The structure and function of platelet-activating factor acetylhydrolases.
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.
Derewenda
Z S
ZS
Department of Molecular Physiology and Biological Physics, University of Virginia Health Sciences Center, Charlottesville 22906-0011, USA.
Derewenda
U
U
D043203:1-Alkyl-2-acetylglycerophosphocholine Esterase; D000818:Animals; D006801:Humans; D008956:Models, Chemical; D008958:Models, Molecular; D010741:Phospholipases A / Q000737:chemistry / Q000502:physiology*; D010972:Platelet Activating Factor / Q000378:metabolism*; D013329:Structure-Activity Relationship
D010972:Platelet Activating Factor; D010741:Phospholipases A; D043203:1-Alkyl-2-acetylglycerophosphocholine Esterase