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 |
Enzyme Information
| 1.14.14.46 |
Pimeloyl-[acyl-carrier protein] synthase.
based on mapping to UniProt P53554
A long-chain acyl-[acyl-carrier protein] + 2 reduced flavodoxin + 3 O(2) = pimeloyl-[acyl-carrier protein] + an n-alkanal + 2 oxidized flavodoxin + 3 H(2)O.
-!- Catalyzes an oxidative C-C bond cleavage of long-chain acyl-[acyl- carrier protein]s of various lengths to generate pimeloyl-[acyl- carrier protein], an intermediate in the biosynthesis of biotin. -!- The preferred substrate of the enzyme from the bacterium Bacillus subtilis is palmitoyl-[acyl-carrier protein] which then gives heptanal as the alkanal. -!- The mechanism is similar to EC 1.14.15.6, followed by a hydroxylation step, which may occur spontaneously. -!- Formerly EC 1.14.15.12.
|
UniProtKB Entries (2)
| P53554 |
BIOI_BACSU
Bacillus subtilis subsp. subtilis str. 168
Biotin biosynthesis cytochrome P450
|
| P0A6A8 |
ACP_ECOLI
Escherichia coli K-12
Acyl carrier protein
|
PDB Structure
| PDB | 3EJE |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structural insights from a P450 Carrier Protein complex reveal how specificity is achieved in the P450(BioI) ACP complex.
Proc.Natl.Acad.Sci.Usa
|
