.beta.- and .gamma.-Thio analogs of adenosine triphosphate as probes of the Escherichia coli valyl transfer ribonucleic acid synthetase reaction pathway. A novel stereospecific interchange of adenosine 5'-O-(2-thiotriphosphate) to adenosine 5'-O-(3-thiotriphosphate)

Biochemistry ◽  
1979 ◽  
Vol 18 (25) ◽  
pp. 5670-5674 ◽  
Author(s):  
Edward F. Rossomando ◽  
Linda Tombras Smith ◽  
Mildred Cohn

Biochemistry ◽  
1971 ◽  
Vol 10 (25) ◽  
pp. 4821-4824 ◽  
Author(s):  
Daniel V. Santi ◽  
Peter V. Danenberg ◽  
Keith A. Montgomery


1979 ◽  
Vol 179 (2) ◽  
pp. 407-412 ◽  
Author(s):  
J M Godeau ◽  
J Charlier

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.



1963 ◽  
Vol 28 (5) ◽  
pp. 1215-1223 ◽  
Author(s):  
J. Černá ◽  
I. Rychlík ◽  
D. Grünberger ◽  
F. Šorm


1970 ◽  
Vol 245 (6) ◽  
pp. 1401-1406 ◽  
Author(s):  
H. Hayashi ◽  
J.R. Knowles ◽  
Jon R. Katze ◽  
J. Lapointe ◽  
Dieter Söll


1970 ◽  
Vol 245 (10) ◽  
pp. 2679-2692
Author(s):  
David A. Sirbasku ◽  
John M. Buchanan


1971 ◽  
Vol 246 (19) ◽  
pp. 5924-5928 ◽  
Author(s):  
Takis S. Papas ◽  
Alan H. Mehler








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