Structural highlights
Function
[IFR_MEDSA] Reduces achiral isoflavones to chiral isoflavanones during the biosynthesis of chiral pterocarpan phytoalexins. The reduction product is a third isomer, which represents the penultimate intermediate in the synthesis of the phytoalexin (-)-medicarpin, the major phytoalexin in Alfalfa.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Isoflavonoids play important roles in plant defense and exhibit a range of mammalian health-promoting activities. Isoflavone reductase (IFR) specifically recognizes isoflavones and catalyzes a stereospecific NADPH-dependent reduction to (3R)-isoflavanone. The crystal structure of Medicago sativa IFR with deletion of residues 39-47 has been determined at 1.6A resolution. Structural analysis, molecular modeling and docking, and comparison with the structures of other NADPH-dependent enzymes, defined the putative binding sites for co-factor and substrate and potential key residues for enzyme activity and substrate specificity. Further mutagenesis has confirmed the role of Lys144 as a catalytic residue. This study provides a structural basis for understanding the enzymatic mechanism and substrate specificity of IFRs as well as the functions of IFR-like proteins.
Crystal structure of isoflavone reductase from alfalfa (Medicago sativa L.).,Wang X, He X, Lin J, Shao H, Chang Z, Dixon RA J Mol Biol. 2006 May 19;358(5):1341-52. Epub 2006 Mar 29. PMID:16600295[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wang X, He X, Lin J, Shao H, Chang Z, Dixon RA. Crystal structure of isoflavone reductase from alfalfa (Medicago sativa L.). J Mol Biol. 2006 May 19;358(5):1341-52. Epub 2006 Mar 29. PMID:16600295 doi:10.1016/j.jmb.2006.03.022
