Adenosine triphosphate consumption by bacterial arginyl-transfer ribonucleic acid synthetases.
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.
D000255:Adenosine Triphosphate / Q000378:metabolism*; D000604:Amino Acyl-tRNA Synthetases / Q000378:metabolism*; D001126:Arginine-tRNA Ligase / Q000378:metabolism*; D002852:Chromatography, Ion Exchange; D004926:Escherichia coli / Q000201:enzymology*; D001411:Geobacillus stearothermophilus / Q000201:enzymology*; D008163:Luminescent Measurements
D000255:Adenosine Triphosphate; D000604:Amino Acyl-tRNA Synthetases; D001126:Arginine-tRNA Ligase