Simulation of the Enzyme Reaction Mechanism of Malate Dehydrogenase-Reference-Cited by-同舟云学术

Simulation of the Enzyme Reaction Mechanism of Malate Dehydrogenase

Published:1997-04-01 Issue:16 Volume:36 Page:4800-4816
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Cunningham Mark A.¹,Ho L. Lawrence¹,Nguyen Dzung T.¹,Gillilan Richard E.¹,Bash Paul A.¹

Affiliation:

1. Center for Mechanistic Biology and Biotechnology, Argonne National Laboratory, Argonne, Illinois 60439, M. A. Cunningham Associates, Northbrook, Illinois 60062, J. W. Gibbs Laboratory, Department of Physics, Yale University, New Haven, Connecticut 06511, InPharmatics Corporation, San Diego, California 92126, and Cornell Theory Center, Cornell University, Ithaca, New York 14853

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi962734n

Reference58 articles.

1. Free-energy profile for the reaction catalyzed by triosephosphate isomerase

2. Evolution of enzyme function and the development of catalytic efficiency

3. Theoretical kinetic isotope effects for the hydride-transfer step in lactate dehydrogenase

4. Calculation of the Relative Change in Binding Free Energy of a Protein-Inhibitor Complex

5. Free energy perturbation method for chemical reactions in the condensed phase: a dynamic approach based on a combined quantum and molecular mechanics potential

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