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.
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Research Article| May 01 1979
Adenosine triphosphate consumption by bacterial arginyl-transfer ribonucleic acid synthetases
Biochem J (1979) 179 (2): 407–412.
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J M Godeau, J Charlier; Adenosine triphosphate consumption by bacterial arginyl-transfer ribonucleic acid synthetases. Biochem J 1 May 1979; 179 (2): 407–412. doi: https://doi.org/10.1042/bj1790407
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