Beta-amyrin 11-oxidase
Class of enzymes
| Beta-amyrin 11-oxidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.14.13.134 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Beta-amyrin 11-oxidase (EC 1.14.13.134, CYP88D6) is an enzyme with systematic name beta-amyrin,NADPH:oxygen oxidoreductase (hydroxylating).[1] This enzyme catalyses the following chemical reaction
- beta-amyrin + 2 O2 + 2 NADPH + 2 H+ 11-oxo-beta-amyrin + 3 H2O + 2 NADP+ (overall reaction)
- (1a) beta-amyrin + O2 + NADPH + H+ 11alpha-hydroxy-beta-amyrin + H2O + NADP+
- (1b) 11alpha-hydroxy-beta-amyrin + O2 + NADPH + H+ 11-oxo-beta-amyrin + 2 H2O + NADP+
Beta-amyrin 11-oxidase requires cytochrome P450.
References
- ^ Seki H, Ohyama K, Sawai S, Mizutani M, Ohnishi T, Sudo H, Akashi T, Aoki T, Saito K, Muranaka T (September 2008). "Licorice beta-amyrin 11-oxidase, a cytochrome P450 with a key role in the biosynthesis of the triterpene sweetener glycyrrhizin". Proceedings of the National Academy of Sciences of the United States of America. 105 (37): 14204–9. Bibcode:2008PNAS..10514204S. doi:10.1073/pnas.0803876105. PMC 2532699. PMID 18779566.
External links
- Beta-amyrin+11-oxidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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