Biology:Lipid-phosphate phosphatase
From HandWiki
| Lipid-phosphate phosphatase | |||||||||
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| 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 | ||||||||
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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 [math]\displaystyle{ \rightleftharpoons }[/math] (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
References
- ↑ * "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. 2003. doi:10.1073/pnas.0437724100. PMID 12574510. Bibcode: 2003PNAS..100.1558N.
- ↑ "The N-terminal domain of mammalian soluble epoxide hydrolase is a phosphatase". Proc. Natl. Acad. Sci. U.S.A. 100 (4): 1552–7. 2003. doi:10.1073/pnas.0437829100. PMID 12574508. Bibcode: 2003PNAS..100.1552C.
- ↑ "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. 2003. doi:10.1073/pnas.0437724100. PMID 12574510. Bibcode: 2003PNAS..100.1558N.
- ↑ "The N-terminal domain of mammalian soluble epoxide hydrolase is a phosphatase". Proc. Natl. Acad. Sci. U.S.A. 100 (4): 1552–7. 2003. doi:10.1073/pnas.0437829100. PMID 12574508. Bibcode: 2003PNAS..100.1552C.
- "Epoxide hydrolases: mechanisms, inhibitor designs, and biological roles". Annu. Rev. Pharmacol. Toxicol. 45: 311–33. 2005. doi:10.1146/annurev.pharmtox.45.120403.095920. PMID 15822179.
- "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. 2005. doi:10.1021/bi050842g. PMID 16142916.
- "Epoxide hydrolases: their roles and interactions with lipid metabolism". Prog. Lipid Res. 44 (1): 1–51. 2005. doi:10.1016/j.plipres.2004.10.001. PMID 15748653.
- "Polymorphisms in human soluble epoxide hydrolase: effects on enzyme activity, enzyme stability, and quaternary structure". Arch. Biochem. Biophys. 427 (2): 164–9. 2004. doi:10.1016/j.abb.2004.05.003. PMID 15196990.
- "Structure of human epoxide hydrolase reveals mechanistic inferences on bifunctional catalysis in epoxide and phosphate ester hydrolysis". Biochemistry 43 (16): 4716–23. 2004. doi:10.1021/bi036189j. PMID 15096040.
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