Distinct Conformation-mediated Functions of an Active Site Loop in the Catalytic Reactions of NAD-dependent D-Lactate Dehydrogenase and Formate Dehydrogenase-Reference-Cited by-同舟云学术

Distinct Conformation-mediated Functions of an Active Site Loop in the Catalytic Reactions of NAD-dependent D-Lactate Dehydrogenase and Formate Dehydrogenase

Published:2005-04 Issue:17 Volume:280 Page:17068-17075
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Shinoda Takeshi,Arai Kazuhito,Shigematsu-Iida Mayu,Ishikura Yoshirou,Tanaka Satoru,Yamada Takashi,Kimber Matthew S.,Pai Emil F.,Fushinobu Shinya,Taguchi Hayao

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference64 articles.

1. D-lactate dehydrogenase is a member of the D-isomer-specific 2-hydroxyacid dehydrogenase family. Cloning, sequencing, and expression in Escherichia coli of the D-lactate dehydrogenase gene of Lactobacillus plantarum

2. Cloning of the D-lactate dehydrogenase gene fromLactobacillus delbrueckiisubsp.bulgaricusby complementation inEscherichia coli

3. Primary structure, physicochemical properties, and chemical modification of NAD(+)-dependent D-lactate dehydrogenase. Evidence for the presence of Arg-235, His-303, Tyr-101, and Trp-19 at or near the active site.

4. Glutamate 264 modulates the pH dependence of the NAD(+)-dependent D-lactate dehydrogenase.

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