KEGG   ENZYME: 1.14.19.66Help
Entry
EC 1.14.19.66               Enzyme                                 

Name
berbamunine synthase;
(S)-N-methylcoclaurine oxidase (C-O phenol-coupling)
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With oxidation of a pair of donors resulting in the reduction of O2 to two molecules of water
BRITE hierarchy
Sysname
(S)-N-methylcoclaurine,[reduced NADPH---hemoprotein reductase]:oxygen oxidoreductase (C-O phenol-coupling)
Reaction(IUBMB)
(S)-N-methylcoclaurine + (R)-N-methylcoclaurine + [reduced NADPH---hemoprotein reductase] + O2 = berbamunine + [oxidized NADPH---hemoprotein reductase] + 2 H2O [RN:R04694]
Reaction(KEGG)
R04694;
(other) R05210 R05215
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Substrate
(S)-N-methylcoclaurine [CPD:C05176];
(R)-N-methylcoclaurine [CPD:C05243];
[reduced NADPH---hemoprotein reductase] [CPD:C03024];
O2 [CPD:C00007]
Product
berbamunine [CPD:C05177];
[oxidized NADPH---hemoprotein reductase] [CPD:C03161];
H2O [CPD:C00001]
Comment
A cytochrome P-450 (heme-thiolate) protein found in plants. Forms the bisbenzylisoquinoline alkaloid berbamunine by phenol oxidation of N-methylcoclaurine without the incorporation of oxygen into the product. Reaction of two molecules of (R)-N-methylcoclaurine gives the dimer guattagaumerine.
History
EC 1.14.19.66 created 1999 as EC 1.1.3.34, transferred 2002 to EC 1.14.21.3, transferred 2018 to EC 1.14.19.66
Pathway
ec00950  Isoquinoline alkaloid biosynthesis
Orthology
K13387  berbamunine synthase
Reference
1  [PMID:8380416]
  Authors
Stadler R, Zenk MH.
  Title
The purification and characterization of a unique cytochrome P-450 enzyme from Berberis stolonifera plant cell cultures.
  Journal
J Biol Chem 268:823-31 (1993)
Other DBs
ExplorEnz - The Enzyme Database: 1.14.19.66
IUBMB Enzyme Nomenclature: 1.14.19.66
ExPASy - ENZYME nomenclature database: 1.14.19.66
BRENDA, the Enzyme Database: 1.14.19.66
CAS: 144941-42-4

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