H
IPR036444

Phospholipase A2 domain superfamily

InterPro entry
Short namePLipase_A2_dom_sf
Overlapping entries
 
Phospholipase A2 (IPR001211)

Description

Proteins containing this domain superfamily include eukaryotic and prokaryotic phospholipase A2 enzymes (PLA2;
3.1.1.4
), small lipolytic enzymes that releases fatty acids from the second carbon group of glycerol, usually in a metal-dependent reaction, to generate lysophospholipid (LysoPL) and a free fatty acid (FA)
[1]
. The resulting products are either dietary or used in synthetic pathways for leukotrienes and prostaglandins. Often, arachidonic acid is released as a free fatty acid and acts as second messenger in signaling networks
[2]
. These enzymes enable the of fatty acids and lysophospholipid by hydrolysing the 2-ester bond of 1,2-diacyl-3-sn-phosphoglycerides. In eukaryotes, PLA2 plays a pivotal role in the biosynthesis of prostaglandin and other mediators of inflammation. These enzymes are either secreted or cytosolic; the latter are either Ca dependent or Ca independent. Secreted PLA2s have also been found to specifically bind to a variety of soluble and membrane proteins in mammals, including receptors
[4]
. As a toxin, PLA2 is a potent presynaptic neurotoxin which blocks nerve terminals by binding to the nerve membrane and hydrolyzing stable membrane lipids
[3]
. The products of the hydrolysis (LysoPL and FA) cannot form bilayers leading to a change in membrane conformation and ultimately to a block in the release of neurotransmitters
[7, 6, 5]
.

References

1.Phospholipase A2. Murakami M, Kudo I. J. Biochem. 131, 285-92, (2002). View articlePMID: 11872155

2.Regulation and inhibition of phospholipase A2. Balsinde J, Balboa MA, Insel PA, Dennis EA. Annu. Rev. Pharmacol. Toxicol. 39, 175-89, (1999). View articlePMID: 10331081

3.Modulation of phospholipase A2 activity generated by molecular evolution. Betzel C, Genov N, Rajashankar KR, Singh TP. Cell. Mol. Life Sci. 56, 384-97, (1999). View articlePMID: 11212293

4.Diversity and regulatory functions of mammalian secretory phospholipase A2s. Murakami M, Kudo I. Adv. Immunol. 77, 163-94, (2001). View articlePMID: 11293116

5.Equivalent effects of snake PLA2 neurotoxins and lysophospholipid-fatty acid mixtures. Rigoni M, Caccin P, Gschmeissner S, Koster G, Postle AD, Rossetto O, Schiavo G, Montecucco C. Science 310, 1678-80, (2005). View articlePMID: 16339444

6.How do presynaptic PLA2 neurotoxins block nerve terminals? Montecucco C, Rossetto O. Trends Biochem. Sci. 25, 266-70, (2000). View articlePMID: 10838563

7.Presynaptic enzymatic neurotoxins. Rossetto O, Morbiato L, Caccin P, Rigoni M, Montecucco C. J. Neurochem. 97, 1534-45, (2006). View articlePMID: 16805767

Further reading

8. Crystal structure of human group X secreted phospholipase A2. Electrostatically neutral interfacial surface targets zwitterionic membranes. Pan YH, Yu BZ, Singer AG, Ghomashchi F, Lambeau G, Gelb MH, Jain MK, Bahnson BJ. J. Biol. Chem. 277, 29086-93, (2002). View articlePMID: 12161451

9. Structure and mechanism of human cytosolic phospholipase A(2). Dessen A. Biochim. Biophys. Acta 1488, 40-7, (2000). View articlePMID: 11080675

10. The crystal structure of prokaryotic phospholipase A2. Matoba Y, Katsube Y, Sugiyama M. J. Biol. Chem. 277, 20059-69, (2002). View articlePMID: 11897785

GO terms

Cross References

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