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Lipid-phosphate phosphatase

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Class 3 Hydrolases

Part of the book series: Springer Handbook of Enzymes ((HDBKENZYMES,volume S5))

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References

  1. Gomez, G.A.; Morisseau, C.; Hammock, B.D.; Christianson, D.W.: Structure of human epoxide hydrolase reveals mechanistic inferences on bifunctional catalysis in epoxide and phosphate ester hydrolysis. Biochemistry, 43, 4716–4723 (2004)

    Article  PubMed  CAS  Google Scholar 

  2. Newman, J.W.; Morisseau, C.; Harris, T.R.; Hammock, B.D.: The soluble epoxide hydrolase encoded by EPXH2 is a bifunctional enzyme with novel lipid phosphate phosphatase activity. Proc. Natl. Acad. Sci. USA, 100, 1558–1563 (2003)

    Article  PubMed  CAS  Google Scholar 

  3. Srivastava, P.K.; Sharma, V.K.; Kalonia, D.S.; Grant, D.F.: Polymorphisms in human soluble epoxide hydrolase: effects on enzyme activity, enzyme stability, and quarternary structure. Arch. Biochem. Biophys., 427, 164–169 (2004)

    Article  PubMed  CAS  Google Scholar 

  4. Enayetallah, A.E.; Grant, D.F.: Effects of human soluble epoxide hydrolase polymorphisms on isoprenoid phosphate hydrolysis. Biochem. Biophys. Res. Commun., 341, 254–260 (2006)

    Article  PubMed  CAS  Google Scholar 

  5. Tran, K.L.; Aronov, P.A.; Tanaka, H.; Newman, J.W.; Hammock, B.D.; Morisseau, C.: Lipid sulfates and sulfonates are allosteric competitive inhibitors of the N-terminal phosphatase activity of the mammalian soluble poxide hydrolase. Biochemistry, 44, 12179–12187 (2005)

    Article  PubMed  CAS  Google Scholar 

  6. Cronin, A.; Mowbray, S.; Duerk, H.; Homburg, S.; Fleming, I.; Fisslthaler, B.; Oesch, F.; Arand, M.: The N-terminal domain of mammalian soluble epoxide hydrolase is a phosphatase. Proc. Natl. Acad. Sci. USA, 100, 1552–1557 (2003)

    Article  PubMed  CAS  Google Scholar 

  7. Newman, J.W.; Morisseau, C.; Hammock, B.D.: Epoxide hydrolases: their roles and interactions with lipid metabolism. Prog. Lipid Res., 44, 1–51 (2005)

    Article  PubMed  CAS  Google Scholar 

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© 2009 Springer-Verlag Berlin Heidelberg

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(2009). Lipid-phosphate phosphatase. In: Chang, A. (eds) Class 3 Hydrolases. Springer Handbook of Enzymes, vol S5. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-540-85703-7_15

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