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

Citation
M. Otagiri et al., Crystal structure of meso-2,3-butanediol dehydrogenase in a complex with NAD(+) and inhibitor mercaptoethanol at 1.7 angstrom resolution for understanding of chiral substrate recognition mechanisms, J BIOCHEM, 129(2), 2001, pp. 205-208
Citations number
24
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Biochemistry & Biophysics
Journal title
JOURNAL OF BIOCHEMISTRY
ISSN journal
0021-924X → ACNP
Volume
129
Issue
2
Year of publication
2001
Pages
205 - 208
Database
ISI
SICI code
0021-924X(200102)129:2<205:CSOMDI>2.0.ZU;2-P
Abstract
The crystal structure of a ternary complex of meso-2,3-butanediol dehydroge nase with NAD(+) and a competitive inhibitor, mercaptoethanol, has been det ermined at 1.7 Angstrom resolution by means of molecular replacement and re fined to a final R-factor of 0.194. The overall structure is similar to tho se of the other short chain dehydrogenase/reductase enzymes. The NAD(+) bin ding site, and the positions of catalytic residues Ser139, Tyr152, and Lys1 56 are also conserved. The crystal structure revealed that mercaptoethanol bound specifically to meso-2,3-butanediol dehydrogenase. Two residues aroun d the active site, GLn140 and Gly183, forming hydrogen bonds with the inhib itor, are important but not sufficient for distinguishing stereoisomerism o f a chiral substrate.