ABSTRACT
The hydrolysis and transfer reactions of purified human renal gamma-glutamyltransferase were studied in vitro with glutathione as substrate at pH and substrate concentration reflecting the physiological conditions. The pH optimum ranged from 7.48 to 8.44 for hydrolysis and 7.90 to 8.92 for transfer with glutamine as acceptor. The Michaelis constants for glutathione were 13 microM in hydrolysis and 58 microM in transfer reactions respectively. Inhibition of transfer occurred for glutathione concentrations above 0.4 mM. Various ions, urea, creatinine, uric acid and L-amino acids were shown to have no appreciable effect on both reactions except L-glutamine which acts as an activator on the hydrolysis activity. Taken together, our results, if they are transposable in vivo would be relevant of an enzyme acting like an hydrolase rather than like a transferase.
