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Biochim Biophys Acta. 2000 Oct 31;1488(1-2):40-7.

Structure and mechanism of human cytosolic phospholipase A(2).

Author information

1
Institut de Biologie Structurale Jean-Pierre Ebel, 41 rue Jules Horowitz, 38027, Grenoble, France. dessen@ibs.fr

Abstract

cPLA(2) is an 85-kDa enzyme whose primary function, the release of arachidonic acid from phospholipid membranes, is a crucial reaction in the metabolism of lipid mediators of inflammation. cPLA(2) consists of two domains: an N-terminal, C2-type unit analogous to those present in other membrane-targeting molecules, and a catalytic domain harboring an active site dyad at the bottom of a deep, mostly hydrophobic catalytic funnel. The absence of a third active site residue in the cPLA(2) cleft, as observed in other lipases, suggests that the enzyme proceeds through a novel catalytic mechanism. Crystallographic and biochemical studies of cPLA(2) will provide essential information for the development of small molecule inhibitors which may be employed in the control of inflammatory and other highly regulated processes.

PMID:
11080675
DOI:
10.1016/s1388-1981(00)00108-6
[Indexed for MEDLINE]

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