EC 3.1.3.76 - Lipid-phosphate phosphatase

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IntEnz Enzyme Nomenclature
EC 3.1.3.76

Names

Accepted name:
lipid-phosphate phosphatase
Other names:
hydroxy fatty acid phosphatase
dihydroxy fatty acid phosphatase
hydroxy lipid phosphatase
sEH [ambiguous]
soluble epoxide hydrolase [ambiguous]
Systematic name:
(9S,10S)-10-hydroxy-9-(phosphonooxy)octadecanoate phosphohydrolase

Reaction

Cofactor

Comments:

Requires Mg2+ for maximal activity. The enzyme from mammals is a bifunctional enzyme: the N-terminal domain exhibits lipid-phosphate-phosphatase activity and the C-terminal domain has the activity of EC 3.3.2.10, soluble epoxide hydrolase (sEH) [1]. The best substrates for this enzyme are 10-hydroxy-9-(phosphonooxy)octadecanoates, with the threo- form being a better substrate than the erythro- form [1]. The phosphatase activity is not found in plant sEH or in EC 3.3.2.9, microsomal epoxide hydrolase, from mammals [1].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0033885
UniProtKB/Swiss-Prot:

References

  1. Newman, J.W., Morisseau, C., Harris, T.R. and Hammock, B.D.
    The soluble epoxide hydrolase encoded by EPXH2 is a bifunctional enzyme with novel lipid phosphate phosphatase activity.
    Proc. Natl. Acad. Sci. USA 100: 1558-1563 (2003). [PMID: 12574510]
  2. Cronin, A., Mowbray, S., Dürk, H., Homburg, S., Fleming, I., Fisslthaler, B., Oesch, F. and Arand, M.
    The N-terminal domain of mammalian soluble epoxide hydrolase is a phosphatase.
    Proc. Natl. Acad. Sci. USA 100: 1552-1557 (2003). [PMID: 12574508]
  3. Morisseau, C. and Hammock, B.D.
    Epoxide hydrolases: mechanisms, inhibitor designs, and biological roles.
    Annu. Rev. Pharmacol. Toxicol. 45: 311-333 (2005). [PMID: 15822179]
  4. Tran, K.L., Aronov, P.A., Tanaka, H., Newman, J.W., Hammock, B.D. and Morisseau, C.
    Lipid sulfates and sulfonates are allosteric competitive inhibitors of the N-terminal phosphatase activity of the mammalian soluble epoxide hydrolase.
    Biochemistry 44: 12179-12187 (2005). [PMID: 16142916]
  5. Newman, J.W., Morisseau, C. and Hammock, B.D.
    Epoxide hydrolases: their roles and interactions with lipid metabolism.
    Prog. Lipid Res. 44: 1-51 (2005). [PMID: 15748653]
  6. Srivastava, P.K., Sharma, V.K., Kalonia, D.S. and Grant, D.F.
    Polymorphisms in human soluble epoxide hydrolase: effects on enzyme activity, enzyme stability, and quaternary structure.
    Arch. Biochem. Biophys. 427: 164-169 (2004). [PMID: 15196990]
  7. Gomez, G.A., Morisseau, C., Hammock, B.D. and Christianson, D.W.
    Structure of human epoxide hydrolase reveals mechanistic inferences on bifunctional catalysis in epoxide and phosphate ester hydrolysis.
    Biochemistry 43: 4716-4723 (2004). [PMID: 15096040]

[EC 3.1.3.76 created 2006]