Inversion of substrate stereoselectivity of horse liver alcohol dehydrogenase by substitutions of Ser-48 and Phe-93-Reference-Cited by-同舟云学术

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Inversion of substrate stereoselectivity of horse liver alcohol dehydrogenase by substitutions of Ser-48 and Phe-93

Published:2017-10 Issue: Volume:276 Page:77-87
ISSN:0009-2797
Container-title:Chemico-Biological Interactions
language:en
Short-container-title:Chemico-Biological Interactions

Author:

Kim Keehyuk^ORCID,Plapp Bryce V.

Funder

U.S. Public Health Service

National Institute on Alcohol Abuse and Alcoholism

National Institute of General Medicine

Center for Biocatalysis and Bioprocessing, The University of Iowa

Office of Science, Office of Basic Energy Sciences in the U.S. Department of Energy

U.S. Department of Energy, Office of Biological and Environmental Research

Publisher

Elsevier BV

Subject

Toxicology,General Medicine

Reference44 articles.

1. Alcohol dehydrogenases;Edenberg,1997

2. Contribution of liver alcohol dehydrogenase to metabolism of alcohols in rats;Plapp;Chem. Biol. Interact.,2015

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

4. Stereospecific oxidation of secondary alcohols by human alcohol dehydrogenases;Stone;J. Biol. Chem.,1989

5. Alpha-isoenzyme of alcohol dehydrogenase from monkey liver. Cloning, expression, mechanism, coenzyme, and substrate specificity;Light;J. Biol. Chem.,1992

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