Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 358, Issue 5, Pages 1341-1352Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2006.03.022
Keywords
isoflavone reductase; Medicago sativa; crystal structure; isoflavonoid; stereospecificity
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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)-isoflavanon. The crystal structure of Medicago sativa IFR with deletion of residues 39-47 has been determined at 1.6 angstrom 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. (c) 2006 Elsevier Ltd. All rights reserved.
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