Feb 25, 1976

Metallophosphoryl and Apophosphoryl Alkaline Phosphatases

The Journal of Biological Chemistry
J F Chlebowski, J E Coleman


The noncovalent phosphate (E-P) and covalent phosphory (E-P) complexes of Zn(II), Cd(II), and apoalkaline phosphatases of Escherichia coli have been studied by stopped flow kinetic methods and 32P-labeling techniques. With 2,4-dinitrophenylphosphate as substrate, preincubation of the Zn(II) enzyme with Pi at pH 8 slows the pre-steady state burst rate, but does not affect the burst magnitude of 1 mol of ROH per enzyme dimer. Preincubation of the enzyme with Pi at pH 5.5 reduces the burst magnitude by one-half, as well as reducing the burst rate. Reduction of the burst magnitude as a function of the pH of the preincubation with Pi follows the same function as that previously established for the formation of E-P. Hence, ROP phosphorylates the enzyme by displacing phosphate from E-P during a pre-steady state reaction, while E-P turns over at the steady state velocity.

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Mentioned in this Paper

Covalent Interaction
Alkalescens-Dispar Group
Phosphoric Monoester Hydrolases
Complex (molecular entity)
Phosphate Measurement
Alkaline Phosphatase

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