KEGG   ENZYME: 1.14.19.67Help
Entry
EC 1.14.19.67               Enzyme                                 

Name
salutaridine synthase;
(R)-reticuline oxidase (C-C 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
(R)-reticuline,[reduced NADPH---hemoprotein reductase]:oxygen oxidoreductase (C-C phenol-coupling)
Reaction(IUBMB)
(R)-reticuline + [reduced NADPH---hemoprotein reductase] + O2 = salutaridine + [oxidized NADPH---hemoprotein reductase] + 2 H2O [RN:R04696]
Reaction(KEGG)
Substrate
(R)-reticuline [CPD:C05178];
[reduced NADPH---hemoprotein reductase] [CPD:C03024];
O2 [CPD:C00007]
Product
salutaridine [CPD:C05179];
[oxidized NADPH---hemoprotein reductase] [CPD:C03161];
H2O [CPD:C00001]
Comment
A cytochrome P-450 (heme-thiolate) protein found in plants. Forms the morphinan alkaloid salutaridine by intramolecular phenol oxidation of reticuline without the incorporation of oxygen into the product.
History
EC 1.14.19.67 created 1999 as EC 1.1.3.35, transferred 2002 to EC 1.14.21.4, transferred 2018 to EC 1.14.19.67
Pathway
ec00950  Isoquinoline alkaloid biosynthesis
ec01100  Metabolic pathways
ec01110  Biosynthesis of secondary metabolites
Orthology
K13391  salutaridine synthase
Genes
PSOM: 113321914
Taxonomy
Reference
1
  Authors
Gerady, R. and Zenk, M.H.
  Title
Formation of salutaridine from (R)-reticuline by a membrane-bound cytochrome P-450 enzyme from Papaver somniferum.
  Journal
Phytochemistry 32:79-86 (1993)
Other DBs
ExplorEnz - The Enzyme Database: 1.14.19.67
IUBMB Enzyme Nomenclature: 1.14.19.67
ExPASy - ENZYME nomenclature database: 1.14.19.67
BRENDA, the Enzyme Database: 1.14.19.67
CAS: 149433-84-1

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