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phospholipase-A2 [PLA2] type 3 (Ca+2-dependent PLA2, bee venom phospholipase-A2, phosphatidylcholine 2-acylhydrolase, PLA2-10, group V phospholipase A2, PLA2G5)

Function: - PA2 catalyzes Ca+2-dependent hydrolysis of 2-acyl groups in 3-sn-phosphoglycerides - hydrolyzes L-alpha-1-palmitoyl-2-oleoyl phosphatidylcholine more efficiently than L-alpha-1-palmitoyl-2-arachidonyl phosphatidylcholine, L- alpha-1-palmitoyl-2-arachidonyl phosphatidylethanolamine, or L-alpha-1-stearoyl-2-arachidonyl phosphatidylinositol - may be involved in a) production of lung surfactant, b) remodeling or regulation of cardiac muscle phosphatidylcholine + H2O 1-acylglycerophosphocholine + a carboxylate Cofactor: binds 1 Ca+2 per subunit (putative) Kinetic parameters: - Optimum pH is 6.5, activity remains high up to pH 9.0 Structure: - belongs to the phospholipase A2 family - acks one of 7 disulfide bonds found in similar PA2 proteins Compartment: secreted Expression: heart, placenta > lung

General

Ca+2 binding protein phospholipase A2; phosphatidylcholine 2-acylhydrolase (PLA2) secreted protein

Properties

SIZE: entity length = 138 aa MW = 16 kD COMPARTMENT: extracellular compartment MOTIF: signal sequence {1-20} cysteine residue {C46} MODIFICATION: cysteine residue {C137} Ca+2-binding site SITE: 47-47 cysteine residue {C48} MODIFICATION: cysteine residue {C64} Ca+2-binding site SITE: 49-49 Ca+2-binding site SITE: 51-51 cysteine residue {C63} MODIFICATION: cysteine residue {C117} cysteine residue {C64} MODIFICATION: cysteine residue {C48} histidine residue {H67} Ca+2-binding site SITE: 68-68 cysteine residue {C70} MODIFICATION: cysteine residue {C110} cysteine residue {C79} MODIFICATION: cysteine residue {C103} cysteine residue {C97} MODIFICATION: cysteine residue {C108} cysteine residue {C103} MODIFICATION: cysteine residue {C79} cysteine residue {C108} MODIFICATION: cysteine residue {C97} cysteine residue {C110} MODIFICATION: cysteine residue {C70} aspartate residue {D111} cysteine residue {C117} MODIFICATION: cysteine residue {C63} cysteine residue {C137} MODIFICATION: cysteine residue {C46}

Database Correlations

OMIM 601192 UniProt P39877 Pfam PF00068 KEGG correlations ENZYME 3.1.1.4

References

  1. Mayer RJ, Marshall LA. New insights on mammalian phospholipase A2(s); comparison of arachidonoyl-selective and -nonselective enzymes. FASEB J. 1993 Feb 1;7(2):339-48. Review. PMID: 8440410
  2. Glaser KB, Mobilio D, Chang JY, Senko N. Phospholipase A2 enzymes: regulation and inhibition. Trends Pharmacol Sci. 1993 Mar;14(3):92-8. Review. PMID: 8488570
  3. UniProt :accession P39877