Comparison of kinetic property between human seminal and renal gamma-glutamyltransferase.

The initial-velocity kinetics, optimal pH, acceptor specificity and the influence of metal ions, EDTA and urea were studied on the human seminal gamma-glytamyltransferase (GGT) in comparison with the human renal GGT. The activity was measured with glycylglycine as an acceptor and with gamma-glutamyl-4-nitroanilide or gamma-glutamyl-3-carboxy-4-nitroanilide as a donor. Because the double-reciprocal plots showed paralled lines, the reaction of seminal GGT proceeds in nonsequence (Ping Pong Bi Bi) mechanism. The acceptor Michaelis constants for the seminal GGT were about 2 times higher than those for the renal enzyme with gamma-glutamyl-3-carboxy-4-nitroanilide as well as gamma-glutamyl-4-nitroanilide as donors, which the donor michaelis constants for seminal GGT were very similar to those for renal enzyme. The optimal pH and pK values were 8.2-8.6 and about 7.7, respectively. There was little difference in the specificity for various acceptors between the seminal and renal enzyme. Glycylglycylglycine was an effective acceptor other than glycylglycine, showing 80% of the activity with glycylgycine. Various substrates including metal ions tested were practically neither inhibitory nor stimulatory for seminal and renal GGTs.