Partial reactions of aminoacyl-tRNA synthetases as functions of pH.
The effect of pH on the properties of the partial reactions of arginyl-tRNA synthetase of E. coli has been investigated. V max of pyrophosphorolysis of arginyl adenylate has a pH optimum at pH 6.1, whereas V max of the transfer of arginine to tRNA has a pH optimum of 8.2. These values correlate with the pH optima of the ATP:PPi exchange and the overall esterification reaction, respectively. Only the pyrophosphorolysis reaction requires a divalent cation; transfer proceeds in the presence of EDTA. Inorganic pyrophosphate inhibits the transfer reaction to an extent independent of the concentration of tRNA; the maximum inhibition is a function of pH, corresponding to the relative rate of pyrophosphorolysis of the common intermediate compared with the rate of transfer. These results show that different groups on the enzyme participate in the rate-limiting steps of the two partial reactions and that these partial reactions have properties consistent with their participation in the overall esterification of arginine with tRNA.
D000604:Amino Acyl-tRNA Synthetases / Q000378:metabolism*; D001126:Arginine-tRNA Ligase / Q000378:metabolism*; D011756:Diphosphates / Q000494:pharmacology; D004926:Escherichia coli / Q000201:enzymology; D006863:Hydrogen-Ion Concentration; D007700:Kinetics
D011756:Diphosphates; D000604:Amino Acyl-tRNA Synthetases; D001126:Arginine-tRNA Ligase