Synthesis of aza and oxaglutamyl-p-nitroanilide derivatives and their kinetic studies with gamma-glutamyltranspeptidase.
A new series of L-glutamic acid p-nitroanilide analogues has been synthesized and tested as substrates and inhibitors of rat kidney gamma-glutamyltranspeptidase (GGT). Kinetic parameters (K(m) and k(cat)) were determined for each analogue and provide insight into the scope and limits of GGT catalytic efficiency.
Lherbet
Christian
C
Département de chimie, Université de Montréal, C.P. 6128, Succursale centre-ville, Montréal, Québec, Canada H3C 3J7.
Morin
Mylène
M
Castonguay
Roselyne
R
Keillor
Jeffrey W
JW
D000813:Anilides / Q000138:chemical synthesis* / Q000494:pharmacology*; D000818:Animals; D002855:Chromatography, Thin Layer; D004791:Enzyme Inhibitors / Q000138:chemical synthesis* / Q000494:pharmacology*; D005971:Glutamates / Q000138:chemical synthesis* / Q000494:pharmacology*; D005978:Glutathione / Q000031:analogs & derivatives / Q000138:chemical synthesis / Q000494:pharmacology; D007668:Kidney / Q000201:enzymology; D007700:Kinetics; D051381:Rats; D013329:Structure-Activity Relationship; D005723:gamma-Glutamyltransferase / Q000037:antagonists & inhibitors*
D000813:Anilides; D004791:Enzyme Inhibitors; D005971:Glutamates; D005723:gamma-Glutamyltransferase; D005978:Glutathione