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. 1979 May 1;179(2):407–412. doi: 10.1042/bj1790407

Adenosine triphosphate consumption by bacterial arginyl-transfer ribonucleic acid synthetases.

J M Godeau, J Charlier
PMCID: PMC1186638  PMID: 384995

Abstract

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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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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