Author/Authors
O. Hayes Griffith، نويسنده , , Margret Ryan، نويسنده ,
DocumentNumber
1601525
Title Of Article
Platelet-activating factor acetylhydrolases (PAF-AHs, EC 3.1.1.47) constitute a unique subfamily of phospholipases A2, specific for short acyl chains in the sn-2 position of the phospholipid. Their primary substrate is the platelet-activating factor, PAF,
شماره ركورد
11748
Latin Abstract
The bacterial phosphatidylinositol-specific phospholipase C (PI-PLC) is a small, water-soluble enzyme that cleaves the natural membrane lipids PI, lyso-PI, and glycosyl-PI. The crystal structure, NMR and enzymatic mechanism of bacterial PI-PLCs are reviewed. These enzymes consist of a single domain folded as a (βα)8-barrel (TIM barrel), are calcium-independent, and interact weakly with membranes. Sequence similarity among PI-PLCs from different bacterial species is extensive, and includes the residues involved in catalysis. Bacterial PI-PLCs are structurally similar to the catalytic domain of mammalian PI-PLCs. Comparative studies of both prokaryotic and eukaryotic isozymes have proved useful for the identification of distinct regions of the proteins that are structurally and functionally important.
From Page
237
NaturalLanguageKeyword
phosphotransferase , catalytic mechanism , Phosphoinositide-speci¢c phospholipase C , Phosphodiesterase , Phosphatidylinositol-speci¢c phospholipase C
JournalTitle
Studia Iranica
To Page
254
To Page
254
Link To Document