Phosphoethanolamine/phosphocholine phosphatase

Phosphoethanolamine/phosphocholine phosphatase
Identifiers
EC number 3.1.3.75
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Phosphoethanolamine/phosphocholine phosphatase (EC 3.1.3.75, PHOSPHO1, 3X11A) is an enzyme highly expressed in mineralizing cells with systematic name phosphoethanolamine phosphohydrolase.[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+. PHOSPHO1 is also active in the presence of Co2+ or Mn2+ but exhibits a lower specific activity with these metal ions.

References

  1. Houston, B.; Seawright, E.; Jefferies, D.; Hoogland, E.; Lester, D.; Whitehead, C.; Farquharson, C. (1999). "Identification and cloning of a novel phosphatase expressed at high levels in differentiating growth plate chondrocytes". Biochim. Biophys. Acta. 1448: 500–506. doi:10.1016/s0167-4889(98)00153-0. PMID 9990301.
  2. Stewart, A.J.; Schmid, R.; Blindauer, C.A.; Paisey, S.J.; Farquharson, C. (2003). "Comparative modelling of human PHOSPHO1 reveals a new group of phosphatases within the haloacid dehalogenase superfamily". Protein Eng. 16: 889–895. doi:10.1093/protein/gzg126. PMID 14983068.
  3. Roberts, S.J.; Stewart, A.J.; Sadler, P.J.; Farquharson, C. (2004). "Human PHOSPHO1 displays high specific phosphoethanolamine and phosphocholine phosphatase activities". Biochem. J. 382: 59–65. doi:10.1042/bj20040511. PMID 15175005.
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