The aminoacylation of transfer ribonucleic acid. Recognition of methionine by Escherichia coli methionyl-transfer ribonucleic acid synthetase

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Abstract
The mechanism of the recognition of methionine by E. coli methionyl-tRNA synthetase was examined by a kinetic study of the recognition of methionine analogs in the ATP-PPi exchange reaction and the tRNA-aminoacylation reaction. The recognition mechanism consists of 3 parts: the recognition of the size, shape and chemical nature of the amino acid side chain at the methionine-binding stage of the reaction; the recognition of the length of the side chain at the stage of aminoacyl-adenylate complex-formation; the recognition of the S atom in the side chain at the stage of methionyl-tRNA formation. The S atom probably interacts with the enzyme to induce a conformational change. A model of the active site incorporating the mechanism of methionine recognition is presented.