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Relationship between Structure and Activity of Pancreatic Phospholipase A2

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Enzymes of Lipid Metabolism

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 101))

Abstract

Phospholipase A2 (EC 3.1.1.4) hydrolyzes exclusively the 2­acyl ester linkage of all types of naturally occurring phosphogly­cerides (1). The enzyme acts highly stereospecific and only 3-sn­phosphoglycerides are hydrolyzed, while the stereoisomeric 1-sn­-phosphoglycerides are competitive inhibitors (2). The pancreatic phospholipase A2 has a nearly absolute requirement for Ca2+ ions which bind in a 1:1 molar ratio to the enzyme at the catalytic or high-affinity site. Ba2+ and Sr2+ ions are competitive inhibitors, while Mg2+ ions are indifferent (3). So far only Gd3+ and Tb3+ ions can replace Ca2+ ions with retention of some activity (4).

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Authors and Affiliations

  1. Laboratory of Biochemistry, State University of Utrecht, Transitorium 3, University Centre “De Uithof”, Padua­laan 8, Utrecht, The Netherlands

    A. J. Slotboom, M. C. E. van Dam-Mieras, E. H. J. M. Jansen, F. Pattus, H. M. Verheij & G. H. de Haas

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  1. A. J. Slotboom
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  2. M. C. E. van Dam-Mieras
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  3. E. H. J. M. Jansen
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  4. F. Pattus
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  5. H. M. Verheij
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  6. G. H. de Haas
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Editors and Affiliations

  1. Department of Biochemistry, The Hebrew University, Hadassah Medical School, P.O. Box 1172, Jerusalem, Israel

    Shimon Gatt

  2. C.N.R.S. Center for Neurochemistry, Louis Pasteur University, 11 rue Humann, 67085, Strasbourg Cedex, France

    Louis Freysz  & Paul Mandel  & 

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© 1978 Plenum Press, New York

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Slotboom, A.J., van Dam-Mieras, M.C.E., Jansen, E.H.J.M., Pattus, F., Verheij, H.M., de Haas, G.H. (1978). Relationship between Structure and Activity of Pancreatic Phospholipase A2 . In: Gatt, S., Freysz, L., Mandel, P. (eds) Enzymes of Lipid Metabolism. Advances in Experimental Medicine and Biology, vol 101. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-9071-2_13

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  • DOI: https://doi.org/10.1007/978-1-4615-9071-2_13

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4615-9073-6

  • Online ISBN: 978-1-4615-9071-2

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