Heinstra P W, Geer B W, Seykens D, Langevin M
Department of Biology, Knox College, Galesburg, IL 61401.
Biochem J. 1989 May 1;259(3):791-7. doi: 10.1042/bj2590791.
Both aldehyde dehydrogenase (ALDH, EC 1.2.1.3) and the aldehyde dehydrogenase activity of alcohol dehydrogenase (ADH, EC 1.1.1.1) were found to coexist in Drosophila melanogaster larvae. The enzymes, however, showed different inhibition patterns with respect to pyrazole, cyanamide and disulphiram. ALDH-1 and ALDH-2 isoenzymes were detected in larvae by electrophoretic methods. Nonetheless, in tracer studies in vivo, more than 75% of the acetaldehyde converted to acetate by the ADH ethanol-degrading pathway appeared to be also catalysed by the ADH enzyme. The larval fat body probably was the major site of this pathway.
在黑腹果蝇幼虫中发现醛脱氢酶（ALDH，EC 1.2.1.3）和乙醇脱氢酶（ADH，EC 1.1.1.1）的醛脱氢酶活性共存。然而，这些酶对吡唑、氰胺和双硫仑表现出不同的抑制模式。通过电泳方法在幼虫中检测到ALDH-1和ALDH-2同工酶。尽管如此，在体内示踪研究中，通过ADH乙醇降解途径转化为乙酸盐的乙醛中，超过75%似乎也由ADH酶催化。幼虫脂肪体可能是该途径的主要部位。
