CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.10 | Orthogonal Bundle |
|
1.10.630 | Cytochrome p450 |
|
1.10.630.10 | Cytochrome P450 |
Domain Context
CATH Clusters
| Superfamily | Cytochrome P450 |
| Functional Family | Erythromycin C-12 hydroxylase |
Enzyme Information
| 1.14.13.154 |
Erythromycin 12 hydroxylase.
based on mapping to UniProt P48635
Erythromycin D + NADPH + O(2) = erythromycin C + NADP(+) + H(2)O.
-!- The enzyme is responsible for the C-12 hydroxylation of the macrolactone ring, one of the last steps in erythromycin biosynthesis. -!- It shows 1200-1900-fold preference for erythromycin D over the alternative substrate erythromycin B.
|
UniProtKB Entries (1)
| P48635 |
ERYK_SACEN
Saccharopolyspora erythraea NRRL 2338
Erythromycin C-12 hydroxylase
|
PDB Structure
| PDB | 2XFH |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Azole Drugs Trap Cytochrome P450 Eryk in Alternative Conformational States.
Biochemistry
|