Order of binding of substrate to valyl-tRNA synthetase from Bacillus stearothermophilus in amino acid activation reaction.
Amino acid activation reaction with valyl-tRNA synthetase (EC 6.1.1.9) from Bacillus stearothermophilus was studied kinetically by measuring ATP-PPi exchange to find the order of the binding of substrate to the enzyme. The effects of the concentration of the substrates (L-valine and ATP) and two dead-end inhibitors (L-valinol and adenosine) on the reaction rate were analyzed. The results indicate that L-valine and ATP are bound to the enzyme in a random sequence. This conclusion is consistent with the one previously suggested by static binding experiments.
Kakitani
M
M
Department of Food Science and Technology, Faculty of Agriculture, Kyoto University, Japan.
Tonomura
B
B
Hiromi
K
K
D000241:Adenosine / Q000494:pharmacology; D000255:Adenosine Triphosphate / Q000494:pharmacology; D000604:Amino Acyl-tRNA Synthetases / Q000378:metabolism*; D001665:Binding Sites; D004735:Energy Transfer / Q000187:drug effects; D001411:Geobacillus stearothermophilus / Q000201:enzymology*; D046249:Transfer RNA Aminoacylation; D014633:Valine / Q000031:analogs & derivatives / Q000494:pharmacology; D014637:Valine-tRNA Ligase / Q000378:metabolism*
C040994:valinol; D000255:Adenosine Triphosphate; D000604:Amino Acyl-tRNA Synthetases; D014637:Valine-tRNA Ligase; D014633:Valine; D000241:Adenosine