Abstract

Abstract Salicylate inhibits glutamyl-transfer ribonucleic acid synthetase by simple competitive inhibition with respect to glutamate and mixed competitive-non-competitive inhibitions with ATP and tRNA. It is suggested that competition between salicylate and amino-acid explains the variable inhibition of the synthetases by the drugs in vitro. The action of salicylate is consistent with a mechanism for glutamyl-tRNA formation involving a concerted interaction of all three substrates. The drug may selectively interfere with protein synthesis in vivo.

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