QM/MM Molecular Dynamics Investigations of the Substrate Binding of Leucotriene A4 Hydrolase: Implication for the Catalytic Mechanism
Author:
Affiliation:
1. MOE Key Laboratory of Green Chemistry and Technology, College of Chemistry, Sichuan University, Chengdu, Sichuan, People’s Republic of China 610064
Funder
Ministry of Science and Technology of the People's Republic of China
National Natural Science Foundation of China
Publisher
American Chemical Society (ACS)
Subject
Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.jpcb.8b04203
Reference61 articles.
1. Albumins activate peptide hydrolysis by the bifunctional enzyme LTA4 hydrolase/aminopeptidase
2. Mechanism-based inactivation of leukotriene A4 hydrolase/aminopeptidase by leukotriene A4. Mass spectrometric and kinetic characterization
3. Leukotriene A4 hydrolase
4. Leukotriene A4 Hydrolase/Aminopeptidase, the Gatekeeper of Chemotactic Leukotriene B4 Biosynthesis
5. Leukotriene A4 Hydrolase as a Target for Cancer Prevention and Therapy
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1. Quantum Mechanical/Molecular Mechanical Elucidation of the Catalytic Mechanism of Leukotriene A4 Hydrolase as an Epoxidase;The Journal of Physical Chemistry B;2023-11-27
2. Theoretical Characterization of the Step-by-Step Mechanism of Conversion of Leukotriene A4 to Leukotriene B4 Catalysed by the Enzyme Leukotriene A4 Hydrolase;International Journal of Molecular Sciences;2022-03-15
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