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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
- 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
- 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
- UniProt :accession P39877