Disease relevance of gamma-Glutamine-4-nitroanilide

• gamma-Glutamyl transpeptidase activity was detected in rat ascites tumor cells (LY-5) suspended in Hanks' balanced saline solution using L-gamma-glutamyl-p-nitroanilide as a substrate [1].

High impact information on gamma-Glutamine-4-nitroanilide

• Levels of alpha-glutamyltranspeptidase (gamma-GTPase), the ectoenzyme reported to convert LTC or LTD, were detected in intact endothelial cells with the chromogenic substrate L-gamma-glutamyl-p-nitroanilide at levels sufficient to account for the observed rate of LTC metabolism [2].
• gamma-Glutamyl transpeptidase (gamma-GT), an enzyme possibly involved in amino acid transport, was investigated in rat small intestine using the synthetic substrate L-gamma-glutamyl-p-nitroanilide [3].
• The kinetic values for the hydrolysis reaction of L-gamma-glutamyl-p-nitroanilide in the mutants followed similar trends to those for transpeptidation [4].
• GSH was lost intact since resident macrophages lack gamma-glutamyl transpeptidase (less than 1 pmol of L-gamma-glutamyl-p-nitroanilide/microgram of protein . h) [5].
• The Km value for L-gamma-glutamyl-p-nitroanilide and glycylglycine, the Ki for anthglutin, and the pH optimum were identical for the enzyme from all three sources [6].

Biological context of gamma-Glutamine-4-nitroanilide

• The substrate specificity study showed that L: -gamma-glutamyl-p-nitroanilide (L: -gamma-Glu-p-NA) is a preference for the enzyme [7].
• 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 [8].

Associations of gamma-Glutamine-4-nitroanilide with other chemical compounds

• At optimal pH and in the absence of acceptors, the enzyme catalyzes the release of about 510 mumol of p-nitroaniline per mg protein per min from the model substrate L-gamma-glutamyl-p-nitroanilide [9].
• The reaction of oxidized and reduced glutathione (with some amino-acids) and L-gamma-glutamyl p-nitroanilide with sheep kidney tissue homogenate. An examination of the reaction products by paper chromatography [10].
• Optimum incubation conditions for the determination of gamma-glutamyltranspeptidase with liver homogenates from rats of different ages have been determined: about 1 mg protein/assay, 4.4 mM L-gamma-glutamyl-p-nitroanilide, 40 mM glycylglycine, 9.6 mM MgCl2 in 0.1 M Tris-HCl buffer, pH 8.0; final volume 1.3 ml [11].

Gene context of gamma-Glutamine-4-nitroanilide

• With L-gamma-glutamyl-p-nitroanilide, the kinetic efficiency increase of diabetic over control gamma-glutamyltransferase was higher with poor acceptors than with highly efficient acceptors [12].

References