Mechanistic aspects of biological redox reactions involving NADH. Part 5.—AM1 transition-state studies for the pyruvate–L-lactate interconversion inL-lactate dehydrogenase-Reference-Cited by-同舟云学术

Mechanistic aspects of biological redox reactions involving NADH. Part 5.—AM1 transition-state studies for the pyruvate–L-lactate interconversion inL-lactate dehydrogenase

Published:1994 Issue:14 Volume:90 Page:2047-2056
ISSN:0956-5000
Container-title:J. Chem. Soc., Faraday Trans.
language:en
Short-container-title:J. Chem. Soc., Faraday Trans.

Author:

Ranganathan Shoba,Gready Jill E.

Publisher

Royal Society of Chemistry (RSC)

Subject

Physical and Theoretical Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/1994/FT/FT9949002047

Reference35 articles.

1. From analysis to synthesis: new ligand binding sites on the lactate dehydrogenase framework. Part I

2. Design and synthesis of new enzymes based on the lactate dehydrogenase framework

3. J. J. Holbrook , A.Liljas, S. J.Steindel and M. G.Rossmann, in The Enzymes, ed. P. D. Boyer, Academic Press, New York, 2nd edn., 1975, vol. 11, p. 191.

4. Site-directed mutagenesis reveals role of mobile arginine residue in lactate dehydrogenase catalysis

5. The importance of arginine 171 in substrate binding by Bacillus stearothermophilus lactate dehydrogenase

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