Methyltetrahydroprotoberberine 14-monooxygenase
| methyltetrahydroprotoberberine 14-monooxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.14.13.37 | ||||||||
| CAS number | 113478-42-5 | ||||||||
| 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 / EGO | ||||||||
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In enzymology, a methyltetrahydroprotoberberine 14-monooxygenase (EC 1.14.13.37) is an enzyme that catalyzes the chemical reaction
- (S)-N-methylcanadine + NADPH + H+ + O2 allocryptopine + NADP+ + H2O
The 4 substrates of this enzyme are (S)-N-methylcanadine, NADPH, H+, and O2, whereas its 3 products are allocryptopine, 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 incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is (S)-N-methylcanadine,NADPH:oxygen oxidoreductase (14-hydroxylating). Other names in common use include methyltetrahydroprotoberberine 14-hydroxylase, (S)-cis-N-methyltetrahydroberberine 14-monooxygenase, and (S)-cis-N-methyltetrahydroprotoberberine-14-hydroxylase. This enzyme participates in alkaloid biosynthesis i. It employs one cofactor, heme.
References
- Rueffer M; Zenk MH (1987). "Enzymatic formation of protopines by a microsomal cytochrome-P-450 system of Corydalis vaginans". Tetrahedron Lett. 28 (44): 5307–5310. doi:10.1016/S0040-4039(00)96715-7.