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Relationship between Structure and Activity of Pancreatic Phospholipase A2

  • A. J. Slotboom
  • M. C. E. van Dam-Mieras
  • E. H. J. M. Jansen
  • F. Pattus
  • H. M. Verheij
  • G. H. de Haas
Part of the Advances in Experimental Medicine and Biology book series (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).

Keywords

Critical Micellar Concentration Substrate Analog Pancreatic Phospholipase Direct Binding Study Micellar Substrate 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1978

Authors and Affiliations

  • A. J. Slotboom
    • 1
  • M. C. E. van Dam-Mieras
    • 1
  • E. H. J. M. Jansen
    • 1
  • F. Pattus
    • 1
  • H. M. Verheij
    • 1
  • G. H. de Haas
    • 1
  1. 1.Laboratory of BiochemistryState University of UtrechtUtrechtThe Netherlands

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