Why Does the G117H Mutation Considerably Improve the Activity of Human Butyrylcholinesterase against Sarin? Insights from Quantum Mechanical/Molecular Mechanical Free Energy Calculations-Reference-Cited by-同舟云学术

Why Does the G117H Mutation Considerably Improve the Activity of Human Butyrylcholinesterase against Sarin? Insights from Quantum Mechanical/Molecular Mechanical Free Energy Calculations

Published:2012-10-23 Issue:44 Volume:51 Page:8980-8992
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Yao Yuan¹²,Liu Junjun¹³,Zhan Chang-Guo¹

Affiliation:

1. Department of Pharmaceutical Sciences, College of Pharmacy, University of Kentucky, 789 South Limestone Street, Lexington, Kentucky 40536, United States

2. The Academy of Fundamental and Interdisciplinary Sciences, Harbin Institute of Technology, Harbin 150080, P. R. China

3. Tongji School of Pharmacy, Huazhong University of Science and Technology, 13 Hangkong Road, Wuhan, Hubei 430030, P. R. China

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi3009246

Reference68 articles.

1. Primary structures of the catalytic subunits from two molecular forms of acetylcholinesterase. A comparison of NH2-terminal and active center sequences.

2. Organophosphate poisoning

3. Structural bases for the specificity of cholinesterase catalysis and inhibition