Adenosine triphosphate consumption by bacterial arginyl-transfer ribonucleic acid synthetases
| Autor: | J Charlier, J M Godeau |
|---|---|
| Rok vydání: | 1979 |
| Předmět: |
Bacillus
Aminoacylation medicine.disease_cause Biochemistry Amino Acyl-tRNA Synthetases Geobacillus stearothermophilus chemistry.chemical_compound Adenosine Triphosphate Escherichia coli medicine Molecular Biology chemistry.chemical_classification Firefly protocol biology Thermophile Cell Biology Arginine-tRNA Ligase Chromatography Ion Exchange biology.organism_classification Molecular biology Enzyme chemistry Luminescent Measurements Transfer RNA bacteria Adenosine triphosphate Research Article |
| Zdroj: | Biochemical Journal. 179:407-412 |
| ISSN: | 0264-6021 |
| DOI: | 10.1042/bj1790407 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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