| Pentalenene oxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.14.15.32 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Pentalenene oxygenase (EC 1.14.15.32, Formerly EC 1.14.13.133, PtlI) is an enzyme with systematic name pentalenene,NADPH:oxygen 13-oxidoreductase.[1] This enzyme catalyses the following chemical reaction
- pentalenene + 2 NADPH + 2 H+ + 2 O2 pentalen-13-al + 2 NADP+ + 3 H2O (overall reaction)
- (1a) pentalenene + NADPH + H+ + O2 pentalen-13-ol + NADP+ + H2O
- (1b) pentalen-13-ol + NADPH + H+ + O2 pentalen-13-al + NADP+ + 2 H2O
Pentalenene oxygenase is a heme-thiolate protein (P-450).
References[edit]
- ^ Quaderer R, Omura S, Ikeda H, Cane DE (October 2006). "Pentalenolactone biosynthesis. Molecular cloning and assignment of biochemical function to PtlI, a cytochrome P450 of Streptomyces avermitilis". Journal of the American Chemical Society. 128 (40): 13036–7. doi:10.1021/ja0639214. PMC 2533730. PMID 17017767.
External links[edit]
- Pentalenene+oxygenase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
