1.14.19.70: mycocyclosin synthase
This is an abbreviated version!
For detailed information about mycocyclosin synthase, go to the full flat file.
Word Map on EC 1.14.19.70
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1.14.19.70
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tuberculosis
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heme
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azole
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antimycobacterial
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clotrimazole
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triazole
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antituberculosis
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fragment-based
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econazole
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fluconazole
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medicine
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isoniazid
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pharmacology
- 1.14.19.70
- tuberculosis
- heme
- azole
-
antimycobacterial
- clotrimazole
- triazole
-
antituberculosis
-
fragment-based
- econazole
- fluconazole
- medicine
- isoniazid
- pharmacology
Reaction
Synonyms
CYP121, EC 1.14.21.9, rv2276
ECTree
1.14.19.70 mycocyclosin synthaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 1.14.19.70 - mycocyclosin synthase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(3S,6S)-3,6-bis(4-hydroxybenzyl)piperazin-2-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
?
cyclo(L-tyrosyl-L-phenylalanyl) + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
?
cyclo(L-tyrosyl-L-tryptophanyl) + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
?
cyclo(L-tyrosyl-L-tyrosyl) + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
mycocyclosin + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
cyclo(L-tyrosyl-L-tyrosyl) + [reduced NADPH-hemoprotein reductase] + O2
mycocyclosin + [oxidized NADPH-hemoprotein reductase] + 2 H2O
cyclo-(L-tyrosyl-DOPA) + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
?
transformation of cyclo-(L-tyrosyl-DOPA) by CYP121 is very slow, 91% of the compound remains after 1 h of incubation with CYP121
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-
?
(3S,6S)-3,6-bis(4-hydroxybenzyl)piperazin-2-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
?
98% of the compound remains after 1 h incubation with CYP121
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-
?
(3S,6S)-3,6-bis(4-hydroxybenzyl)piperazin-2-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
?
98% of the compound remains after 1 h incubation with CYP121
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-
?
cyclo(L-tyrosyl-L-phenylalanyl) + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
?
the rate of transformation of cyclo(L-tyrosyl-L-phenylalanyl) is very slow, with about 98% of compound remaining after 1 h of incubation with CYP121
-
-
?
cyclo(L-tyrosyl-L-phenylalanyl) + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
?
the rate of transformation of cyclo(L-tyrosyl-L-phenylalanyl) is very slow, with about 98% of compound remaining after 1 h of incubation with CYP121
-
-
?
cyclo(L-tyrosyl-L-tryptophanyl) + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
?
about 50% of the initial compound remains after a 1 h incubation with CYP121
-
-
?
cyclo(L-tyrosyl-L-tryptophanyl) + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
?
about 50% of the initial compound remains after a 1 h incubation with CYP121
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-
?
cyclo(L-tyrosyl-L-tyrosyl) + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
mycocyclosin + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
cyclo(L-tyrosyl-L-tyrosyl) + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
mycocyclosin + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
-
?
cyclo(L-tyrosyl-L-tyrosyl) + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
mycocyclosin + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
cyclo(L-tyrosyl-L-tyrosyl) + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
mycocyclosin + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
100% transformation
-
-
?
cyclo(L-tyrosyl-L-tyrosyl) + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
mycocyclosin + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
cyclo(L-tyrosyl-L-tyrosyl) + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
mycocyclosin + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
100% transformation
-
-
?
cyclo(L-tyrosyl-L-tyrosyl) + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
mycocyclosin + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
cyclo(L-tyrosyl-L-tyrosyl) + [reduced NADPH-hemoprotein reductase] + O2
mycocyclosin + [oxidized NADPH-hemoprotein reductase] + 2 H2O
the enzyme is involved in the biosynthesis of mycocyclosin. It is crucial for the viability of this pathogen
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-
?
cyclo(L-tyrosyl-L-tyrosyl) + [reduced NADPH-hemoprotein reductase] + O2
mycocyclosin + [oxidized NADPH-hemoprotein reductase] + 2 H2O
classical and quantum based computer simulation methods are used to study in detail the reaction mechanism. Substrate binding promotes formation of the initial oxy complex. Compound I is responsible for first Tyr radical formation, and that the second Tyr radical is formed subsequently, through a proton-coupled electron transfer reaction, promoted by the presence of key residue Arg386. The final C-C coupling reaction possibly occurs in bulk solution, thus yielding the product in one oxygen reduction cycle
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-
?
cyclo(L-tyrosyl-L-tyrosyl) + [reduced NADPH-hemoprotein reductase] + O2
mycocyclosin + [oxidized NADPH-hemoprotein reductase] + 2 H2O
study of substrate binding kinetics
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-
?
additional information
?
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no activity with cyclo(L-tyrosyl-L-alanyl)
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-
?
additional information
?
-
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no activity with cyclo(L-tyrosyl-L-alanyl)
-
-
?
additional information
?
-
no activity with cyclo(L-tyrosyl-L-alanyl)
-
-
?
