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. 1976 Dec;73(12):4415-9.
doi: 10.1073/pnas.73.12.4415.

Isolation of 3-phosphohistidine from phosphorylated pyruvate, phosphate dikinase

Isolation of 3-phosphohistidine from phosphorylated pyruvate, phosphate dikinase

A M Spronk et al. Proc Natl Acad Sci U S A. 1976 Dec.

Abstract

Pyruvate, phosphate dikinase (EC 2-7-9-1) catalyzes formation of phosphoenolpyruvate, AMP, and inorganic pyrophosphate from pyruvate, ATP, and orthophosphate. A pyrophosphoryl and phosphoryl form of the enzyme is involved in this transfer. The [32P]phosphoryl form of pyruvate, phosphate dikinase was prepared with enzyme isolated from Bacteroides symbiosus. The [32P]phosphoryl enzyme was found to have properties corresponding to a phosphoramidate linkage and this was confirmed by isolation of 3-[32P]phosphohistidine from alkaline hydrolysates of the enzyme. The histidyl residue is considered to be the pyrophosphoryl- and phosphoryl-carrier between the three substrate sites of this enzyme.

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