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. Pyropho...

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Veröffentlicht in:	The Journal of biological chemistry 1983-11, Vol.258 (22), p.13592-13596
Hauptverfasser:	Hilderman, R H, Zimmerman, J K, Dang, C V, Grothusen, J R
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acyl-tRNA Synthetases - metabolism Analytical, structural and metabolic biochemistry Animals Arginine-tRNA Ligase - metabolism Biological and medical sciences Diphosphates - pharmacology Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Kinetics Ligases Liver - enzymology Lysine - analogs & derivatives Lysine - pharmacology Lysine-tRNA Ligase - metabolism Male Multienzyme Complexes - metabolism Rats Zinc - pharmacology
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Beschreibung
Zusammenfassung:	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.
ISSN:	0021-9258 1083-351X
DOI:	10.1016/S0021-9258(17)43956-1