Journal
FEBS LETTERS
Volume 584, Issue 1, Pages 219-223Publisher
WILEY
DOI: 10.1016/j.febslet.2009.11.068
Keywords
Butanediol dehydrogenase; Chiral recognition; Stereoisomer; Short-chain dehydrogenase/reductase family; X-ray crystallography
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2,3-Butanediol dehydrogenase (BDH) catalyzes the NAD-dependent redox reaction between acetoin and 2,3-butanediol. There are three types of homologous BDH, each stereospecific for both substrate and product. To establish how these homologous enzymes possess differential stereospecificities, we determined the crystal structure of L-BDH with a bound inhibitor at 2.0 angstrom. Comparison with the inhibitor binding mode of meso-BDH highlights the role of a hydrogen-bond from a conserved Trp residue(192). Site-directed mutagenesis of three active site residues of meso-BDH, including Trp(190), which corresponds to Trp(192) of L-BDH, converted its stereospecificity to that of L-BDH. This result confirms the importance of conserved residues in modifying the stereospeci. city of homologous enzymes. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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