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Abstract The forward reaction catalyzed by galactosyltransferase has been studied kinetically at pH 8.0 with N-acetylglucosamine as the galactosyl group acceptor. From the results of initial velocity studies, as well as investigations of the deadend inhibition by UDP-glucose and the substrate inhibition by higher concentrations of N-acetylglucosamine, it has been concluded that the reaction has an ordered mechanism with the reactants adding in the order: Mn2+, UDP-galactose, N-acetylglucosamine. A further conclusion is that Mn2+ reacts with the free enzyme under conditions of thermodynamic equilibrium and does not dissociate after each catalytic cycle. Values are reported for the various kinetic parameters.
Morrison et al. (1971) studied this question.