Enantioselective affinity labelling of horse liver alcohol dehydrogenase. Correlation of inactivation kinetics with the three-dimensional structure of the enzyme.

Kinetic data for the inactivation of horse liver alcohol dehydrogenase with S-2-chloro-3-(imidazol-5-yl)propionate at pH8.2 were correlated with the three-dimensional structure of the enzyme. The R-2-chloro-3-(imidazol-5-yl)propionate enantiomer did not inactivate the enzyme, and the reaction is thu...

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Bibliographic Details
Main Authors: Dahl, K H, Eklund, H, McKinley-McKee, J S
Format: Artigo
Language:Inglês
Published: 1983
Subjects:
Research Article
Online Access:https://ncbi.nlm.nih.gov/pmc/articles/PMC1154371/
https://ncbi.nlm.nih.gov/pubmed/6347187
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