An Electrophoretically Cryptic Alcohol Dehydrogenase Variant in Drosophila melanogaster. III. Biochemical Properties and Comparison with Common Enzyme Forms

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Abstract
The biochemical properties of the heat-stable alcohol dehydrogenase variant ADH-FCh.D. were investigated and compared with those of the 2 common enzyme forms ADH-F and ADH-S. ADH-F and ADH-S differ with respect to substrate specificity, their response to high concentrations of secondary alcohols and their apparent Km for 3 alcohols in 2 different buffer systems. In all these tests the enzyme ADH-FCh.D. resembles ADH-S much more closely than ADH-F. 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 3 enzymes are discussed in relation to the role of alcohol dehydrogenase in the exploitation of alcohol by D. melanogaster.