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- W1986719211 abstract "Using EDTA-dialyzed tyrosyl-tRNA synthetase and tRNA, which retain 0.8 and 0.25 atom of Mg2+ per molecule, respectively, tyrosine activation as well as tyrosyl-tRNA formation were investigated in the absence of added magnesium ions. It is shown that the tyrosyladenylate · enzyme complex is still formed, but the rate of the reaction is reduced by a factor of 104. The rate of the ATP-PPi exchange reaction, under these conditions, is reduced by a factor of 4 · 104. In the presence of pyrophosphate the predominant reaction is not the pyrophosphorolysis of the enzyme-bound tyrosyladenylate but its hydrolysis. The rate of tyrosyl-tRNA formation, starting with free ATP and tyrosine and in the presence of spermidine, was only 15 times lower than in the presence of Mg2+. Spermidine has no effect on the rate of the ATP-PPi exchange reaction." @default.
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- W1986719211 date "1973-05-01" @default.
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- W1986719211 title "Tyrosyl-tRNA Synthetase of Escherichia coli B. Role of Magnesium Ions in the Reaction Catalyzed by the Enzyme" @default.
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- W1986719211 doi "https://doi.org/10.1111/j.1432-1033.1973.tb02807.x" @default.
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