嗜热脂肪芽孢杆菌缬氨酰 - tRNA合成酶在氨基酸活化反应中底物结合的顺序
Order of binding of substrate to valyl-tRNA synthetase from Bacillus stearothermophilus in amino acid activation reaction.
作者信息
Kakitani M, Tonomura B, Hiromi K
机构信息
Department of Food Science and Technology, Faculty of Agriculture, Kyoto University, Japan.
出版信息
Biochem Int. 1987 Apr;14(4):597-603.
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.
通过测量ATP-PPi交换，对嗜热脂肪芽孢杆菌的缬氨酰-tRNA合成酶（EC 6.1.1.9）的氨基酸活化反应进行了动力学研究，以确定底物与酶结合的顺序。分析了底物（L-缬氨酸和ATP）以及两种终产物抑制剂（L-缬氨醇和腺苷）浓度对反应速率的影响。结果表明，L-缬氨酸和ATP以随机顺序与酶结合。这一结论与先前通过静态结合实验得出的结论一致。
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