Biochemistry international 1987-04-01

Order of binding of substrate to valyl-tRNA synthetase from Bacillus stearothermophilus in amino acid activation reaction.

M Kakitani, B Tonomura, K Hiromi

Index: Biochem. Int. 14(4) , 597-603, (1987)

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Abstract

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.

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