Characterization of a homogeneous arginyl- and lysyl-tRNA synthetase complex isolated from rat liver. Kinetic mechanism for lysyl-tRNA synthetase.
Bisubstrate kinetics and end product and dead end inhibition studies were performed on lysyl-tRNA synthetase isolated from rat liver. The kinetic patterns obtained are consistent with a sequential ordered mechanism of substrate addition, tRNA bound first, followed by lysine, and then by ATP. Pyrophosphate and AMP are released in a random fashion with aminoacylated tRNA the last product to dissociate from the enzyme. This is the first report of a kinetic mechanism for lysyl-tRNA synthetase.
D000604:Amino Acyl-tRNA Synthetases / Q000378:metabolism*; D000818:Animals; D001126:Arginine-tRNA Ligase / Q000378:metabolism*; D011756:Diphosphates / Q000494:pharmacology; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008239:Lysine / Q000031:analogs & derivatives / Q000494:pharmacology; D008250:Lysine-tRNA Ligase / Q000378:metabolism*; D008297:Male; D009097:Multienzyme Complexes / Q000378:metabolism*; D051381:Rats; D015032:Zinc / Q000494:pharmacology
D011756:Diphosphates; D009097:Multienzyme Complexes; C039763:lysine hydroxamate; D000604:Amino Acyl-tRNA Synthetases; D001126:Arginine-tRNA Ligase; D008250:Lysine-tRNA Ligase; D015032:Zinc; D008239:Lysine