Protein engineering of alcohol dehydrogenases: effects of amino acid changes at positions 93 and 48 of yeast ADH1.

doi:10.1093/protein/3.6.523

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Article

Protein engineering of alcohol dehydrogenases: effects of amino acid changes at positions 93 and 48 of yeast ADH1.

Protein engineering - 1 May 1990

Creaser E H, Murali C, Britt K A

Abstract excerpt

By protein engineering we have investigated changes to two amino acid residues (Trp93 and Ser48) in the substrate pocket of yeast alcohol dehydrogenase 1. Upon changing Thr48 to serine we produced an enzyme which has markedly greater activity towards aliphatic alcohols with chain length up to 8,...

Topics

Alcohol Dehydrogenase
Alcohols
Amino Acids
Binding Sites
DNA, Fungal
Escherichia coli
Kinetics
Mutation
Protein Engineering
Saccharomyces cerevisiae

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