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Article

Structural and mechanistic insight into covalent substrate binding by Escherichia coli dihydroxyacetone kinase.

Proceedings of the National Academy of Sciences of the United States of America - 25 Jan 2011

Shi Rong, McDonald Laura, Cui Qizhi, Matte Allan, Cygler Miroslaw, Ekiel Irena

Abstract excerpt

The Escherichia coli dihydroxyacetone (Dha) kinase is an unusual kinase because (i) it uses the phosphoenolpyruvate carbohydrate: phosphotransferase system (PTS) as the source of high-energy phosphate, (ii) the active site is formed by two subunits, and (iii) the substrate is covalently bound to His218(K)* of the DhaK subunit. The PTS transfers phosphate to DhaM, which in turn phosphorylates the permanently bound...

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Identifiers

PMID: 21209328
DOI: 10.1073/pnas.1012596108
PMCID: PMC3029771

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PTS

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

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