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Phosphoethanolamine/phosphocholine phosphatase

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Phosphoethanolamine/phosphocholine phosphatase
Identifiers
EC no.3.1.3.75
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
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PMCarticles
PubMedarticles
NCBIproteins

Phosphoethanolamine/phosphocholine phosphatase (EC 3.1.3.75, PHOSPHO1, 3X11A; systematic name phosphoethanolamine phosphohydrolase) is an enzyme highly expressed in mineralizing cells .[1][2][3] This enzyme is implicated in bone and cartilage formation and catalyses the following chemical reactions:

(1) O-phosphoethanolamine + H2O ethanolamine + phosphate
(2) phosphocholine + H2O choline + phosphate

The enzyme is a member of the haloacid dehalogenase superfamily. Like other members of this superfamily it requires a metal ion for catalysis, which is usually Mg2+, it is also active in the presence of Co2+ or Mn2+ but exhibits a lower specific activity with these metal ions.

References

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  1. ^ Houston B, Seawright E, Jefferies D, Hoogland E, Lester D, Whitehead C, Farquharson C (January 1999). "Identification and cloning of a novel phosphatase expressed at high levels in differentiating growth plate chondrocytes". Biochimica et Biophysica Acta. 1448 (3): 500–6. doi:10.1016/s0167-4889(98)00153-0. PMID 9990301.
  2. ^ Stewart AJ, Schmid R, Blindauer CA, Paisey SJ, Farquharson C (December 2003). "Comparative modelling of human PHOSPHO1 reveals a new group of phosphatases within the haloacid dehalogenase superfamily". Protein Engineering. 16 (12): 889–95. doi:10.1093/protein/gzg126. PMID 14983068.
  3. ^ Roberts SJ, Stewart AJ, Sadler PJ, Farquharson C (August 2004). "Human PHOSPHO1 exhibits high specific phosphoethanolamine and phosphocholine phosphatase activities". The Biochemical Journal. 382 (Pt 1): 59–65. doi:10.1042/bj20040511. PMC 1133915. PMID 15175005.
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