The Enzyme Database

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EC 1.1.1.348     
Accepted name: (3R)-2′-hydroxyisoflavanone reductase
Reaction: a (4R)-4,2′-dihydroxyisoflavan + NADP+ = a (3R)-2′-hydroxyisoflavanone + NADPH + H+
For diagram of medicarpin and formononetin derivatives biosynthesis, click here
Glossary: (3R)-vestitone = (3R)-2′,7-dihydroxy-4′-methoxyisoflavanone
Other name(s): vestitone reductase; pterocarpin synthase (incorrect); pterocarpan synthase (incorrect)
Systematic name: (3R)-2′-hydroxyisoflavanone:NADP+ 4-oxidoreductase
Comments: This plant enzyme participates in the biosynthesis of the pterocarpan phytoalexins medicarpin, maackiain, and several forms of glyceollin. The ezyme has a strict stereo specificity for the 3R-isoflavanones.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 118477-70-6
References:
1.  Bless, W. and Barz, W. Isolation of pterocarpan synthase, the terminal enzyme of pterocarpan phytoalexin biosynthesis in cell-suspension cultures of Cicer arietinum. FEBS Lett. 235 (1988) 47–50.
2.  Guo, L., Dixon, R.A. and Paiva, N.L. Conversion of vestitone to medicarpin in alfalfa (Medicago sativa L.) is catalyzed by two independent enzymes. Identification, purification, and characterization of vestitone reductase and 7,2′-dihydroxy-4′-methoxyisoflavanol dehydratase. J. Biol. Chem. 269 (1994) 22372–22378. [PMID: 8071365]
3.  Guo, L., Dixon, R.A. and Paiva, N.L. The ‘pterocarpan synthase’ of alfalfa: association and co-induction of vestitone reductase and 7,2′-dihydroxy-4′-methoxy-isoflavanol (DMI) dehydratase, the two final enzymes in medicarpin biosynthesis. FEBS Lett. 356 (1994) 221–225. [PMID: 7805842]
4.  Guo, L. and Paiva, N.L. Molecular cloning and expression of alfalfa (Medicago sativa L.) vestitone reductase, the penultimate enzyme in medicarpin biosynthesis. Arch. Biochem. Biophys. 320 (1995) 353–360. [PMID: 7625843]
5.  Shao, H., Dixon, R.A. and Wang, X. Crystal structure of vestitone reductase from alfalfa (Medicago sativa L.). J. Mol. Biol. 369 (2007) 265–276. [PMID: 17433362]
[EC 1.1.1.348 created 1992 as EC 1.1.1.246, part transferred 2013 to EC 1.1.1.348]
 
 


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