Phosphoethanolamine/phosphocholine phosphatase

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

\rightleftharpoons

ethanolamine + phosphate

(2) phosphocholine + H₂O

\rightleftharpoons

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

↑ Houston, B., Seawright, E., Jefferies, D., Hoogland, E., Lester, D., Whitehead, C. and 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.
↑ Stewart, A.J., Schmid, R., Blindauer, C.A., Paisey, S.J. and 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.
↑ Roberts, S.J., Stewart, A.J., Sadler, P.J. and Farquharson, C. (2004). "Human PHOSPHO1 displays high specific phosphoethanolamine and phosphocholine phosphatase activities". Biochem. J. 382: 59–65. doi:10.1042/bj20040511. PMID 15175005.

External links

Phosphoethanolamine/phosphocholine phosphatase at the US National Library of Medicine Medical Subject Headings (MeSH)

Hydrolase: esterases (EC 3.1)

3.1.1: Carboxylic
ester hydrolases

Lipase

Phospholipase
- A1
- A2
- B

3.1.2: Thioesterase

3.1.3: Phosphatase

3.1.4: Phosphodiesterase

3.1.6: Sulfatase

Nuclease (includes
deoxyribonuclease and
ribonuclease)

3.1.11-16: Exonuclease

Exodeoxyribonuclease	RecBCD

Exoribonuclease	Oligonucleotidase

3.1.21-31: Endonuclease

Endodeoxyribonuclease	Deoxyribonuclease I Deoxyribonuclease II Deoxyribonuclease IV Restriction enzyme UvrABC endonuclease

Endoribonuclease	RNase III RNase H 1 2A 2B 2C RNase P RNase A 1 2 3 4/5 RNase T1 RNA-induced silencing complex

either deoxy- or ribo-	Aspergillus nuclease S1 Micrococcal nuclease

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

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