Lipid-phosphate phosphatase

Lipid-phosphate phosphatase
Identifiers
EC number	3.1.3.76
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Search PMC articles PubMed articles NCBI proteins

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).

References

• 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 (4): 1558–63. doi:10.1073/pnas.0437724100. PMC 149871. 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 (4): 1552–7. doi:10.1073/pnas.0437829100. PMC 149870. 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 (36): 12179–87. doi:10.1021/bi050842g. PMC 1473036. PMID 16142916.
• Newman JW, Morisseau C, Hammock BD (2005). "Epoxide hydrolases: their roles and interactions with lipid metabolism". Prog. Lipid. Res. 44 (1): 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 (2): 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 (16): 4716–23. doi:10.1021/bi036189j. PMID 15096040.