NDLI: Structural determinants of stereospecificity in yeast alcohol dehydrogenase.

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Structural determinants of stereospecificity in yeast alcohol dehydrogenase.

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Structural determinants of stereospecificity in yeast alcohol dehydrogenase.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Weinhold, E. G. Benner, S. A. Glasfeld, A. Ellington, A. D.
Description	Author Affiliation: Weinhold EG ( Laboratory for Organic Chemistry, Swiss Federal Institute of Technology, Zurich.);
Abstract	Replacing Leu-182 by Ala in yeast alcohol dehydrogenase (YADH; alcohol:NAD+ oxidoreductase, EC 1.1.1.1) yields a mutant that retains 34% of its kcat value and makes one stereochemical 'mistake' every 850,000 turnovers (instead of approximately 1 error every 7,000,000,000 turnovers in native YADH) in its selection of the 4-Re hydrogen of NADH. Half of the decrease in stereochemical fidelity comes from an increase in the rate of transfer of the 4-Si hydrogen of NADH. The mutant also accepts 5-methylnicotinamide adenine dinucleotide, a cofactor analog not accepted by native YADH. The stereospecificity of the mutant is lower still with analogs of NADH where the carboxamide group of the nicotinamide ring is replaced by groups with weaker hydrogen bonding potential. For example, with thio-NADH, the mutant enzyme makes 1 stereochemical 'mistake' every 450 turnovers. Finally, the double mutant T157S/L182A, in which Thr-157 is replaced by Ser and Leu-182 is replaced by Ala, also shows decreased stereochemical fidelity. These results suggest that Si transfer in the mutant enzymes arises from NADH bound in a syn conformation in the active site and that this binding is not obstructed in native YADH by side chains essential for catalysis.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	19
Volume Number	88
Language	English
Publisher	National Academy of Sciences
Publisher Date	1991-10-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Alcohol Dehydrogenase Metabolism Saccharomyces Cerevisiae Enzymology DNA Mutational Analysis Ethanol Kinetics NAD Stereoisomerism Structure-Activity Relationship Substrate Specificity Research Support, Non-U.S. Gov't Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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