Amino acid substitutions at glutamate-354 in dihydrolipoamide dehydrogenase of Escherichia coli lower the sensitivity of pyruvate dehydrogenase to NADH-Reference-Cited by-同舟云学术

Amino acid substitutions at glutamate-354 in dihydrolipoamide dehydrogenase of Escherichia coli lower the sensitivity of pyruvate dehydrogenase to NADH

Published:2012-05-01 Issue:5 Volume:158 Page:1350-1358
ISSN:1350-0872
Container-title:Microbiology
language:en
Short-container-title:

Author:

Sun Zhentao¹²,Do Phi Minh¹,Rhee Mun Su¹,Govindasamy Lakshmanan³,Wang Qingzhao¹,Ingram Lonnie O.¹,Shanmugam K. T.¹

Affiliation:

1. Department of Microbiology and Cell Science, University of Florida, Gainesville, FL 32611, USA

2. College of Resources and Environmental Sciences, China Agricultural University, PR China

3. Department of Biochemistry and Molecular Biology, University of Florida, Gainesville, FL 32611, USA

Publisher

Microbiology Society

Subject

Microbiology

Reference37 articles.

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2. Lipoamide Dehydrogenase from Azotobacter vinelandii: site-directed mutagenesis of the His450-Glu455 diad. Spectral properties of wild type and mutated enzymes

3. Substrate specificity of the pyruvate dehydrogenase complex from Escherichia coli;Bisswanger;J Biol Chem,1981

4. Regulatory Properties of the Pyruvate-Dehydrogenase Complex from Escherichia coli. Positive and Negative Cooperativity

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