Specific base catalysis by yeast alcohol dehydrogenase I with substitutions of histidine-48 by glutamate or serine residues in the proton relay system-Reference-Cited by-同舟云学术

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Specific base catalysis by yeast alcohol dehydrogenase I with substitutions of histidine-48 by glutamate or serine residues in the proton relay system

Published:2023-09 Issue: Volume:382 Page:110558
ISSN:0009-2797
Container-title:Chemico-Biological Interactions
language:en
Short-container-title:Chemico-Biological Interactions

Author:

Plapp Bryce V.,Kratzer Darla Ann,Souhrada Susan K.,Warth Edda,Jacobi Tobias

Funder

National Institute on Alcohol Abuse and Alcoholism

U.S. Public Health Service

Publisher

Elsevier BV

Subject

Toxicology,General Medicine

Reference87 articles.

1. Alcohol Dehydrogenases;Brändén,1975

2. Binding of substrate in a ternary complex of horse liver alcohol dehydrogenase;Eklund;J. Biol. Chem.,1982

3. Kinetic studies of liver alcohol dehydrogenase and pH effects with coenzyme preparations of high purity;Dalziel;J. Biol. Chem.,1963

4. The effects of pH and temperature on hydrogen transfer in the liver alcohol dehydrogenase mechanism;Brooks;J. Biol. Chem.,1972

5. Unified mechanism for proton-transfer reactions affecting the catalytic activity of liver alcohol dehydrogenase;Kvassman;Eur. J. Biochem.,1980

Cited by 2 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. Substitution of both histidines in the active site of yeast alcohol dehydrogenase 1 exposes underlying pH dependencies;Chemico-Biological Interactions;2024-05

2. Dynamics of the activated state of NAD-dependent dehydrogenase investigated by a weighted histogram analysis semi-empirical method;Catalysis Science & Technology;2024

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