ADENOSINE-TRIPHOSPHATE CONSUMPTION BY BACTERIAL ARGINYL-TRANSFER RIBONUCLEIC-ACID SYNTHETASES

被引：8

作者：

GODEAU, JM ^{[1
]}

CHARLIER, J ^{[1
]}

机构：

[1] VRIJE UNIV BRUSSEL,FAK WETENSCHAPPEN,BIOCHEM,B-1050 BRUSSELS,BELGIUM

来源：

BIOCHEMICAL JOURNAL | 1979年 / 179卷 / 02期

关键词：

D O I：

10.1042/bj1790407

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：

ATP consumption by arginyl-tRNA synthetases from Escherichia coli and Bacillus stearothermophilus has been investigated by the firefly luciferin--luciferase assay. Arginyl-tRNA synthetase from E. coli utilizes ATP only for aminocylation of tRNA with a 1:1 stoicheiometry. In contrast, we have shown an adenosine triphosphatase activity of arginyl-tRNA synthetase from B. stearothermophilus in the absence of tRNAArg. Dowex chromatography revealed the formation of ADP by the thermophile enzyme; under aminoacylation conditions, AMP was also formed in amounts stoicheiometric with arginyl-tRNA formation.

引用

页码：407 / 412

页数：6

共 13 条

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