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Modulating Enzyme Catalysis through Mutations Designed to Alter Rapid Protein Dynamics

Published:2016-03-08 Issue:10 Volume:138 Page:3403-3409
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Zoi Ioanna¹,Suarez Javier²,Antoniou Dimitri¹,Cameron Scott A.²,Schramm Vern L.²,Schwartz Steven D.¹

Affiliation:

1. Department of Chemistry and Biochemistry, University of Arizona, 1306 East University Blvd, Tucson, Arizona 85721, United States

2. Department of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Ave, Bronx, New York 10461, United States

Funder

National Institute of General Medical Sciences

Argonne National Laboratory, Office of Science

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/jacs.5b12551

Reference35 articles.

1. Topics in Current Chemistry;Klinman J.,2013

2. Enzymatic transition states and dynamic motion in barrier crossing

3. Barrier crossing in dihydrofolate reductase does not involve a rate-promoting vibration

4. Hydride Transfer in DHFR by Transition Path Sampling, Kinetic Isotope Effects, and Heavy Enzyme Studies

5. Are there dynamical effects in enzyme catalysis? Some thoughts concerning the enzymatic chemical step

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