Abstract
AMP inhibition of Candida utilis fructose bisphosphatase (d-fructose-1,6-bisphosphatase 1-phosphohydrolase) has been studied and effects on both V and apparent substrate inhibition have been found. These results have been analyzed by application of both phenomenological and concerted transition two-state models. Both models show that AMP promotes Fru-P2 binding, but a stoichiometry of two Fru-P2 sites per enzyme molecule is allowed by the phenomenological model and not allowed by the two-state model. These results are discussed in the light of recent equilibrium dialysis and quaternary structure experiments.
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