Kinetic mechanism of threonyl-tRNA synthetase from human placenta
- 12 January 2009
- journal article
- research article
- Published by Wiley in International Journal of Peptide and Protein Research
- Vol. 20 (2) , 159-166
- https://doi.org/10.1111/j.1399-3011.1982.tb02670.x
Abstract
Using purified enzyme and homologous tRNA, the order of substrate binding and product release for the human placental threonyl-tRNA synthetase was investigated by isotope exchange, initial velocity, dead-end inhibition and product inhibition studies. The kinetic patterns obtained from these studies are consistent with a unique Bi Uni Uni Bi ping-pong mechanism. The order of addition of the first 2 substrates ATP and threonine is random, while the release of products follows an obligatory sequence, with AMP as the last product to dissociate from the enzyme.Keywords
This publication has 23 references indexed in Scilit:
- The kinetics of enzyme-catalyzed reactions with two or more substrates or products: II. Inhibition: Nomenclature and theoryPublished by Elsevier ,2003
- Purification and subunit structure studies of human placental threonyl‐tRNA synthetaseInternational Journal of Peptide and Protein Research, 1982
- Catalytic mechanism of valyl-tRNA synthetase from baker's yeast. Reaction pathway and rate-determining step in the aminoacylation tRNAvalBiochemistry, 1981
- The 32PPi—ATP isotope‐exchange reaction catalyzed by the yeast valyl‐tRNA synthetase Order of substrate binding and effect of tRNAFEBS Letters, 1979
- Influence of Magnesium on the Steady‐State‐Derived Order of Substrate Addition and Product Release in tRNA Trp Aminoacylation by Beef Pancreas Tryptophan: tRNA LigaseEuropean Journal of Biochemistry, 1978
- The Mechanism of Action of Methionyl-tRNA Synthetase from Escherichia coli. Mechanism of the Amino-Acid Activation Reaction Catalyzed by the Native and the Trypsin-Modified EnzymesEuropean Journal of Biochemistry, 1974
- Human tryptophanyl transfer ribonucleic acid synthetase. Comparison of the kinetic mechanism to that of the Escherichia coli tryptophanyl transfer ribonucleic acid synthetaseBiochemistry, 1974
- Random sequential mechanism for arginyl transfer ribonucleic acid synthetase of Escherichia coliBiochemistry, 1972
- Order of substrate binding to tyrosyl‐tRNA synthetase of Escherichia coli BFEBS Letters, 1971
- The kinetics of enzyme-catalyzed reactions with two or more substrates or productsBiochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects, 1963