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Article

Structural analysis of the bacterial HPr kinase/phosphorylase V267F mutant gives insights into the allosteric regulation mechanism of this bifunctional enzyme.

The Journal of biological chemistry - 30 Nov 2007

Chaptal Vincent, Vincent Fanny, Gueguen-Chaignon Virginie, Monedero Vicente, Poncet Sandrine, Deutscher Josef, Nessler Sylvie, Morera Solange

Abstract excerpt

The HPr kinase/phosphorylase (HPrK/P) is a bifunctional enzyme that controls the phosphorylation state of the phospho-carrier protein HPr, which regulates the utilization of carbon sources in Gram-positive bacteria. It uses ATP or pyrophosphate for the phosphorylation of serine 46 of HPr and inorganic phosphate for the dephosphorylation of Ser(P)-46-HPr via a phosphorolysis reaction. HPrK/P is a hexameric protein...

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PMID: 17878158
DOI: 10.1074/jbc.M705979200

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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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