree, salicylate hydroxylase homologue FgShy1 is most closely related to NahG from Pseudomonas putida and Shy1 from Ustilago maydis
-
malfunction
a mutant strain with multiple copies of salA exhibits elevated expression of salA and increased terbinafine resistance
malfunction
-
deletion of shyA, dhbA, and crcA in Aspergillus niger results in reduced growth on salicylic acid, 2,3-dihydroxybenzoic acid, and catechol, respectively, confirming their in vivo roles
malfunction
-
a mutant strain with multiple copies of salA exhibits elevated expression of salA and increased terbinafine resistance
-
malfunction
-
deletion of shyA, dhbA, and crcA in Aspergillus niger results in reduced growth on salicylic acid, 2,3-dihydroxybenzoic acid, and catechol, respectively, confirming their in vivo roles
-
metabolism
-
naphthalene degradation
metabolism
salicylate 1-hydroxylase is not clustered with the meta cleavage pathway
metabolism
strain MT1 is capable of degrading 4- and 5-chlorosalicylates via 4-chlorocatechol, 3-chloromuconate, and maleylacetate by the chlorocatechol pathway, overview
metabolism
-
in the filamentous fungus Aspergillus niger, two salicylic acid metabolic pathways have been suggested. The first pathway converts salicylic acid to catechol by a salicylate hydroxylase (ShyA). In the second pathway, salicylic acid is 3-hydroxylated to 2,3-dihydroxybenzoic acid, followed by decarboxylation to catechol by 2,3-dihydroxybenzoate decarboxylase (DhbA). ShyA, DhbA, and CrcA are involved in the fungal salicylic acid pathway, overview. The recombinant ShyA and CrcA together can efficiently convert salicylic acid into cis,cis-muconic acid through catechol as an intermediate. NRRL3_43 is suggested to be a salicylic acid hydroxylase-like enzyme
metabolism
salicylate hydroxylase (NahG) is a flavin-dependent monooxygenase that catalyzes the decarboxylative hydroxylation of salicylate into catechol in the naphthalene degradation pathway in Pseudomonas putida strain G7 with stoichiometric consumption of NADH and O2. This reaction links the upper and lower pathways of naphthalene degradation by soil pseudomonads, a bacterial genus encompassing many species that can use naphthalene or salicylate as sole carbon sources
metabolism
-
in the filamentous fungus Aspergillus niger, two salicylic acid metabolic pathways have been suggested. The first pathway converts salicylic acid to catechol by a salicylate hydroxylase (ShyA). In the second pathway, salicylic acid is 3-hydroxylated to 2,3-dihydroxybenzoic acid, followed by decarboxylation to catechol by 2,3-dihydroxybenzoate decarboxylase (DhbA). ShyA, DhbA, and CrcA are involved in the fungal salicylic acid pathway, overview. The recombinant ShyA and CrcA together can efficiently convert salicylic acid into cis,cis-muconic acid through catechol as an intermediate. NRRL3_43 is suggested to be a salicylic acid hydroxylase-like enzyme
-
metabolism
-
salicylate hydroxylase (NahG) is a flavin-dependent monooxygenase that catalyzes the decarboxylative hydroxylation of salicylate into catechol in the naphthalene degradation pathway in Pseudomonas putida strain G7 with stoichiometric consumption of NADH and O2. This reaction links the upper and lower pathways of naphthalene degradation by soil pseudomonads, a bacterial genus encompassing many species that can use naphthalene or salicylate as sole carbon sources
-
metabolism
-
naphthalene degradation
-
physiological function
enzyme activity is needed for growth on plates with salicylic acid as a sole carbon source. Enzyme does not contribute significantly to virulence in a seedling infection assay
physiological function
-
expression of enzyme gene in Arabidopsis thaliana, with chloroplast targeting sequence. Plants expressing NahG gene in the chloroplasts are unable to accumulate salicylic acid induced after pathogen or UV exposure. The decreased levels in chloroplast-targeted NahG are in the same range as those observed in transgenic plants expressing NahG in the cytosol. Data infer that salicylic acid is initially located in the chloroplasts
physiological function
FgShy1 is not essential for the growth of Fusarium graminearum on agar medium with SA, suggesting additional enzymes or other SA degradation pathways exist
physiological function
