“Lipid-phosphate phosphatase”的意思、由来-开放百科全书

词条

Lipid-phosphate phosphatase

释义

References

{{enzyme
| Name = Lipid-phosphate phosphatase
| EC_number = 3.1.3.76
| CAS_number =
| IUBMB_EC_number = 3/1/3/76
| GO_code =
| image =
| width =
| caption =
}}

In enzymology, a lipid-phosphate phosphatase ({{EC number|3.1.3.76}}) is an enzyme that catalyzes the chemical reaction

(9S,10S)-10-hydroxy-9-(phosphonooxy)octadecanoate + H₂O (9S,10S)-9,10-dihydroxyoctadecanoate + phosphate

Thus, the two substrates of this enzyme are (9S,10S)-10-hydroxy-9-(phosphonooxy)octadecanoate and H₂O, whereas its two products are (9S,10S)-9,10-dihydroxyoctadecanoate and phosphate.

This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name of this enzyme class 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).

References

{{cite journal |vauthors=Newman JW, Morisseau C, Harris TR, Hammock BD | date = 2003 | title = The soluble epoxide hydrolase encoded by EPXH2 is a bifunctional enzyme with novel lipid phosphate phosphatase activity | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 100 | pages = 1558–63 | pmid = 12574510 | doi = 10.1073/pnas.0437724100 | issue = 4 | pmc = 149871 }}
{{cite journal |vauthors=Oesch F, Arand M | date = 2003 | title = The N-terminal domain of mammalian soluble epoxide hydrolase is a phosphatase | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 100 | pages = 1552–7 | pmid = 12574508 | doi = 10.1073/pnas.0437829100 | issue = 4 | pmc = 149870 }}
{{cite journal |vauthors=Morisseau C, Hammock BD | date = 2005 | title = Epoxide hydrolases: mechanisms, inhibitor designs, and biological roles | journal = Annu. Rev. Pharmacol. Toxicol. | volume = 45 | pages = 311–33 | pmid = 15822179 | doi = 10.1146/annurev.pharmtox.45.120403.095920 }}
{{cite journal |vauthors=Tran KL, Aronov PA, Tanaka H, Newman JW, Hammock BD, Morisseau C | date = 2005 | title = Lipid sulfates and sulfonates are allosteric competitive inhibitors of the N-terminal phosphatase activity of the mammalian soluble epoxide hydrolase | journal = Biochemistry | volume = 44 | pages = 12179–87 | pmid = 16142916 | doi = 10.1021/bi050842g | issue = 36 | pmc = 1473036 }}
{{cite journal |vauthors=Newman JW, Morisseau C, Hammock BD | date = 2005 | title = Epoxide hydrolases: their roles and interactions with lipid metabolism | journal = Prog. Lipid. Res. | volume = 44 | pages = 1–51 | pmid = 15748653 | doi = 10.1016/j.plipres.2004.10.001 | issue = 1 }}
{{cite journal |vauthors=Srivastava PK, Sharma VK, Kalonia DS, Grant DF | date = 2004 | title = Polymorphisms in human soluble epoxide hydrolase: effects on enzyme activity, enzyme stability, and quaternary structure | journal = Arch. Biochem. Biophys. | volume = 427 | pages = 164–9 | pmid = 15196990 | doi = 10.1016/j.abb.2004.05.003 | issue = 2 }}
{{cite journal |vauthors=Gomez GA, Morisseau C, Hammock BD, Christianson DW | date = 2004 | title = Structure of human epoxide hydrolase reveals mechanistic inferences on bifunctional catalysis in epoxide and phosphate ester hydrolysis | journal = Biochemistry | volume = 43 | pages = 4716–23 | pmid = 15096040 | doi = 10.1021/bi036189j | issue = 16 }}

2 : EC 3.1.3|Enzymes of unknown structure

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