Apr 6, 1976

31P nuclear magnetic resonance study of alkaline phosphatase: the role of inorganic phosphate in limiting the enzyme turnover rate at alkaline pH

Biochemistry
W E HullB D Sykes

Abstract

31P nuclear magnetic resonance (NMR) was used to directly observe the binding of inorganic phosphate to alkaline phosphatase. Evidencq for the tight binding of 1.5-2.0 mol of inorganic phosphate per dimer of alkaline phosphatase is presented. Two distinct forms of bound phosphate are observed, one predominating above pH 7 and representing the non-covalent E-P1 complex and the other predominating below pH 5 and representing the covalent E-P1 complex. The 31P NMR line width of the E-P1 complex indicates that the dissociation of noncovalent phosphate is the rate-limiting step in the turnover of the enzyme at high pH.

Mentioned in this Paper

In Vivo NMR Spectroscopy
Alkalescens-Dispar Group
Alkaline Phosphatase
Plasma Protein Binding Capacity
Zinc
Protein Conformation
Orthophosphate
Cadmium
Physical Dialysis
Hydrogen-Ion Concentration

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