| berbamunine synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.14.19.66 | ||||||||
| CAS no. | 144941-42-4 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a berbamunine synthase (EC 1.14.19.66, Formerly EC 1.1.3.34 and EC 1.14.21.3) is an enzyme that catalyzes the chemical reaction
- (S)-N-methylcoclaurine + (R)-N-methylcoclaurine + NADPH + H+ + O2 berbamunine + NADP+ + 2 H2O
The 5 substrates of this enzyme are (S)-N-methylcoclaurine, (R)-N-methylcoclaurine, NADPH, H+, and O2, whereas its 3 products are berbamunine, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and the other dehydrogenated. The systematic name of this enzyme class is (S)-N-methylcoclaurine,NADPH:oxygen oxidoreductase (C-O phenol-coupling). This enzyme is also called (S)-N-methylcoclaurine oxidase (C-O phenol-coupling). This enzyme participates in alkaloid biosynthesis i.
References
- Stadler R, Zenk MH (1993). "The purification and characterization of a unique cytochrome P-450 enzyme from Berberis stolonifera plant cell cultures". J. Biol. Chem. 268 (2): 823–31. PMID 8380416.