Chambers G K
Biochem Genet. 1984 Jun;22(5-6):529-49. doi: 10.1007/BF00484521.
Alcohol dehydrogenase has been purified from Drosophila melanogaster lines bearing the AdhF, AdhS, and AdhFCh.D. alleles. Biochemical investigations show that the properties of the purified enzymes are very similar to those of crude enzyme extracts except that the pure enzymes are more heat stable. ADH-FCh.D. resembles ADH-S very closely in specific activity, substrate specificity, and a number of kinetic parameters including limiting values for Km(app.) for ethanol. However, it is considerably more heat stable than either of the two common variants. ADH-F differs from ADH-S and ADH-FCh.D. particularly with regard to the rate of oxidation of secondary alcohols. Atomic absorbtion spectroscopy shows that all three allozymes lack zinc or other divalent cations as active-site components. Peptide mapping experiments identify one very active cysteinyl residue; and amide residues in the NAD+ binding domain.
已从携带AdhF、AdhS和AdhFCh.D.等位基因的黑腹果蝇品系中纯化出乙醇脱氢酶。生化研究表明，纯化酶的特性与粗酶提取物非常相似，只是纯酶更耐热。ADH-FCh.D.在比活性、底物特异性以及包括乙醇Km（app.）极限值在内的一些动力学参数方面与ADH-S非常相似。然而，它比两种常见变体中的任何一种都更耐热。ADH-F与ADH-S和ADH-FCh.D.的不同之处尤其在于仲醇的氧化速率。原子吸收光谱表明，所有三种同工酶都缺乏锌或其他二价阳离子作为活性位点成分。肽图谱实验确定了一个非常活跃的半胱氨酰残基；以及NAD+结合域中的酰胺残基。
