The glutamyl-tRNA synthetase of Escherichia coli: substrate-induced protection against its thermal inactivation.
The substrates-induced protection against the heat-inactivation of the glutamyl-tRNA synthetase has been investigated. tRNAGlu and ATP protect efficiently the enzyme, whereas glutamate does not. In the presence of tRNAGlu, glutamate induces an additional protection to that given by the tRNAGlu alone. A weak synergism was observed between ATP and tRNAGlu, whereas no synergism was detected between ATP and glutamate. These results suggest that tRNAGlu and ATP, but not glutamate are able to bind to the free enzyme form; glutamate binds only to the Enzyme.tRNAGlu and to the Enzyme.tRNAGlu.ATP complexes. The presence of the three substrates induces a higher stabilization of the enzyme than that expected from the protection observed for the various other substrates combinations, suggesting the existence of a marked synergism between the three substrates against the heat-inactivation of the enzyme. The protection constants determined from this study are similar to the dissociation constants determined by direct binding experiments and to the Km values determined kinetically.
D000255:Adenosine Triphosphate / Q000494:pharmacology; D000604:Amino Acyl-tRNA Synthetases / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology*; D005975:Glutamate-tRNA Ligase / Q000378:metabolism*; D005971:Glutamates; D007700:Kinetics; D011489:Protein Denaturation; D012346:RNA, Transfer, Amino Acyl / Q000494:pharmacology; D013696:Temperature
D005971:Glutamates; D012346:RNA, Transfer, Amino Acyl; D000255:Adenosine Triphosphate; D000604:Amino Acyl-tRNA Synthetases; D005975:Glutamate-tRNA Ligase