Crystal structure of meso-2,3-butanediol dehydrogenase in a complex with NAD+ and inhibitor mercaptoethanol at 1.7 A resolution for understanding of chiral substrate recognition mechanisms

J Biochem. 2001 Feb;129(2):205-8. doi: 10.1093/oxfordjournals.jbchem.a002845.


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 A 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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alcohol Oxidoreductases / chemistry*
  • Alcohol Oxidoreductases / metabolism
  • Crystallization*
  • In Vitro Techniques
  • Klebsiella pneumoniae / enzymology
  • Mercaptoethanol / antagonists & inhibitors
  • Mercaptoethanol / chemistry*
  • NAD / chemistry*
  • NAD / metabolism
  • Stereoisomerism
  • Substrate Specificity


  • NAD
  • Mercaptoethanol
  • Alcohol Oxidoreductases
  • butanol dehydrogenase