in plants, salicylate (SA) is best known as an important phytohormone involved in the activation of defense response against a wide range of biotic and abiotic stresses. Besides its role in immune responses, SA also plays crucial roles in plant growth and developmental processes such as photosynthesis, flowering, and senescence. Because of its chemical reactivity, lipophilicity, and phytotoxicity, most of the SA synthesized in plants is further modified into different derivatives to fine-tune its storage, function, and/or mobility. These modifications include glycosylation, methylation, sulfonation, amino acid conjugation, and hydroxylation. Enzyme SlSA1H may play an important role in the homeostasis of SA in vivo
physiological function
salicylate hydroxylase (NahG) is a flavin-dependent monooxygenase that catalyzes the decarboxylative hydroxylation of salicylate into catechol in the naphthalene degradation pathway in Pseudomonas putida strain G7
physiological function
salicylate hydroxylase (SALH) is a member of oxygen oxidoreductases, which catalyzes the hydroxylation and decarboxylation of salicylate to generate catechol
physiological function
the salA gene, encoding salicylate 1-monooxygenase, is involved in resistance of the dermatophyte Trichophyton rubrum to terbinafine (TRB), one of the most effective antifungal drugs against dermatophytes. Resistance to TRB is mediated by multiple salA copies in Trichophyton rubrum. Salicylate 1-monooxygenase is an enzyme that participates in the naphthalene degradation pathway, converting the intermediate metabolite salicylic acid into catechol
physiological function
-
the salA gene, encoding salicylate 1-monooxygenase, is involved in resistance of the dermatophyte Trichophyton rubrum to terbinafine (TRB), one of the most effective antifungal drugs against dermatophytes. Resistance to TRB is mediated by multiple salA copies in Trichophyton rubrum. Salicylate 1-monooxygenase is an enzyme that participates in the naphthalene degradation pathway, converting the intermediate metabolite salicylic acid into catechol
-
physiological function
-
FgShy1 is not essential for the growth of Fusarium graminearum on agar medium with SA, suggesting additional enzymes or other SA degradation pathways exist
-
physiological function
-
salicylate hydroxylase (NahG) is a flavin-dependent monooxygenase that catalyzes the decarboxylative hydroxylation of salicylate into catechol in the naphthalene degradation pathway in Pseudomonas putida strain G7
-
physiological function
-
expression of enzyme gene in Arabidopsis thaliana, with chloroplast targeting sequence. Plants expressing NahG gene in the chloroplasts are unable to accumulate salicylic acid induced after pathogen or UV exposure. The decreased levels in chloroplast-targeted NahG are in the same range as those observed in transgenic plants expressing NahG in the cytosol. Data infer that salicylic acid is initially located in the chloroplasts
-
physiological function
-
enzyme activity is needed for growth on plates with salicylic acid as a sole carbon source. Enzyme does not contribute significantly to virulence in a seedling infection assay
-
physiological function
-
FgShy1 is not essential for the growth of Fusarium graminearum on agar medium with SA, suggesting additional enzymes or other SA degradation pathways exist
-
physiological function
-
FgShy1 is not essential for the growth of Fusarium graminearum on agar medium with SA, suggesting additional enzymes or other SA degradation pathways exist
-
physiological function
-
FgShy1 is not essential for the growth of Fusarium graminearum on agar medium with SA, suggesting additional enzymes or other SA degradation pathways exist
-
physiological function
-
salicylate hydroxylase (SALH) is a member of oxygen oxidoreductases, which catalyzes the hydroxylation and decarboxylation of salicylate to generate catechol
-
physiological function
-
FgShy1 is not essential for the growth of Fusarium graminearum on agar medium with SA, suggesting additional enzymes or other SA degradation pathways exist
-
additional information
struccture-function relationship and reaction mechansim analysis, overview. Hammett plots for Km and kcat using substituted salicylates indicate changes in rate-limiting step. Electron-donating groups favor the hydroxylation of salicylate by a peroxyflavin to yield a Wheland-like intermediate, whereas the decarboxylation of this intermediate is faster for electron-withdrawing groups
additional information
structure-function relationship and analysis using combined quantum mechanical/molecular mechanical (QM/MM) calculations, overview
additional information
-
