Eisses K T, Davies S L, Chambers G K
Biochemical Institute, University of Oslo, Norway.
Biochem Genet. 1994 Apr;32(3-4):91-103. doi: 10.1007/BF00554418.
Purified thermostable alcohol dehydrogenase allozymes ADH-71k and ADH-FCh.D. of Drosophila melanogaster have been compared with the two common enzyme forms ADH-F and ADH-S. Enzyme kinetic parameters for various primary and secondary alcohols were determined under standard conditions used previously. Both ADH-71k and ADH-FCh.D. show ADH-S-like reaction kinetics and Km values, due to retrograde evolution at site 214, Pro-->Ser. Inhibition studies with alcohol dehydrogenase inhibitors pyrazole, 4-methylpyrazole, and cibacron blue 3GA were also performed. Activity measurements on crude extracts of larvae and flies from isogenic lines of ADH-FCh.D. revealed a consistently higher activity than in ADH-71k-containing strains, in contrast to the original strains.
已将纯化的黑腹果蝇热稳定乙醇脱氢酶同工酶ADH - 71k和ADH - FCh.D.与两种常见的酶形式ADH - F和ADH - S进行了比较。在先前使用的标准条件下测定了各种伯醇和仲醇的酶动力学参数。由于第214位发生逆行进化（脯氨酸→丝氨酸），ADH - 71k和ADH - FCh.D.均表现出类似ADH - S的反应动力学和Km值。还使用乙醇脱氢酶抑制剂吡唑、4 - 甲基吡唑和汽巴克隆蓝3GA进行了抑制研究。对ADH - FCh.D.同基因系幼虫和果蝇粗提物的活性测量显示，与原始菌株相比，其活性始终高于含ADH - 71k的菌株。
