KEGG   ENZYME: 1.14.14.141
Entry
EC 1.14.14.141              Enzyme                                 

Name
psoralen synthase;
CYP71AJ1
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor
Sysname
(+)-marmesin,[reduced NADPH---hemoprotein reductase]:oxygen oxidoreductase
Reaction(IUBMB)
(+)-marmesin + [reduced NADPH---hemoprotein reductase] + O2 = psoralen + [oxidized NADPH---hemoprotein reductase] + acetone + 2 H2O [RN:R08207]
Reaction(KEGG)
R08207
Substrate
(+)-marmesin [CPD:C09276];
[reduced NADPH---hemoprotein reductase] [CPD:C03024];
O2 [CPD:C00007]
Product
psoralen [CPD:C09305];
[oxidized NADPH---hemoprotein reductase] [CPD:C03161];
acetone [CPD:C00207];
H2O [CPD:C00001]
Comment
This microsomal cytochrome P-450 (heme-thiolate) enzyme is rather specific for (+)-marmesin, although it can also accept 5-hydroxymarmesin to a much lesser extent. Furanocoumarins protect plants from fungal invasion and herbivore attack. (+)-Columbianetin, the angular furanocoumarin analogue of the linear furanocoumarin (+)-marmesin, acts as a competitive inhibitor even though it is not a substrate.
History
EC 1.14.14.141 created 2007 as EC 1.14.13.102, transferred 2018 to EC 1.14.14.141
Orthology
K21714  psoralen synthase
Reference
1  [PMID:17068340]
  Authors
Larbat R, Kellner S, Specker S, Hehn A, Gontier E, Hans J, Bourgaud F, Matern U.
  Title
Molecular cloning and functional characterization of psoralen synthase, the first committed monooxygenase of furanocoumarin biosynthesis.
  Journal
J Biol Chem 282:542-54 (2007)
DOI:10.1074/jbc.M604762200
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 1.14.14.141
IUBMB Enzyme Nomenclature: 1.14.14.141
ExPASy - ENZYME nomenclature database: 1.14.14.141
BRENDA, the Enzyme Database: 1.14.14.141

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