Journal
JOURNAL OF BIOCHEMISTRY
Volume 129, Issue 2, Pages 205-208Publisher
OXFORD UNIV PRESS
DOI: 10.1093/oxfordjournals.jbchem.a002845
Keywords
butanediol dehydrogenase; chiral recognition; crystal structure; Klebsiella pneumoniae; short-chain dehydrogenase/reductase family; stereoisomer
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The crystal structure of a ternary complex of meso-2,3-butanediol dehydrogenase with NAD(+) and a competitive inhibitor, mercaptoethanol, has been determined at 1.7 Angstrom resolution by means of molecular replacement and refined to a final R-factor of 0.194. The overall structure is similar to those of the other short chain dehydrogenase/reductase enzymes. The NAD(+) binding site, and the positions of catalytic residues Ser139, Tyr152, and Lys156 are also conserved. The crystal structure revealed that mercaptoethanol bound specifically to meso-2,3-butanediol dehydrogenase. Two residues around the active site, GLn140 and Gly183, forming hydrogen bonds with the inhibitor, are important but not sufficient for distinguishing stereoisomerism of a chiral substrate.
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