Human hypoxanthine-guanine phosphoribosyltransferase. IMP-GMP exchange stoichiometry and steady state kinetics of the reaction.
Steady state kinetics of hypoxanthine guanine phosphoribosyltransferase-catalyzed reactions are studied. The results obtained suggest that IMP, GMP, P-Rib-PP, and pyrophosphate bind to the same enzyme form, while hypoxanthine and guanine bind to a different form. Guanine activates IMP-pyrophosphorolysis. During the reaction guanine and IMP are consumed with formation of GM
D004912:Erythrocytes / Q000201:enzymology*; D006157:Guanosine Monophosphate; D006801:Humans; D007041:Hypoxanthine Phosphoribosyltransferase / Q000097:blood*; D007291:Inosine Monophosphate; D007700:Kinetics; D008433:Mathematics
D007291:Inosine Monophosphate; D006157:Guanosine Monophosphate; D007041:Hypoxanthine Phosphoribosyltransferase