Abstract
Inhibition of methionyl-transfer RNA synthetase from Escherichia coli by adenosine and 8-aminoadenosine, both competitive inhibitors of ATP-Mg 2+, has been investigated using dialysis and fluorescence spectroscopy at equilibrium. The binding parameters of the nucleosides are shown to depend drastically on the binding of methionine, pyrophosphate and magnesium ions, by way of two distinct synergistic steps. The synergistic coupling on the enzyme between methionine and the nucleoside is insensitive to magnesium ions, while the other synergistic coupling on the enzyme-nucleoside complex between methionine and pyrophosphate is completely dependent on the presence of the divalent ion. On the basis of these results, models for adenylate formation from amino acid plus ATP and from aminoacyl-tRNA plus AMP are discussed.
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