Cofactor-Mediated Conformational Dynamics Promote Product Release From Escherichia coli Dihydrofolate Reductase via an Allosteric Pathway-Reference-Cited by-同舟云学术

Cofactor-Mediated Conformational Dynamics Promote Product Release From Escherichia coli Dihydrofolate Reductase via an Allosteric Pathway

Published:2015-07-14 Issue:29 Volume:137 Page:9459-9468
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Oyen David¹,Fenwick R. Bryn¹,Stanfield Robyn L.¹,Dyson H. Jane¹,Wright Peter E.¹

Affiliation:

1. Department of Integrative Structural and Computational Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, United States

Funder

Belgian American Educational Foundation

National Institute of General Medical Sciences

Skaggs Institute of Chemical Biology, Scripps Research Institute

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/jacs.5b05707

Reference61 articles.

1. What limits the rate of an enzyme-catalyzed reaction

2. The time scale of the catalytic loop motion in triosephosphate isomerase11Edited by P. E. Wright

3. An NMR Perspective on Enzyme Dynamics

4. The Dynamic Energy Landscape of Dihydrofolate Reductase Catalysis

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