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Article

Amino acids important in enzyme activity and dimer stability for Drosophila alcohol dehydrogenase.

The Biochemical journal - 1 Jun 1995

Chenevert S W, Fossett N G, Chang S H, Tsigelny I, Baker M E, Lee W R

Abstract excerpt

We have determined the nucleotide sequences of eight ethyl methanesulphonate-induced mutants in Drosophila alcohol dehydrogenase (ADH), of which six were previously characterized by Hollocher and Place [(1988) Genetics 116, 253-263 and 265-274]. Four of these ADH mutants contain a single amino acid change: glycine-17 to arginine, glycine-93 to glutamic acid, alanine-159 to threonine, and glycine-184 to aspartic...

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Identifiers

PMID: 7772022
DOI: 10.1042/bj3080419
PMCID: PMC1136942

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