EC Number | Cloned (Comment) | Organism |
---|---|---|
1.14.15.36 | expression in Escherichia coli | Mycobacterium tuberculosis |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.14.15.36 | Iron | - |
Mycobacterium tuberculosis |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.15.36 | estriol + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+ + 3 O2 | Mycobacterium tuberculosis | - |
? + formate + 6 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O | - |
? | |
1.14.15.36 | estriol + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+ + 3 O2 | Mycobacterium tuberculosis H37Rv | - |
? + formate + 6 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.14.15.36 | Mycobacterium tuberculosis | P9WPP9 | - |
- |
1.14.15.36 | Mycobacterium tuberculosis H37Rv | P9WPP9 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.14.15.36 | recombinant protein | Mycobacterium tuberculosis |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.15.36 | estriol + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+ + 3 O2 | - |
Mycobacterium tuberculosis | ? + formate + 6 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O | - |
? | |
1.14.15.36 | estriol + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+ + 3 O2 | - |
Mycobacterium tuberculosis H37Rv | ? + formate + 6 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.14.15.36 | CYP51 | - |
Mycobacterium tuberculosis |
1.14.15.36 | sterol demethylase 450 | - |
Mycobacterium tuberculosis |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.14.15.36 | Ferredoxin | - |
Mycobacterium tuberculosis | |
1.14.15.36 | heme | heme-iron reduction is the rate limiting step in catalysis. Protonation of the cysteinate ligand to the ferrous CYP51 underlies the collapse of the Fe(II)-CO adduct of the enzyme from its P450 to its P420 form. The protonation is reversible and the rate of P420 formation is substantially retarded in the estriol-bound form of CYP51 | Mycobacterium tuberculosis |