| Literature DB >> 8532667 |
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.Entities:
Mesh:
Substances:
Year: 1995 PMID: 8532667 DOI: 10.1093/protein/8.5.457
Source DB: PubMed Journal: Protein Eng ISSN: 0269-2139