Lipid-phosphate phosphatase

From Wikipedia, the free encyclopedia

In enzymology, a lipid-phosphate phosphatase (EC 3.1.3.76) is an enzyme that catalyzes the chemical reaction

(9S,10S)-10-hydroxy-9-(phosphonooxy)octadecanoate + H₂O $\rightleftharpoons$ (9S,10S)-9,10-dihydroxyoctadecanoate + phosphate

Thus, the two substrates of this enzyme are (9S,10S)-10-hydroxy-9-(phosphonooxy)octadecanoate and H₂O, whereas its two products are (9S,10S)-9,10-dihydroxyoctadecanoate and phosphate.

This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name of this enzyme class is (9S,10S)-10-hydroxy-9-(phosphonooxy)octadecanoate phosphohydrolase. Other names in common use include hydroxy fatty acid phosphatase, dihydroxy fatty acid phosphatase, hydroxy lipid phosphatase, sEH (ambiguous), and soluble epoxide hydrolase (ambiguous).

[edit] References

IUBMB entry for 3.1.3.76
BRENDA references for 3.1.3.76 (Recommended.)
PubMed references for 3.1.3.76
PubMed Central references for 3.1.3.76
Google Scholar references for 3.1.3.76
Newman JW, Morisseau C, Harris TR, Hammock BD (2003). "The soluble epoxide hydrolase encoded by EPXH2 is a bifunctional enzyme with novel lipid phosphate phosphatase activity". Proc. Natl. Acad. Sci. U. S. A. 100: 1558–63. doi:10.1073/pnas.0437724100. PMID 12574510.
Oesch F, Arand M (2003). "The N-terminal domain of mammalian soluble epoxide hydrolase is a phosphatase". Proc. Natl. Acad. Sci. U. S. A. 100: 1552–7. doi:10.1073/pnas.0437829100. PMID 12574508.
Morisseau C, Hammock BD (2005). "Epoxide hydrolases: mechanisms, inhibitor designs, and biological roles". Annu. Rev. Pharmacol. Toxicol. 45: 311–33. doi:10.1146/annurev.pharmtox.45.120403.095920. PMID 15822179.
Tran KL, Aronov PA, Tanaka H, Newman JW, Hammock BD, Morisseau C (2005). "Lipid sulfates and sulfonates are allosteric competitive inhibitors of the N-terminal phosphatase activity of the mammalian soluble epoxide hydrolase". Biochemistry. 44: 12179–87. doi:10.1021/bi050842g. PMID 16142916.
Newman JW, Morisseau C, Hammock BD (2005). "Epoxide hydrolases: their roles and interactions with lipid metabolism". Prog. Lipid. Res. 44: 1–51. doi:10.1016/j.plipres.2004.10.001. PMID 15748653.
Srivastava PK, Sharma VK, Kalonia DS, Grant DF (2004). "Polymorphisms in human soluble epoxide hydrolase: effects on enzyme activity, enzyme stability, and quaternary structure". Arch. Biochem. Biophys. 427: 164–9. doi:10.1016/j.abb.2004.05.003. PMID 15196990.
Gomez GA, Morisseau C, Hammock BD, Christianson DW (2004). "Structure of human epoxide hydrolase reveals mechanistic inferences on bifunctional catalysis in epoxide and phosphate ester hydrolysis". Biochemistry. 43: 4716–23. doi:10.1021/bi036189j. PMID 15096040.