Old J M, Jones D S
Biochem J. 1977 Aug 1;165(2):367-73. doi: 10.1042/bj1650367.
The mechanism of the recognition of methionine by Escherichia coli methionyl-tRNA synthetase was examined by a kinetic study of the recognition of methionine analogues in the ATP-PPi exchange reaction and the tRNA-aminoacylation reaction. The results show that the recognition mechanism consists of three parts: (1) the recognition of the size, shape and chemical nature of the amino acid side chain at the methionine-binding stage of the reaction; (2) the recognition of the length of the side chain at the stage of aminoacyl-adenylate complex-formation; (3) the recognition of the sulphur atom in the side chain at the stage of methionyl-tRNA formation. It is proposed that the sulphur atom interacts with the enzyme to induce a conformational change. A model of the active site incorporating the mechanism of methionine recognition is presented.
通过对ATP-PPi交换反应和tRNA氨基酰化反应中蛋氨酸类似物识别的动力学研究,考察了大肠杆菌蛋氨酰-tRNA合成酶对蛋氨酸的识别机制。结果表明,识别机制包括三个部分:(1)在反应的蛋氨酸结合阶段对氨基酸侧链的大小、形状和化学性质的识别;(2)在氨酰-腺苷酸复合物形成阶段对侧链长度的识别;(3)在蛋氨酰-tRNA形成阶段对侧链中硫原子的识别。有人提出,硫原子与酶相互作用以诱导构象变化。提出了一个包含蛋氨酸识别机制的活性位点模型。