Lipid-phosphate phosphatase
| Lipid-phosphate phosphatase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 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 | ||||||||
| |||||||||
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 (9S,10S)-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
[edit]References
[edit]- ^ * 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. Bibcode:2003PNAS..100.1558N. 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. Bibcode:2003PNAS..100.1552C. doi:10.1073/pnas.0437829100. PMC 149870. PMID 12574508.
- ^ 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. Bibcode:2003PNAS..100.1558N. 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. Bibcode:2003PNAS..100.1552C. 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.
