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- Title
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 Mechanisms1.
- Authors
Otagiri, Masato; Kurisu, Genji; Ui, Sadaharu; Takusagawa, Yusuke; Ohkuma, Moriya; Kudo, Toshiaki; Kusunoki, Masami
- Abstract
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 Å 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, Tyrl52, 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, Glnl40 and Glyl83, forming hydrogen bonds with the inhibitor, are important but not sufficient for distinguishing stereoisomerism of a chiral substrate.
- Subjects
PROTEINS; BUTANEDIOL; DEHYDROGENASES; MOLECULAR structure; PROTEOMICS
- Publication
Journal of Biochemistry, 2001, Vol 129, Issue 2, p205
- ISSN
0021-924X
- Publication type
Article
- DOI
10.1093/oxfordjournals.jbchem.a002845