Chambers G K, Wilks A V, Gibson J B
Aust J Biol Sci. 1981;34(5-6):625-37. doi: 10.1071/bi9810625.
The biochemical properties of the heat-stable alcohol dehydrogenase variant ADH-FCh.D. have been investigated and compared with those of the two common enzyme forms ADH-F and ADH-S. The results show that ADH-F and ADH-S differ with respect to substrate specificity, their response to high concentrations of secondary alcohols and their apparent Michaelis constants for three alcohols in two different buffer systems. In all these tests the enzyme ADH-FCh.D. resembles ADH-S much more closely than ADH-F. It is concluded that if natural selection is to distinguish between the alleles AdhS and AdhFCh.D. then it most probably does so on the basis of the superior thermostability of ADH-FCh.D. The biochemical properties of all three enzymes are discussed in relation to the role of alcohol dehydrogenase in the exploitation of alcohol by D. melanogaster.
已对热稳定型乙醇脱氢酶变体ADH-FCh.D.的生化特性进行了研究，并与两种常见酶形式ADH-F和ADH-S的特性进行了比较。结果表明，ADH-F和ADH-S在底物特异性、对高浓度仲醇的反应以及在两种不同缓冲系统中对三种醇的表观米氏常数方面存在差异。在所有这些测试中，酶ADH-FCh.D.与ADH-S的相似程度远高于与ADH-F的相似程度。得出的结论是，如果自然选择要区分等位基因AdhS和AdhFCh.D.，那么很可能是基于ADH-FCh.D.具有更高的热稳定性来进行区分的。还结合乙醇脱氢酶在黑腹果蝇利用酒精过程中的作用，对这三种酶的生化特性进行了讨论。
