PAF-acetylhydrolases

Platelet-activating factor acetylhydrolases (PAF-AHs, EC 3.1.1.47) constitute a unique subfamily of phospholipases A 2, specific for short acyl chains in the sn-2 position of the phospholipid. Their primary substrate is the platelet-activating factor, PAF, from which they cleave an acetyl moiety wit...

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Bibliographic Details
Published in:BBA - Molecular and Cell Biology of Lipids 1999-11, Vol.1441 (2), p.229-236
Main Authors: Derewenda, Zygmunt S, Ho, Yew S
Format: Article
Language:English
Subjects:
1-Alkyl-2-acetylglycerophosphocholine Esterase
Animals
Brain - enzymology
Catalytic triad
Enzyme structure
Humans
Models, Molecular
Molecular Structure
Phospholipase A2
Phospholipases A - chemistry
Phospholipases A - metabolism
Platelet-activating factor acetylhydrolase
Serine hydrolase
Structure-Activity Relationship
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Summary:Platelet-activating factor acetylhydrolases (PAF-AHs, EC 3.1.1.47) constitute a unique subfamily of phospholipases A 2, specific for short acyl chains in the sn-2 position of the phospholipid. Their primary substrate is the platelet-activating factor, PAF, from which they cleave an acetyl moiety with concomitant release of lysoPAF. However, some acetylhydrolase will also hydrolyze other polar phospholipids with up to 6-carbons long acyl chains in the sn-2 position. PAF-acetylhydrolases are diverse enzymes, and the well-characterized isoforms are serine-dependent hydrolases, which do not require Ca 2+ for activity. Given the existence of two pools of PAF, intra- and extracellular, the acetylhydrolases can be divided into two subclasses: those found in the cytosol and enzymes secreted to blood plasma or other body fluids. Recent crystallographic studies shed new light on the complex structure–function relationships in PAF-AHs.
ISSN:1388-1981
0006-3002
1879-2618
DOI:10.1016/S1388-1981(99)00158-4