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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