KEGG   ENZYME: 1.14.21.3Help
Entry
EC 1.14.21.3                Enzyme                                 

Name berbamunine synthase;
(S)-N-methylcoclaurine oxidase (C-O phenol-coupling)
Class Oxidoreductases;
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
BRITE hierarchy
Sysname (S)-N-methylcoclaurine,NADPH:oxygen oxidoreductase (C-O
phenol-coupling)
Reaction(IUBMB) (S)-N-methylcoclaurine + (R)-N-methylcoclaurine + NADPH + H+ + O2 =
berbamunine + NADP+ + 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];
NADPH [CPD:C00005];
H+ [CPD:C00080];
O2 [CPD:C00007]
Product berbamunine [CPD:C05177];
NADP+ [CPD:C00006];
H2O [CPD:C00001]
Comment A heme-thiolate enzyme (P-450). 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.
Pathway PATH: ec00950  Isoquinoline alkaloid biosynthesis
Orthology KO: K13387  cytochrome P450, family 80, subfamily A, polypeptide 1
            (berbamunine synthase)
Reference
  Authors
  Title

  Journal
  Organism
1  [PMID:8380416]
Stadler R, Zenk MH.
The purification and characterization of a unique cytochrome P-450
enzyme from Berberis stolonifera plant cell cultures.
J. Biol. Chem. 268 (1993) 823-31.
Berberis stolonifera
Other DBs ExplorEnz - The Enzyme Database: 1.14.21.3
IUBMB Enzyme Nomenclature: 1.14.21.3
ExPASy - ENZYME nomenclature database: 1.14.21.3
BRENDA, the Enzyme Database: 1.14.21.3
CAS: 144941-42-4

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