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• W1503670641 abstract "1 For the Zn2+-phosphatase, the ratio k3/k2 (pH 8.4) of the dephosphorylation (k3) and phosphorylation (k2) rates is very similar, about 1.4–1.7, for substrates which are very different chemically such as p-nitrophenyl phosphate, β-glycerophosphate, 5′-AMP and ATP. This means that k2 is nearly the same for all these substrates. On the other hand with o-carboxyphenyl phosphate, phosphorylation is the determining step. 2 The Co2+-enzyme has a much lower specific activity than the Zn2+-phosphatase. The substitution of Zn2+ by Co2+ decreased the rate of phosphorylation by a factor of 6.4 for o-carboxyphenyl phosphate and 16 for the above mentioned substrates; no such decrease is observed on k3. The phosphorylation is inhibited by nucleophilic agents which otherwise activate the Zn2+-enzyme in the same conditions. The Co2+-phosphatase offers a unique opportunity to compare the free energy of binding of the different substrates to form the Michaelis complex; those free energies are strikingly similar, they vary between – 6.1 and – 7.0 kcal. This is further evidence that specificity of the enzyme is not directed against the R part of RO PO3 even in such a peculiar case as ATP. Neither the Zn2+ nor the Co2+-enzyme are able to catalyse the hydrolysis of a P-N bond. Organic phosphates (P-O bond) bind better to the phosphatase than p-chloro-anilido-phosphonic acid (P-N bond). The exchange of Zn2+ by Co2+ decrease only slightly the affinity for the active center of organic substrates or inhibitors; a factor of 1.78 for o-carboxyphenyl phosphate and 2.65 for p-chloroanilido-phosphonic acid. The difference is more pronounced for inorganic phosphate; a factor of 23 (pH 9.16) and 27 (pH 8.5). 3 Two ionisable groups are important for the binding of the substrate to the active center. One must be in the basic form, it has a pK of 7.1 and 7.4 in the Zn2+ and Co2+-phosphatase, respectively. The other must be acidic, the corresponding pK values are 8.6 and 8.9, respectively. With both metallo-enzymes the phosphorylation step is pH-independent between pH 6 and 9. The dephosphorylation step is dependent upon the ionization of a group which must be in the basic form and has a pK of 7.5 for the Zn2+-phosphatase. 4 The enzyme remains dimeric in the course of the catalysis and it seems that there is only one active site phosphorylated per dimer. k 2 and k3 are decreased in 2H2O indicating possibly rate-determining proton transfers. The enthalpy and entropy of activation corresponding to both steps have been calculated." @default.
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• W1503670641 date "1969-01-01" @default.
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• W1503670641 title "Zn2+ and Co2+-Alkaline Phosphatases of E. coli. A Comparative Kinetic Study" @default.
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• W1503670641 doi "https://doi.org/10.1111/j.1432-1033.1969.tb19606.x" @default.
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