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.

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 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.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Otagiri M,Kurisu G,Ui S,Takusagawa Y,Ohkuma M,Kudo T,Kusunoki M

doi

10.1093/oxfordjournals.jbchem.a002845

keywords:

subject

Has Abstract

pub_date

2001-02-01 00:00:00

pages

205-8

issue

2

eissn

0021-924X

issn

1756-2651

journal_volume

129

pub_type

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