The Enzyme Database

Your query returned 3 entries.    printer_iconPrintable version

EC 1.14.13.102      
Transferred entry: psoralen synthase. Now EC 1.14.14.141, psoralen synthase
[EC 1.14.13.102 created 2007, deleted 2018]
 
 
EC 1.14.14.66     
Accepted name: marmesin synthase
Reaction: demethylsuberosin + [reduced NADPH—hemoprotein reductase] + O2 = (+)-marmesin + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of psoralen biosynthesis, click here
Glossary: demethylsuberosin = 7-hydroxy-6-prenyl-1-benzopyran-2-one
(+)-marmesin = (S)-2-(2-hydroxypropan-2-yl)-2,3-dihydro-7H-furo[3,2-g]chromen-7-one
Systematic name: demethylsuberosin,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase
Comments: A P-450 monoxygenase involved in psoralen biosynthesis, see EC 1.14.13.102, psoralen synthase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Hamerski, D. and Matern, U. Elicitor-induced biosynthesis of psoralens in Ammi majus L. suspension cultures. Microsomal conversion of demethylsuberosin into (+)marmesin and psoralen. Eur. J. Biochem. 171 (1988) 369–375. [PMID: 2828055]
[EC 1.14.14.66 created 2018]
 
 
EC 1.14.14.141     
Accepted name: psoralen synthase
Reaction: (+)-marmesin + [reduced NADPH—hemoprotein reductase] + O2 = psoralen + [oxidized NADPH—hemoprotein reductase] + acetone + 2 H2O
For diagram of reaction, click here
Glossary: (+)-marmesin = (S)-2-(2-hydroxypropan-2-yl)-2,3-dihydro-7H-furo[3,2-g]chromen-7-one
psoralen = 7H-furo[3,2-g]chromen-7-one
Other name(s): CYP71AJ1
Systematic name: (+)-marmesin,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase
Comments: 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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Larbat, R., Kellner, S., Specker, S., Hehn, A., Gontier, E., Hans, J., Bourgaud, F. and Matern, U. Molecular cloning and functional characterization of psoralen synthase, the first committed monooxygenase of furanocoumarin biosynthesis. J. Biol. Chem. 282 (2007) 542–554. [DOI] [PMID: 17068340]
[EC 1.14.14.141 created 2007 as EC 1.14.13.102, transferred 2018 to EC 1.14.14.141]
 
 


Data © 2001–2024 IUBMB
Web site © 2005–2024 Andrew McDonald