gamma-Glutamyl transpeptidase activity can be altered by kainic acid and related compounds.
The effect of kainic acid and related compounds, gamma-D-glutamylglycine, cis-2,3-piperidine dicarboxylic acid and DL alpha-aminoadipic acid, was investigated on purified and membrane bound gamma-glutamyl transpeptidase [GGT]. All four compounds suppressed enzyme activity to an extent which depended upon the presence of a gamma-glutamyl moiety acceptor. Of the amino acid and dipeptide acceptors used, glycyl-glycine was the most affected. These compounds may be useful probes in determining the physiological role of gamma-glutamyl transpeptidase. The relationship between GGT, the gamma-glutamyl cycle and the toxicity of kainic acid is discussed.
D015074:2-Aminoadipic Acid / Q000494:pharmacology; D000818:Animals; D004151:Dipeptides / Q000494:pharmacology; D005971:Glutamates / Q000378:metabolism; D018698:Glutamic Acid; D007608:Kainic Acid / Q000494:pharmacology*; D011759:Pyrrolidines / Q000494:pharmacology*; D051381:Rats; D013329:Structure-Activity Relationship; D005723:gamma-Glutamyltransferase / Q000037:antagonists & inhibitors*
D004151:Dipeptides; D005971:Glutamates; D011759:Pyrrolidines; D015074:2-Aminoadipic Acid; D018698:Glutamic Acid; D005723:gamma-Glutamyltransferase; D007608:Kainic Acid