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- W208049287 abstract "The PPase reaction requires the participation of three metal ion cofactors. One metal ion binds to PP activating it for reaction and the other two bind to the enzyme activating it for catalysis. Of the metal ions tested only Mg/sup 2 +/, Zn/sup 2 +/, Co/sup 2 +/, Mn/sup 2 +/ can perform all these roles. Most trivalent metal ions can function to activate the PP for reaction but cannot activate the enzyme for catalysis. The Mg/sup 2 +/ activated enzyme is specific for M-PP and M-PPS complexes while the Zn/sup 2 +/ activated enzyme also acts on metal complexes of PPP, PPPOR, PPOR and PPF. /sup 18/O-Incorporation studies show that the substituted phosphoryl group of the unsymmetrical PP complexes always serves as the leaving group. To gain insight into the mechanism of the cofactor control over the substrate specificity the order of substrate/cofactor binding to the enzyme was examined. Dead end inhibition studies in which Cr(III)PP served as substrate and Mg/sup 2 +/ as cofactor indicate that the mechanism is rapid equilibrium ordered (CrPP binds first) while dead end inhibitor induced activator inhibition studies with Mg/sup 2 +/ and MgPP indicate that the kinetic mechanism is steady state preferredmore » order. Cofactor-enzyme binding was studied as a function of substrate structure and the results obtained rule out interference of Mg/sup 2 +/ binding by substrate analogs as an explanation for the different substrate specificities of the Zn/sup 2 +/ and Mg/sup 2 +/ activated enzymes.« less" @default.
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- W208049287 date "1986-05-01" @default.
- W208049287 modified "2023-09-23" @default.
- W208049287 title "Investigation of the cofactor controlled substrate specificity of yeast inorganic pyrophosphatase" @default.
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