Structural highlights
Function
VESTR_MEDSA Stereospecific enzyme that catalyzes the NADPH-dependent reduction of (3R)-vestitone to (3R,4R)-4'-methoxyisoflavan-2',4,7-triol (DMI). Has no activity with (3S)-vestitone. Catalyzes the penultimate step in the biosynthesis of the phytoalexin medicarpin, and thereby contributes to plant defense reactions.[1] [2] [3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
- ↑ Guo L, Paiva NL. Molecular cloning and expression of alfalfa (Medicago sativa L.) vestitone reductase, the penultimate enzyme in medicarpin biosynthesis. Arch Biochem Biophys. 1995 Jul 10;320(2):353-60. PMID:7625843
- ↑ Guo L, Dixon RA, Paiva NL. 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. 1994 Dec 19;356(2-3):221-5. PMID:7805842
- ↑ Guo L, Dixon RA, Paiva NL. 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. 1994 Sep 2;269(35):22372-8. PMID:8071365
