Engineering yeast alcohol dehydrogenase. Replacing Trp54 by Leu broadens substrate specificity
- 1 January 1995
- journal article
- Published by Oxford University Press (OUP) in Protein Engineering, Design and Selection
- Vol. 8 (5) , 457-461
- https://doi.org/10.1093/protein/8.5.457
Abstract
Analysis of a crystal structure of alcohol dehydrogenase (Adh) from horse liver suggests that Trp54 in the homologous yeast alcohol dehydrogenase prevents the yeast enzyme from efficiently catalysing the oxidation of long-chain primary alcohols with branching at the 4 position (e.g. 4-methyl-1-pentanol, cinnamyl alcohol). This residue has been altered to Leu by site-directed mutagenesis. The alteration yields an enzyme that serves as an effective catalyst for both longer straight-chain primary alcohols and branched chain alcohols.Keywords
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