A steady state kinetic study of the hypoxanthine-guanine phosphoribosyltransferase-catalyzed reaction in the forward and the reverse directions was carried out. The results obtained favor a sequential mechanism where the monomagnesium complexes of IMP and PP(i) bind to the enzyme in a rapid equilibrium random fashion while products must dissociate from the enzyme in ordered sequence, first the purine base and then the magnesium complex(es) of P-Rib-PP.
Human hypoxanthine-guanine phosphoribosyltransferase. Steady state kinetics of the forward and reverse reactions / Giacomello, Alessandro; Salerno, Costantino. - In: THE JOURNAL OF BIOLOGICAL CHEMISTRY. - ISSN 0021-9258. - 253:17(1978), pp. 6038-6044.
Human hypoxanthine-guanine phosphoribosyltransferase. Steady state kinetics of the forward and reverse reactions
GIACOMELLO, Alessandro;SALERNO, Costantino
1978
Abstract
A steady state kinetic study of the hypoxanthine-guanine phosphoribosyltransferase-catalyzed reaction in the forward and the reverse directions was carried out. The results obtained favor a sequential mechanism where the monomagnesium complexes of IMP and PP(i) bind to the enzyme in a rapid equilibrium random fashion while products must dissociate from the enzyme in ordered sequence, first the purine base and then the magnesium complex(es) of P-Rib-PP.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
