| 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).
- ^ * 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.