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

@article{Chenevert1995AminoAI,
  title={Amino acids important in enzyme activity and dimer stability for Drosophila alcohol dehydrogenase.},
  author={S W Chenevert and N G Fossett and Simon H. Chang and Igor F. Tsigelny and Michael E. Baker and William R. Lee},
  journal={The Biochemical journal},
  year={1995},
  volume={308 ( Pt 2)},
  pages={419-23}
}
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 acid. Although these mutants are inactive, three mutants (Gly17Arg, Gly93Glu and… CONTINUE READING
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