
pmid: 4333517
Abstract The optimum concentration of MgCl2 for the activity of yeast lysyl-tRNA synthetase (l-lysine:tRNA ligase (AMP), EC 6.1.1.6) in the presence of 1 mm ATP was lower for the ATP-PPi exchange reaction (5 mm) than for the aminoacylation reaction (15 mm) using 1 to 2 mg per ml of tRNA. The presence of 0.1 m KCl was without effect on the ATP-PPi exchange reaction but gave considerable stimulation of the rate of the aminoacylation reaction at 1 to 10 mm MgCl2. The stimulation was not reduced by addition of pyrophosphatase to the assay system. Of the salts tested for stimulation of the esterification reaction, KCl and NH4Cl were the most effective, while NaCl and Tris-HCl gave similar, but lower effects. At 2.5 mm MgCl2 there were marked increases in the observed rate of the aminoacylation reaction after incubation of tRNA but not enzyme, in presence of 0.1 m KCl or 2.5 mm MgCl2, 0.1 m KCl. The results obtained are interpreted in terms of a requirement for the presence of salt to maintain tRNAlys in active conformation for the esterification reaction catalyzed by lysyl-tRNA synthetase.
Carbon Isotopes, Lysine, Phosphorus Isotopes, Saccharomyces cerevisiae, Sodium Chloride, Ammonium Chloride, Catalysis, Potassium Chloride, Amino Acyl-tRNA Synthetases, Diphosphates, Enzyme Activation, Kinetics, Saccharomyces, Adenosine Triphosphate, Chlorides, RNA, Transfer, Nucleic Acid Conformation, Magnesium, Hydrochloric Acid, Pyrophosphatases
Carbon Isotopes, Lysine, Phosphorus Isotopes, Saccharomyces cerevisiae, Sodium Chloride, Ammonium Chloride, Catalysis, Potassium Chloride, Amino Acyl-tRNA Synthetases, Diphosphates, Enzyme Activation, Kinetics, Saccharomyces, Adenosine Triphosphate, Chlorides, RNA, Transfer, Nucleic Acid Conformation, Magnesium, Hydrochloric Acid, Pyrophosphatases
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