General Physiology and Biophysics 1996-10-01

Analysis of kinetic properties of gamma-glutamyl transpeptidase from rat kidney.

L Dvoráková, J Krůsek, F Stastný, V Lisý

Index: Gen. Physiol. Biophys. 15(5) , 403-13, (1996)

Full Text: HTML

Abstract

The initial rate kinetics of rat kidney gamma-glutamyl transpeptidase were measured using L-gamma-glutamyl-p-nitroanilide and glycyl-glycine as the donor and the acceptor substrate, respectively. Experimental data were fitted with the initial rate equation, and the obtained results indicated that: (1) Michaelis constants for transpeptidation (Kb), autotranspeptidation (Ka), and hydrolysis (Kh) are 8.56 mmol/l, 2.02 mmol/l and 0.005 mmol/l, respectively. (2) The maximum rate of transpeptidation (Vb) exceeds that of hydrolysis (Vh) and autotranspeptidation (Va) 160 times and 5 times, respectively. (3) A comparison of the ratios of maximal rate: Michaelis constant of individual reactions shows that hydrolysis is approximately 10 times more efficient than the remaining two reactions. (4) Under routine conditions used for gamma-glutamyl transpeptidase estimation, transpeptidation is the prevalent reaction.


Related Compounds

  • GPNA hydrochlori...
  • N-(4-Nitrophenyl)...

Related Articles:

Donor substrate specificity of bovine kidney gamma-glutamyltransferase

2013-04-25

[Chem. Biol. Interact. 203(2) , 480-5, (2013)]

Cross-talk between ER and HER2 regulates c-MYC-mediated glutamine metabolism in aromatase inhibitor resistant breast cancer cells.

2015-05-01

[J. Steroid Biochem. Mol. Biol. 149 , 118-27, (2015)]

Rapid purification and characterization of γ-glutamyl-transpeptidase from shiitake mushroom (Lentinus edodes).

2012-06-01

[J. Food Sci. 77(6) , C640-5, (2012)]

Changes in the kinetic parameters of hepatic gamma-glutamyltransferase from streptozotocin-induced diabetic rats.

2001-02-09

[Biochim. Biophys. Acta 1545(1-2) , 184-91, (2001)]

An isopeptide bond splitting enzyme from Hirudo medicinalis similar to gamma-glutamyl transpeptidase.

1998-09-01

[Eur. J. Biochem. 256(2) , 297-302, (1998)]

More Articles...