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大肠杆菌中精氨酸生物合成的调控:精氨酰转移核糖核酸合成酶突变体的特性分析

Control of arginine biosynthesis in Escherichia coli: characterization of arginyl-transfer ribonucleic acid synthetase mutants.

作者信息

Williams A L, Williams L S

出版信息

J Bacteriol. 1973 Mar;113(3):1433-41. doi: 10.1128/jb.113.3.1433-1441.1973.

Abstract

The arginyl-transfer ribonucleic acid (Arg-tRNA) synthetase (EC 6.1.1.13, arginine: RNA ligase adenosine monophosphate) mutants, exhibiting nonrepressible synthesis of arginine by exogenous arginine, were employed in studies of several biochemical properties. Two of these mutants possessed Arg-tRNA synthetases with a reduced affinity for arginine, and this enzyme of another mutant had a reduced affinity for arginine-tRNA (tRNA(arg)). The mutant possessing an Arg-tRNA synthetase with an altered K(m) for tRNA(arg) was found to have reduced in vivo aminoacylation of two of the five isoaccepting species of tRNA(arg) and complete absence of aminoacylation of one of the isoaccepting species.

摘要

精氨酰转移核糖核酸(Arg-tRNA)合成酶(EC 6.1.1.13,精氨酸:RNA连接酶单磷酸腺苷)突变体,表现出对外源精氨酸不可抑制的精氨酸合成,被用于多项生化特性研究。这些突变体中的两个具有对精氨酸亲和力降低的Arg-tRNA合成酶,另一个突变体的这种酶对精氨酰-tRNA(tRNA(arg))的亲和力降低。发现拥有对tRNA(arg)的K(m)改变的Arg-tRNA合成酶的突变体,其体内五种同功受体类型的tRNA(arg)中有两种的氨酰化作用降低,且有一种同功受体类型完全没有氨酰化作用。

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