title: The binding of tyrosinyl-5'-AMP to tyrosyl-tRNA synthetase (E.coli).
abstract: The binding between tyrosyl-tRNA synthetase (E.coli) and the alkylanalogue of the aminoacyladenylate, tyrosinyl-5'-AMP, has been investigated by fluorescence titrations and rapid mixing experiments. Tyrosyl-tRNA synthetase has two equivalent and independent binding sites for tyrosinyl-5'-AMP. The intrinsic binding constant is 4 x 10(7)M-1. The binding sites for tRNATyr and tyrosinyl-5'-AMP are independent of each other, the anticooperative mode of tRNA binding being preserved in the presence of tyrosinyl-5-AMP.
mesh_terms: D000249:Adenosine Monophosphate / Q000031:analogs & derivatives; D000604:Amino Acyl-tRNA Synthetases / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology*; D007700:Kinetics; D011485:Protein Binding; D046249:Transfer RNA Aminoacylation; D014443:Tyrosine / Q000031:analogs & derivatives*; D014448:Tyrosine-tRNA Ligase / Q000378:metabolism*
chemical_list: D000249:Adenosine Monophosphate; D014443:Tyrosine; C019586:tyrosinyl-5'-AMP; D000604:Amino Acyl-tRNA Synthetases; D014448:Tyrosine-tRNA Ligase