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Literature summary for 1.14.14.16 extracted from
- Interaction between substrate and oxygen ligand responsible for effective O-O bond cleavage in bovine cytochrome P450 steroid 21-hydroxylase proved by Raman spectroscopy (2008), J. Biol. Chem., 283, 3708-3717.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Escherichia coli | Bos taurus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bos taurus | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Bos taurus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 17alpha-hydroxyprogesterone + NADPH + H+ + O2 | P450c21 catalyzes hydroxylation at C-21, 17alpha-hydroxyprogesterone is a better substrate for P450c21 than progesterone from the catalytic coupling with consumption of NADPH | Bos taurus | 11-deoxycortisol + NADP+ + H2O | - |
? |  |
| progesterone + NADPH + H+ + O2 | P450c21 catalyzes hydroxylation at C-21 | Bos taurus | 11-deoxycorticosterone + NADP+ + H2O | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| cytochrome P450 steroid 21-hydroxylase | - |
Bos taurus |
| P450c21 | - |
Bos taurus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| cytochrome P450 | - |
Bos taurus | |
| NADPH | - |
Bos taurus | |
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Release 2023.1 (January 2023)
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