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- W1626197854 abstract "Interactions of several amino acids and nucleotides with valyl-tRNA synthetase [EC 6.1.1.9] (VRS) from Bacillus stearothermophilus were investigated using as a probe the ligand-induced quenching of protein fluorescence (λex=295 nm, λem=340 nm) of VRS. L-Valine, L-threonine, L-isoleucine, L-glutamic acid, L-Ieucine, and D-valine caused fluorescence quenching. Among them, L-threonine had a Kd value comparable to that for the cognate substrate, L-valine, but the other amino acids were bound more weakly as estimated by the fluorescence titration method. L-Alanine, L-histidine, and L-Serine did not cause any fluorescence change. Among the nucleotides tested (ATP, ADP, AMP, GTP, ITP, CTP, and UTP), only ATP caused the fluorescence change. In the presence of an excess amount of ATP, only L-valine and L-threonine, among the tested amino acids, induced the fluorescence quenching, and the binding of L-valine was greatly favored under this condition. This is consistent with the results of the ATP-PP exchange reaction by VRS, in which only L-valine and L-threonine, of these 9 amino acids tested, could serve as substrates, and the Km value for L-valine was much smaller than that for L. threonine. Thus the binding of ATP to YRS enhances the substrate specificity of VRS towards amino acids. The binding stoichiometry deduced from equilibrium dialysis experiments for L-valine and ATP was found to be one when these substrates exist together, in contrast to our previous observation that there were two equivalent binding sites for each of L-valine and ATP when these substrates were added separately to the enzyme" @default.
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- W1626197854 date "1987-02-01" @default.
- W1626197854 modified "2023-10-18" @default.
- W1626197854 title "Fluorometric Study on the Interaction of Amino Acids and ATP with Valyl-tRNA Synthetase fromBacillus stearothermophilus1" @default.
- W1626197854 doi "https://doi.org/10.1093/oxfordjournals.jbchem.a121933" @default.
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