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Article

Human alcohol dehydrogenase: dependence of secondary alcohol oxidation on the amino acids at positions 93 and 94.

Biochemical and biophysical research communications - 28 Feb 1992

Hurley T D, Bosron W F

Abstract excerpt

The human liver alpha alpha and beta 1 beta 1 isoenzymes are straight-chain alcohol dehydrogenases with different efficiencies toward secondary alcohols. Two of the 24 amino acid substitutions in alpha alpha (A for F93 and I for T94) were made by site-directed mutagenesis of beta 1 beta 1 and the substrate specificity of beta 93A94I was examined. The Vmax/KM values of beta 93A94I for secondary alcohols...

Topics

Alcohol Dehydrogenase
Alcohols
Binding Sites
Humans
Isoenzymes
Mutagenesis, Site-Directed
Mutation
Recombinant Proteins
Stereoisomerism
Substrate Specificity

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Identifiers

PMID: 1543513
DOI: 10.1016/0006-291x(92)91613-u

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1543513-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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