struccture-function relationship and reaction mechansim analysis, overview. Hammett plots for Km and kcat using substituted salicylates indicate changes in rate-limiting step. Electron-donating groups favor the hydroxylation of salicylate by a peroxyflavin to yield a Wheland-like intermediate, whereas the decarboxylation of this intermediate is faster for electron-withdrawing groups
-
additional information
-
structure-function relationship and analysis using combined quantum mechanical/molecular mechanical (QM/MM) calculations, overview
-
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K163E
-
site directed mutagenesis, Lys163 is involved in the NADH-binding site
K163G
-
site directed mutagenesis, Lys163 is involved in the NADH-binding site
K163R
-
site directed mutagenesis, Lys163 is involved in the NADH-binding site
additional information
-
generation of six deletion mutants, the DELTAshyA, DELTAdhbA, DELTAcrcA, DELTA43 (putative salicylate hydroxylase), DELTA2597 (putative salicylate 3-hydroxylase), and DELTA5330 (putative catechol 1,2-dioxygenase) mutants. The growth of the DELTAshyA mutant is reduced on salicylic acid but not on the other aromatic compounds tested, confirming its role as the salicylate hydroxylase of Aspergillus niger. Growth of the DELTAdhbA mutant is reduced on 2,3-dihydroxybenzoic acid but not on salicylic acid or catechol, confirming its metabolic role. Deletion of crcA results in growth similar to that of the no-carbon source control on salicylic acid, 2,3-dihydroxybenzoic acid, and catechol, while deletion of NRRL3_5330 or hqdA does not result in a phenotype, indicating that crcA encodes the catechol 1,2-dioxygenase of Aspergillus niger. Growth of the DELTA43, DELTA5330, and DELTA2597 mutants do not result in any phenotypes on the tested aromatic compounds
additional information
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generation of six deletion mutants, the DELTAshyA, DELTAdhbA, DELTAcrcA, DELTA43 (putative salicylate hydroxylase), DELTA2597 (putative salicylate 3-hydroxylase), and DELTA5330 (putative catechol 1,2-dioxygenase) mutants. The growth of the DELTAshyA mutant is reduced on salicylic acid but not on the other aromatic compounds tested, confirming its role as the salicylate hydroxylase of Aspergillus niger. Growth of the DELTAdhbA mutant is reduced on 2,3-dihydroxybenzoic acid but not on salicylic acid or catechol, confirming its metabolic role. Deletion of crcA results in growth similar to that of the no-carbon source control on salicylic acid, 2,3-dihydroxybenzoic acid, and catechol, while deletion of NRRL3_5330 or hqdA does not result in a phenotype, indicating that crcA encodes the catechol 1,2-dioxygenase of Aspergillus niger. Growth of the DELTA43, DELTA5330, and DELTA2597 mutants do not result in any phenotypes on the tested aromatic compounds
-
additional information
generation of a disruption mutant of Fusarium graminearum strain NRRL 46422 gene shyC, replacement of FgShyC is confirmed by genome sequencing and analysis
additional information
generation of a disruption mutant of Fusarium graminearum strain NRRL 46422 gene shyC, replacement of FgShyC is confirmed by genome sequencing and analysis
additional information
-
generation of a disruption mutant of Fusarium graminearum strain NRRL 46422 gene shyC, replacement of FgShyC is confirmed by genome sequencing and analysis
additional information
generation of enzyme deletion mutants. The wild-type strain PH-1 degrades approximately 80% of the added salicylate (SA) whereas Fgshy1 deletion mutants are significantly reduced in their ability to degrade SA in liquid culture. Compared to media control, Fgshy1-M1 and M2 mutants are able to degrade 10 and 11% of the SA, respectively, but mutant Fgshy1-M18 is almost inactive. With addition of SA at concentrations of 1 and 2 mM, the Fgshy1 mutant grows slightly slower than the wild-type PH-1 and the hyphae turn yellow. But no significant growth difference between Fgshy1 mutant and PH-1 is found by statistical analysis. Disruption of FgShy1 does not significantly affect Fusarium graminearum
additional information
generation of enzyme deletion mutants. The wild-type strain PH-1 degrades approximately 80% of the added salicylate (SA) whereas Fgshy1 deletion mutants are significantly reduced in their ability to degrade SA in liquid culture. Compared to media control, Fgshy1-M1 and M2 mutants are able to degrade 10 and 11% of the SA, respectively, but mutant Fgshy1-M18 is almost inactive. With addition of SA at concentrations of 1 and 2 mM, the Fgshy1 mutant grows slightly slower than the wild-type PH-1 and the hyphae turn yellow. But no significant growth difference between Fgshy1 mutant and PH-1 is found by statistical analysis. Disruption of FgShy1 does not significantly affect Fusarium graminearum
