Isolation of 3-phosphohistidine from phosphorylated pyruvate, phosphate dikinase.
- 1 December 1976
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 73 (12) , 4415-4419
- https://doi.org/10.1073/pnas.73.12.4415
Abstract
Pyruvate, phosphate dikinase (EC 2.7.9.1) catalyzes formation of phosphoenolpyruvate, AMP and PPi from pyruvate, ATP and Pi. 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 had 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 3 substrate sites of this enzyme.This publication has 29 references indexed in Scilit:
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