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Article

Phosphohistidyl active sites in polyphosphate kinase of Escherichia coli.

Proceedings of the National Academy of Sciences of the United States of America - 10 Dec 1996

Kumble K D, Ahn K, Kornberg A

Abstract excerpt

In the synthesis of inorganic polyphosphate (polyP) from ATP by polyphosphate kinase (PPK; EC 2.7.4.1) of Escherichia coli, an N-P-linked phosphoenzyme was previously identified as the intermediate. The phosphate is presumed to be linked to N3 of the histidine residue because of its chemical stabilities and its resemblance to other enzymes known to contain N3-phosphohistidine. Tryptic digests of [32P]PPK contain...

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Identifiers

PMID: 8962061
DOI: 10.1073/pnas.93.25.14391
PMCID: PMC26142

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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