additional information
-
generation of enzyme deletion mutants. The wild-type strain PH-1 degrades approximately 80% of the added salicylate (SA) whereas Fgshy1 deletion mutants are significantly reduced in their ability to degrade SA in liquid culture. Compared to media control, Fgshy1-M1 and M2 mutants are able to degrade 10 and 11% of the SA, respectively, but mutant Fgshy1-M18 is almost inactive. With addition of SA at concentrations of 1 and 2 mM, the Fgshy1 mutant grows slightly slower than the wild-type PH-1 and the hyphae turn yellow. But no significant growth difference between Fgshy1 mutant and PH-1 is found by statistical analysis. Disruption of FgShy1 does not significantly affect Fusarium graminearum
additional information
-
generation of enzyme deletion mutants. The wild-type strain PH-1 degrades approximately 80% of the added salicylate (SA) whereas Fgshy1 deletion mutants are significantly reduced in their ability to degrade SA in liquid culture. Compared to media control, Fgshy1-M1 and M2 mutants are able to degrade 10 and 11% of the SA, respectively, but mutant Fgshy1-M18 is almost inactive. With addition of SA at concentrations of 1 and 2 mM, the Fgshy1 mutant grows slightly slower than the wild-type PH-1 and the hyphae turn yellow. But no significant growth difference between Fgshy1 mutant and PH-1 is found by statistical analysis. Disruption of FgShy1 does not significantly affect Fusarium graminearum
-
additional information
-
generation of enzyme deletion mutants. The wild-type strain PH-1 degrades approximately 80% of the added salicylate (SA) whereas Fgshy1 deletion mutants are significantly reduced in their ability to degrade SA in liquid culture. Compared to media control, Fgshy1-M1 and M2 mutants are able to degrade 10 and 11% of the SA, respectively, but mutant Fgshy1-M18 is almost inactive. With addition of SA at concentrations of 1 and 2 mM, the Fgshy1 mutant grows slightly slower than the wild-type PH-1 and the hyphae turn yellow. But no significant growth difference between Fgshy1 mutant and PH-1 is found by statistical analysis. Disruption of FgShy1 does not significantly affect Fusarium graminearum
-
additional information
-
generation of enzyme deletion mutants. The wild-type strain PH-1 degrades approximately 80% of the added salicylate (SA) whereas Fgshy1 deletion mutants are significantly reduced in their ability to degrade SA in liquid culture. Compared to media control, Fgshy1-M1 and M2 mutants are able to degrade 10 and 11% of the SA, respectively, but mutant Fgshy1-M18 is almost inactive. With addition of SA at concentrations of 1 and 2 mM, the Fgshy1 mutant grows slightly slower than the wild-type PH-1 and the hyphae turn yellow. But no significant growth difference between Fgshy1 mutant and PH-1 is found by statistical analysis. Disruption of FgShy1 does not significantly affect Fusarium graminearum
-
additional information
-
generation of enzyme deletion mutants. The wild-type strain PH-1 degrades approximately 80% of the added salicylate (SA) whereas Fgshy1 deletion mutants are significantly reduced in their ability to degrade SA in liquid culture. Compared to media control, Fgshy1-M1 and M2 mutants are able to degrade 10 and 11% of the SA, respectively, but mutant Fgshy1-M18 is almost inactive. With addition of SA at concentrations of 1 and 2 mM, the Fgshy1 mutant grows slightly slower than the wild-type PH-1 and the hyphae turn yellow. But no significant growth difference between Fgshy1 mutant and PH-1 is found by statistical analysis. Disruption of FgShy1 does not significantly affect Fusarium graminearum
-
additional information
-
generation of a disruption mutant of Fusarium graminearum strain NRRL 46422 gene shyC, replacement of FgShyC is confirmed by genome sequencing and analysis
-
additional information
-
generation of enzyme deletion mutants. The wild-type strain PH-1 degrades approximately 80% of the added salicylate (SA) whereas Fgshy1 deletion mutants are significantly reduced in their ability to degrade SA in liquid culture. Compared to media control, Fgshy1-M1 and M2 mutants are able to degrade 10 and 11% of the SA, respectively, but mutant Fgshy1-M18 is almost inactive. With addition of SA at concentrations of 1 and 2 mM, the Fgshy1 mutant grows slightly slower than the wild-type PH-1 and the hyphae turn yellow. But no significant growth difference between Fgshy1 mutant and PH-1 is found by statistical analysis. Disruption of FgShy1 does not significantly affect Fusarium graminearum
