Phospholipase D

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This chapter discusses phospholipase D. Phospholipase D belongs to a class of enzymes that function in a heterogeneous system, cleaving water insoluble substrate. The adsorption of the enzyme at the interface of lipid and water or oil and water is a crucial step for the performance of the catalytic reaction. If the reaction rates are proportional to the interfacial areas, an increase in such surface area should lead to more efficient reactions. The reaction catalyzed by phospholipase D is a reversible transfer of the phosphatidyl moiety between two nucleophilic compounds containing a primary hydroxylic group. With water as acceptor, this reaction can become a hydrolysis and the products can be phosphatidic acid and a water-soluble nucleophile containing a hydroxyl such as choline. Phospholipase D catalyzes reactions involving phospholipids of different forms. This includes a variety of naturally occurring phospholipids containing a mixture of saturated and unsaturated fatty acids that can be presented to the enzyme in a pure form or as soluble or membrane-bound lipoproteins. Phospholipase D from certain sources catalyzes the hydrolysis of a wide range of phospholipids.

References (152)

  • AstrachanL.

    Biochim. Biophys. Acta

    (1973)
  • AudetA. et al.

    Biochim. Biophys. Acta

    (1975)
  • BanghamA.D. et al.

    Biochim. Biophys. Acta

    (1962)
  • BatrakovS.G. et al.

    Biochem. Biophys. Res. Commun.

    (1975)
  • BaumG. et al.

    Anal. Chim. Acta

    (1973)
  • BensonA.A. et al.

    Biochim. Biophys. Acta

    (1958)
  • BilinskiE. et al.

    Biochim. Biophys. Acta

    (1968)
  • BonsenP.P.M. et al.

    Biochim. Biophys. Acta

    (1965)
  • BorkenhagenL.F. et al.

    J. Biol. Chem.

    (1961)
  • BrockerhoffH.

    Bioorg. Chem.

    (1974)
  • ColeR. et al.

    Biochim. Biophys. Acta

    (1974)
  • ComesP. et al.

    Biochim. Biophys. Acta

    (1973)
  • DawsonR.M.C.
  • de HaasG.H. et al.

    Biochim. Biophys. Acta

    (1966)
  • de SiervoA.J. et al.

    Biochim. Biophys. Acta

    (1971)
  • DilsR.R. et al.

    Biochim. Biophys. Acta

    (1959)
  • DilsR.R. et al.

    Biochim. Biophys. Acta

    (1961)
  • EinsetE. et al.

    J. Biol. Chem.

    (1958)
  • FerrariR.A. et al.

    Arch. Biochem. Biophys.

    (1961)
  • FolchJ. et al.

    J. Biol. Chem.

    (1957)
  • GaitiA. et al.

    FEBS Lett.

    (1975)
  • GrossmanS. et al.

    Arch. Biochem. Biophys.

    (1973)
  • HagaT. et al.

    Biochim. Biophys. Acta

    (1973)
  • HanahanD.J. et al.

    J. Biol. Chem.

    (1947)
  • HanahanD.J. et al.

    J. Biol. Chem.

    (1947)
  • HanahanD.J. et al.

    J. Biol. Chem.

    (1948)
  • HaverkateF. et al.

    Biochim. Biophys. Acta

    (1964)
  • HellerM. et al.

    Biochim. Biophys. Acta

    (1970)
  • HellerM. et al.

    Biochim. Biophys. Acta

    (1974)
  • HellerM. et al.
  • HübscherG.

    Biochim. Biophys. Acta

    (1962)
  • HübscherG. et al.

    Biochim. Biophys. Acta

    (1959)
  • JezykP.F. et al.

    Biochim. Biophys. Acta

    (1973)
  • KanferJ.N.

    J. Lipid Res.

    (1972)
  • KatesM.

    Adv. Lipid Res.

    (1970)
  • KatesM. et al.
  • LadbrookeB.D. et al.

    Chem. Phys. Lipids

    (1969)
  • LandsW.E.M. et al.

    Biochim. Biophys. Acta

    (1965)
  • AckerL. et al.

    Z. Lebensm.-Unters. -Forsch.

    (1956)
  • AckerL. et al.

    Biochem. Z.

    (1954)
  • AckerL. et al.

    Nahrung

    (1965)
  • AckerL. et al.

    Biochem. Z.

    (1952)
  • AntiaN.J. et al.

    Can. J. Biochem.

    (1970)
  • AscherY. et al.

    J. Gen. Virol.

    (1969)
  • BanghamA.D. et al.

    Biochem. J.

    (1959)
  • BartlesC.T. et al.

    Biochim. Biophys. Acta

    (1966)
  • Benson, A. A., Freer, S., and Yang, S. F. (1965). Proc. Int. Conf. Biochem. Lipids, 9th, 1965, p....
  • BlighE.G. et al.

    Can. J. Biochem. Physiol.

    (1959)
  • BonsenP.P.M. et al.

    Biochemistry

    (1966)
  • BrockerhoffH. et al.
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