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IUBMB Comments Also acts on phosphatidylethanolamine, choline plasmalogen and phosphatides, removing the fatty acid attached to the 2-position. Requires Ca2+.
The taxonomic range for the selected organisms is: Naja kaouthia The enzyme appears in selected viruses and cellular organisms
Synonyms
phospholipase a2, cpla2, spla2, spla(2), prdx6, cytosolic phospholipase a2, crotoxin, pla2s, ipla2, spla2-iia,
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14 kDa phospholipase A2
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Basic protein I/II
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Group IB phospholipase A2
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Group IIA phospholipase A2
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Group V phospholipase A2
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Group VI phospholipase A2
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Muscarinic inhibitor
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Non-pancreatic secretory phospholipase A2
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pgPLA 1a/pgPLA 2a
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phosphatide 2-acylhydrolase
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phosphatidolipase
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Phosphatidylcholine 2-acylhydrolase
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Phosphatidylcholine 2-acylhydrolase GIIC
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Phosphatidylcholine 2-acylhydrolase GIID
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Phosphatidylcholine 2-acylhydrolase GIIE
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Phosphatidylcholine 2-acylhydrolase GIIF
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Phosphatidylcholine 2-acylhydrolase GIII
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Phosphatidylcholine 2-acylhydrolase GX
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Phosphatidylcholine 2-acylhydrolase GXII
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Phosphatidylcholine 2-acylhydrolase GXIII
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Phospholipase A2 inhibitor
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platelet activating factor acetyl hydrolase
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Secretory-type PLA, stroma-associated homolog
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hydrolysis of carboxylic ester
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-, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -
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phosphatidylcholine 2-acylhydrolase
Also acts on phosphatidylethanolamine, choline plasmalogen and phosphatides, removing the fatty acid attached to the 2-position. Requires Ca2+.
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phosphatidylcholine + H2O
1-acylglycerophosphocholine + fatty acid
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preferred substrate for both isoenzymes, NK-PLA2-I and NK-PLA2-II
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phosphatidylethanolamine + H2O
1-acylglycerophosphorylethanolamine + fatty acid
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phosphatidylserine + H2O
1-acylglycerophosphoserine + fatty acid
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additional information
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additional information
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both isoenzymes NK-PLA2-I and NK-PLA2-II cause significantly more damage to mitochondrial membranes as compared to erythrocyte membranes
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additional information
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isoenzyme NK-PLA2-I does not discriminate between saturated and unsaturated fatty acids whereas isoenzyme NK-PLA2-II shows a preference for unsaturated fatty acids
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additional information
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both isoenzymes NK-PLA2-I and NK-PLA2-II cause significantly more damage to mitochondrial membranes as compared to erythrocyte membranes
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4-bromophenacyl bromide
selectively and irreversibly modifies the His48 residue in the active site
p-bromophenacylbromide
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i.e. pBPB, 3.3 mM, 95% inhibition of isoenzyme NK-PLA2-I, 89% inhibition of isoenzyme NK-PLA2-II
additional information
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not inhibitory to both isoenzymes: p-methylsulfonylfluoride, tosyl-L-phenylalaninchlormethylketon, N-bromosuccinamide, tosyl-L-lysinechlormethylketon
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101.2
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isoenzyme NK-PLA2-I, substrate phosphatidylserine, sn-2 fatty acid C18:1, 25°C
133
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isoenzyme NK-PLA2-II, substrate phosphatidylcholine, sn-2 fatty acid C16:0, 25°C
153.9
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isoenzyme NK-PLA2-II, substrate phosphatidylcholine, sn-2 fatty acid C18:0, 25°C
178.4
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isoenzyme NK-PLA2-I, substrate phosphatidylcholine, sn-2 fatty acid C18:1, 25°C
202.3
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isoenzyme NK-PLA2-I, substrate phosphatidylcholine, sn-2 fatty acid C18:2, 25°C
218.4
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isoenzyme NK-PLA2-II, substrate phosphatidylcholine, sn-2 fatty acid C18:2, 25°C
220.5
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isoenzyme NK-PLA2-I, substrate phosphatidylcholine, sn-2 fatty acid C16:0, 25°C
229.9
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isoenzyme NK-PLA2-II, substrate phosphatidylcholine, sn-2 fatty acid C18:1, 25°C
243.1
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isoenzyme NK-PLA2-I, substrate phosphatidylcholine, sn-2 fatty acid C18:0, 25°C
69.2
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isoenzyme NK-PLA2-II, substrate phosphatidylethanolamine, sn-2 fatty acid C18:1, 25°C
76.3
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isoenzyme NK-PLA2-II, substrate phosphatidylethanolamine, sn-2 fatty acid C18:2, 25°C
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isoenzyme NK-PLA2-I, substrate phosphatidylethanolamine, sn-2 fatty acid C18:2, 25°C
89.3
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isoenzyme NK-PLA2-I, substrate phosphatidylcholine, sn-2 fatty acid C20:4, 25°C
96.3
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isoenzyme NK-PLA2-II, substrate phosphatidylserine, sn-2 fatty acid C18:1, 25°C
61
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isoenzyme NK-PLA2-I, substrate phosphatidylethanolamine, sn-2 fatty acid C18:1, 25°C
61
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isoenzyme NK-PLA2-II, substrate phosphatidylcholine, sn-2 fatty acid C20:4, 25°C
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SwissProt
brenda
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brenda
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brenda
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physiological function
does not impair the adhesion of PC12 cells to plates. Is at least 2 orders of magnitude more cytotoxic than thrombin inhibitor from Naja haje
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PA2A1_NAJKA
146
0
16271
Swiss-Prot
Secretory Pathway (Reliability: 2 )
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13346
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1 * 13100, SDS-PAGE, 1 * 13346, MALDI-MS
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monomer
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1 * 13100, SDS-PAGE, 1 * 13346, MALDI-MS
additional information
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N-terminal amino acid sequence is identical for both isoenzymes NK-PLA2-I and NK-PLA2-II
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100
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45 min, isoenzyme NK-PLA2-I, 50% residual activity, isoenzyme NK-PLA2-II, 43% residual activity
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Doley, R.; King, G.F.; Mukherjee, A.K.
Differential hydrolysis of erythrocyte and mitochondrial membrane phospholipids by two phospholipase A2 isoenzymes (NK-PLA2-I and NK-PLA2-II) from the venom of the Indian monocled cobra Naja kaouthia
Arch. Biochem. Biophys.
425
1-13
2004
Naja kaouthia
brenda
Osipov, A.V.; Filkin, S.Y.; Makarova, Y.V.; Tsetlin, V.I.; Utkin, Y.N.
A new type of thrombin inhibitor, noncytotoxic phospholipase A2, from the Naja haje cobra venom
Toxicon
55
186-194
2010
Naja haje, Naja kaouthia (P00596)
brenda