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Article

The kinetic characteristics of K228G mutant horse liver alcohol dehydrogenase.

Archives of pharmacal research - 1 Feb 1999

Cho S H, Ryu J W, Lee K M

Abstract excerpt

The kinetic constants and the reaction mechanism of the K228G mutant horse liver alcohol dehydrogenase isoenzyme E (HLADH-E) were compared to the wild-type enzyme. All the Km and Ki constants of the mutant enzyme for NAD+, ethanol, acetaldehyde and NADH were larger than those of the wild-type enzyme. The dissociation constants for the NADH and NAD+ (Kiq and Kia) were greatly increased by 130- and 460-fold,...

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Identifiers

PMID: 10071953
DOI: 10.1007/BF02976429

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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