pyrophosphate and lysine-hydroxamate

pyrophosphate has been researched along with lysine-hydroxamate* in 1 studies

Other Studies

1 other study(ies) available for pyrophosphate and lysine-hydroxamate

Article	Year
Characterization of a homogeneous arginyl- and lysyl-tRNA synthetase complex isolated from rat liver. Kinetic mechanism for lysyl-tRNA synthetase. The Journal of biological chemistry, 1983, Nov-25, Volume: 258, Issue:22 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. Topics: Amino Acyl-tRNA Synthetases; Animals; Arginine-tRNA Ligase; Diphosphates; Kinetics; Liver; Lysine; Lysine-tRNA Ligase; Male; Multienzyme Complexes; Rats; Zinc	1983

Article

Year

Characterization of a homogeneous arginyl- and lysyl-tRNA synthetase complex isolated from rat liver. Kinetic mechanism for lysyl-tRNA synthetase.

The Journal of biological chemistry, 1983, Nov-25, Volume: 258, Issue:22

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.

Topics: Amino Acyl-tRNA Synthetases; Animals; Arginine-tRNA Ligase; Diphosphates; Kinetics; Liver; Lysine; Lysine-tRNA Ligase; Male; Multienzyme Complexes; Rats; Zinc

1983