-
additional information
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construction of transgenic plants, using wild-type Columbia(0) plants and sid2 mutant plants, overexpressing the bacterial NahG, germination of NahG transgenic plants is influenced to a lesser degree by high salinity. Catechol accumulates in the transgenic plants and acts as an antioxidant that compromises the inhibitory effects of high salinity. Salicylic acid promotes seed germination under high salinity by modulating antioxidant activity in transgenic Arabidopsis thaliana, detailed overview
additional information
generation of SlSA1H antisense knockdown transgenic tomato plants. In three analyzed SlSA1H RNAi lines (RNAi-23, RNAi-4, and RNAi-22), mRNA levels of SlSA1H relative to wild-type are reduced by 54%, 59%, and 56% in stems, respectively, and by 35%, 55%, and 66% in leaves, respectively. Whereas no significant morphological changes are observed in these plants, the guaiacol levels relative to wild-type are reduced by 47%, 52%, and 60% in stems, respectively, and by 22%, 24%, and 65% in leaves, respectively. Veratrole cannot be detected in any of these three RNAi lines
additional information
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generation of SlSA1H antisense knockdown transgenic tomato plants. In three analyzed SlSA1H RNAi lines (RNAi-23, RNAi-4, and RNAi-22), mRNA levels of SlSA1H relative to wild-type are reduced by 54%, 59%, and 56% in stems, respectively, and by 35%, 55%, and 66% in leaves, respectively. Whereas no significant morphological changes are observed in these plants, the guaiacol levels relative to wild-type are reduced by 47%, 52%, and 60% in stems, respectively, and by 22%, 24%, and 65% in leaves, respectively. Veratrole cannot be detected in any of these three RNAi lines
additional information
construction of a strain with multiple copies of salA via protoplast transformations, the mutant exhibits elevated expression of salA and increased terbinafine resistance
additional information
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construction of a strain with multiple copies of salA via protoplast transformations, the mutant exhibits elevated expression of salA and increased terbinafine resistance
additional information
-
construction of a strain with multiple copies of salA via protoplast transformations, the mutant exhibits elevated expression of salA and increased terbinafine resistance
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Pseudomonas sp.
-
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Pseudomonas sp.
-
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Aspergillus niger, Aspergillus niger NRRL3
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Fusarium graminearum (A0A455ZJ87), Fusarium graminearum (I1RIL9), Fusarium graminearum, Fusarium graminearum NRRL 31084 (I1RIL9), Fusarium graminearum NRRL 46422 (A0A455ZJ87), Fusarium graminearum CBS 123657 (I1RIL9), Fusarium graminearum PH-1 (I1RIL9), Fusarium graminearum ATCC MYA-4620 (I1RIL9), Fusarium graminearum FGSC 9075 (I1RIL9)
brenda
Costa, D.M.A.; Gomez, S.V.; de Araujo, S.S.; Pereira, M.S.; Alves, R.B.; Favaro, D.C.; Hengge, A.C.; Nagem, R.A.P.; Brandao, T.A.S.
Catalytic mechanism for the conversion of salicylate into catechol by the flavin-dependent monooxygenase salicylate hydroxylase
Int. J. Biol. Macromol.
129
588-600
2019
Pseudomonas putida (Q8RMN4), Pseudomonas putida G7 (Q8RMN4), Pseudomonas putida G7
brenda
Santos, H.; Lang, E.; Segato, F.; Rossi, A.; Martinez-Rossi, N.
Terbinafine resistance conferred by multiple copies of the salicylate 1-monooxygenase gene in Trichophyton rubrum
Med. Mycol.
56
378-381
2018
Trichophyton rubrum (F2SJL1), Trichophyton rubrum, Trichophyton rubrum CBS118892 (F2SJL1)
brenda
Zhou, F.; Last, R.L.; Pichersky, E.
Degradation of salicylic acid to catechol in Solanaceae by SA 1-hydroxylase
Plant Physiol.
185
876-891
2021
Solanum lycopersicum (A0A3Q7IJD4), Solanum lycopersicum
brenda
Wang, X.; Hou, Q.; Liu, Y.
Insights into the decarboxylative hydroxylation of salicylate catalyzed by the flavin-dependent monooxygenase salicylate hydroxylase
Theoret. Chem. Accounts
137
89
2018
Pseudomonas putida (Q59713), Pseudomonas putida S-1 (Q59713)
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