The structure and function of platelet-activating factor acetylhydrolases |
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| Authors: | Z. S. Derewenda U. Derewenda |
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| Affiliation: | (1) Department of Molecular Physiology and Biological Physics and Center for Structural Biology, University of Virginia Health Sciences Center, P.O. Box 1011, Charlottesville (Virginia 22906-0011, USA), Fax +1 804 243 6843, e-mail: zsd4n@virginia.edu, US |
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| Abstract: | Platelet-activating factor acetylhydrolases (PAF-AHs, EC 3.1.1.47) constitute a unique and biologically important family of phospholipase A2s. They are related to neither the well-characterized secretory nor cytosolic PLA2s, and unlike them do not require Ca2+ for catalytic activity. The distinguishing property of PAF-AHs is their unique substrate specificity they act on the phospholipid platelet-activating factor (PAF), and in some cases on proinflammatory polar phospholipids, from which they remove a short acyl moiety – acetyl in the case of PAF – located at the sn-2 position. Because PAF is found both in the plasma and in the cytosol of many tissues, PAF-acetylhydrolases are equally widely distributed in an animal organism. Recent crystallographic studies shed new light on the complex structure-function relationships in PAF-AHs. Received 15 September 1997; received after revision 23 February 1998; accepted 25 February 1998 |
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| Keywords: | . Platelet-activating factor acetylhydrolase α /β hydrolase phospholipase A2 molecular modelling. |
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