The Enzyme Database

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Accepted name: phosphohistidine phosphatase
Reaction: a [protein]-N-phospho-L-histidine + H2O = a [protein]-L-histidine + phosphate
Other name(s): PHPT1 (gene name); protein histidine phosphatase; PHP
Systematic name: [protein]-N-phospho-L-histidine phosphohydrolase
Comments: This eukaryotic enzyme dephosphorylates phosphorylated histidine residues within proteins and peptides. The enzyme acts on phosphate groups attached to both the pros- and tele-nitrogen atoms, but the pros- position is somewhat preferred (by a factor of two at the most) [4]. The substrate specificity depends on the amino acid sequence or structural context of the phosphohistidine in a phosphoprotein. The enzyme is also active on free phosphoramidate [1,4] and peptide-bound phospholysine [5].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
1.  Ek, P., Pettersson, G., Ek, B., Gong, F., Li, J.P. and Zetterqvist, O. Identification and characterization of a mammalian 14-kDa phosphohistidine phosphatase. Eur. J. Biochem. 269 (2002) 5016–5023. [DOI] [PMID: 12383260]
2.  Klumpp, S., Hermesmeier, J., Selke, D., Baumeister, R., Kellner, R. and Krieglstein, J. Protein histidine phosphatase: a novel enzyme with potency for neuronal signaling. J Cereb Blood Flow Metab 22 (2002) 1420–1424. [DOI] [PMID: 12468887]
3.  Baumer, N., Maurer, A., Krieglstein, J. and Klumpp, S. Expression of protein histidine phosphatase in Escherichia coli, purification, and determination of enzyme activity. Methods Mol. Biol. 365 (2007) 247–260. [DOI] [PMID: 17200567]
4.  Attwood, P.V., Ludwig, K., Bergander, K., Besant, P.G., Adina-Zada, A., Krieglstein, J. and Klumpp, S. Chemical phosphorylation of histidine-containing peptides based on the sequence of histone H4 and their dephosphorylation by protein histidine phosphatase. Biochim. Biophys. Acta 1804 (2010) 199–205. [DOI] [PMID: 19836471]
5.  Ek, P., Ek, B. and Zetterqvist, O. Phosphohistidine phosphatase 1 (PHPT1) also dephosphorylates phospholysine of chemically phosphorylated histone H1 and polylysine. Ups J Med Sci 120 (2015) 20–27. [DOI] [PMID: 25574816]
[EC created 2016]

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