Phenylalanyl transfer ribonucleic acid synthetase from Escherichia coli. Analysis of the adenosine triphosphate binding site

Biochemistry ◽  
1971 ◽  
Vol 10 (25) ◽  
pp. 4821-4824 ◽  
Author(s):  
Daniel V. Santi ◽  
Peter V. Danenberg ◽  
Keith A. Montgomery
Keyword(s):  
Escherichia Coli ◽  
Binding Site ◽  
Adenosine Triphosphate ◽  
Ribonucleic Acid

Nonanucleotide sequence from 16S ribonucleic acid at the peptidyl tRNA binding site of the Escherichia coli ribosome

Biochemistry ◽  
1981 ◽  
Vol 20 (26) ◽  
pp. 7581-7588 ◽  
Author(s):  
Brian H. Taylor ◽  
Jeffrey B. Prince ◽  
James Ofengand ◽  
Robert A. Zimmermann
Keyword(s):  
Escherichia Coli ◽  
Binding Site ◽  
Ribonucleic Acid ◽  
Nonanucleotide Sequence ◽  
Trna Binding

scholarly journals Adenosine triphosphate consumption by bacterial arginyl-transfer ribonucleic acid synthetases

1979 ◽  
Vol 179 (2) ◽  
pp. 407-412 ◽  
Author(s):  
J M Godeau ◽  
J Charlier
Keyword(s):  
Escherichia Coli ◽  
Adenosine Triphosphate ◽  
Ribonucleic Acid ◽  
Adenosine Triphosphatase ◽  
Bacillus Stearothermophilus ◽  
Trna Synthetase ◽  
Luciferase Assay ◽  
Trna Synthetases ◽  
E Coli ◽  
Firefly Luciferin

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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