Substitution of arginine for histidine-47 in the coenzyme binding site of yeast alcohol dehydrogenase I.

doi:10.1021/bi00475a009

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Article

Substitution of arginine for histidine-47 in the coenzyme binding site of yeast alcohol dehydrogenase I.

Biochemistry - 12 Jun 1990

Gould R M, Plapp B V

Abstract excerpt

Molecular modeling of alcohol dehydrogenase suggests that His-47 in the yeast enzyme (His-44 in the protein sequence, corresponding to Arg-47 in the horse liver enzyme) binds the pyrophosphate of the NAD coenzyme. His-47 in the Saccharomyces cerevisiae isoenzyme I was substituted with an arginine...

Topics

Alcohol Dehydrogenase
Arginine
Base Sequence
Binding Sites
DNA, Fungal
Histidine
Hydrogen-Ion Concentration
Kinetics
Molecular Sequence Data
Mutation
NAD
Saccharomyces cerevisiae

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