Lipid-phosphate phosphatase explained
The enzyme lipid-phosphate phosphatase[1] [2] [3] [4] (EC 3.1.3.76) catalyzes the reaction
(9S,10S)-10-hydroxy-9-(phosphonooxy)octadecanoate + H2O
(9
S,10
S)-9,10-dihydroxyoctadecanoate + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name 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).
See also
References
- Morisseau C, Hammock BD . 2005 . Epoxide hydrolases: mechanisms, inhibitor designs, and biological roles . Annu. Rev. Pharmacol. Toxicol. . 45 . 311 - 33 . 15822179 . 10.1146/annurev.pharmtox.45.120403.095920 .
- 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 . 16142916 . 10.1021/bi050842g . 36 . 1473036 .
- Newman JW, Morisseau C, Hammock BD . 2005 . Epoxide hydrolases: their roles and interactions with lipid metabolism . Prog. Lipid Res. . 44 . 1 - 51 . 15748653 . 10.1016/j.plipres.2004.10.001 . 1 .
- 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 . 15196990 . 10.1016/j.abb.2004.05.003 . 2 .
- David W. Christianson. 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 . 15096040 . 10.1021/bi036189j . 16 .
Notes and 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 . 1558 - 63 . 12574510 . 10.1073/pnas.0437724100 . 4 . 149871 . 2003PNAS..100.1558N . free .
- 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 . 12574508 . 10.1073/pnas.0437829100 . 4 . 149870 . 2003PNAS..100.1552C . free .
- 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 . 12574510 . 10.1073/pnas.0437724100 . 4 . 149871 . 2003PNAS..100.1558N . free .
- 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 . 12574508 . 10.1073/pnas.0437829100 . 4 . 149870 . 2003PNAS..100.1552C . free .