Weinhold E G, Benner S A
Department of Chemistry, ETH, Zurich, Switzerland.
Protein Eng. 1995 May;8(5):457-61. doi: 10.1093/protein/8.5.457.
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.
对马肝醇脱氢酶（Adh）晶体结构的分析表明，同源酵母醇脱氢酶中的色氨酸54会阻止酵母酶有效催化在4位带有支链的长链伯醇（如4-甲基-1-戊醇、肉桂醇）的氧化反应。通过定点诱变，该残基已被改变为亮氨酸。这种改变产生了一种对较长直链伯醇和支链醇均起有效催化作用的酶。
