Hydride Transfer in DHFR by Transition Path Sampling, Kinetic Isotope Effects, and Heavy Enzyme Studies-Reference-Cited by-同舟云学术

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

Published:2015-12-23 Issue:1 Volume:55 Page:157-166
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Wang Zhen¹,Antoniou Dimitri²,Schwartz Steven D.²,Schramm Vern L.¹

Affiliation:

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

2. Department of Chemistry and Biochemistry, University of Arizona, P.O. Box 210041, 1306 East University Boulevard, Tucson, Arizona 85721, United States

Funder

National Institute of General Medical Sciences

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.5b01241

Reference52 articles.

1. Network of coupled promoting motions in enzyme catalysis

2. Impact of distal mutations on the network of coupled motions correlated to hydride transfer in dihydrofolate reductase

3. Connecting Protein Conformational Dynamics with Catalytic Function As Illustrated in Dihydrofolate Reductase

4. Simulations of remote mutants of dihydrofolate reductase reveal the nature of a network of residues coupled to hydride transfer

5. Protein Mass-Modulated Effects in the Catalytic Mechanism of Dihydrofolate Reductase: Beyond Promoting Vibrations

Cited by 33 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Mutexa: A Computational Ecosystem for Intelligent Protein Engineering;Journal of Chemical Theory and Computation;2023-10-13

2. Protein Dynamics and Enzymatic Catalysis;J PHYS CHEM B;2023

3. Protein Dynamics and Enzymatic Catalysis;The Journal of Physical Chemistry B;2023-03-21

4. Perspective: Path Sampling Methods Applied to Enzymatic Catalysis;Journal of Chemical Theory and Computation;2022-10-28

5. Comparison of the Role of Protein Dynamics in Catalysis by Dihydrofolate Reductase from E. coli and H. sapiens;The Journal of Physical Chemistry B;2022-09-07