SUBSTRATE AND INHIBITOR SPECIFICITIES OF THE THERMOSTABLE ALCOHOL-DEHYDROGENASE ALLOZYMES ADH-71K AND ADH-FCH.D OF DROSOPHILA-MELANOGASTER

被引：12

作者：

EISSES, KT

DAVIES, SL

CHAMBERS, GK

机构：

[1] UNIV OSLO,INST BIOCHEM,OSLO,NORWAY

[2] VICTORIA UNIV WELLINGTON,SCH BIOL SCI,WELLINGTON,NEW ZEALAND

来源：

BIOCHEMICAL GENETICS | 1994年 / 32卷 / 3-4期

关键词：

THERMOSTABLE ALCOHOL DEHYDROGENASE; DROSOPHILA MELANOGASTER; SUBSTRATE SPECIFICITY; INHIBITORS; RETROGRADE EVOLUTION;

D O I：

10.1007/BF00554418

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 K-m 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.

引用

页码：91 / 103

页数：13

共 53 条

[11] INHIBITORY POWER OF SOME FURTHER PYRAZOLE DERIVATIVES OF HORSE LIVER ALCOHOL-DEHYDROGENASE [J].