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Information on EC 3.1.1.4 - phospholipase A2 and Organism(s) Naja kaouthia and UniProt Accession P00596

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.1 Carboxylic-ester hydrolases
                3.1.1.4 phospholipase A2
IUBMB Comments
Also acts on phosphatidylethanolamine, choline plasmalogen and phosphatides, removing the fatty acid attached to the 2-position. Requires Ca2+.
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This record set is specific for:
Naja kaouthia
UNIPROT: P00596
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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, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospholipase A2
-
14 kDa phospholipase A2
-
-
-
-
Agkistrotoxin
-
-
-
-
amdI1
-
-
-
-
Ammodytin I2
-
-
-
-
APLA
-
-
-
-
APP-D-49
-
-
-
-
ASPLA1
-
-
-
-
ASPLA10
-
-
-
-
ASPLA11
-
-
-
-
ASPLA12
-
-
-
-
ASPLA13
-
-
-
-
ASPLA14
-
-
-
-
ASPLA15
-
-
-
-
ASPLA16
-
-
-
-
ASPLA17
-
-
-
-
ASPLA2
-
-
-
-
ASPLA3
-
-
-
-
ASPLA4
-
-
-
-
ASPLA5
-
-
-
-
ASPLA6
-
-
-
-
ASPLA7
-
-
-
-
ASPLA8
-
-
-
-
ASPLA9
-
-
-
-
ATX
-
-
-
-
Basic protein I/II
-
-
-
-
BJ-PLA2
-
-
-
-
BJUPLA2
-
-
-
-
BPI/BPII
-
-
-
-
CaI-PLA2
-
-
-
-
Caudoxin
-
-
-
-
cPm09
-
-
-
-
Enhancing factor
-
-
-
-
GIIC sPLA2
-
-
-
-
GIID sPLA2
-
-
-
-
GIIE sPLA2
-
-
-
-
GIIF sPLA2
-
-
-
-
GIII sPLA2
-
-
-
-
Group IB phospholipase A2
-
-
-
-
Group IIA phospholipase A2
-
-
-
-
Group V phospholipase A2
-
-
-
-
Group VI phospholipase A2
-
-
-
-
GVI PLA2
-
-
-
-
GX sPLA2
-
-
-
-
GXII sPLA2
-
-
-
-
GXIII sPLA2
-
-
-
-
iPLA2
-
-
-
-
lecithinase A
-
-
-
-
MP-III 4R
-
-
-
-
Muscarinic inhibitor
-
-
-
-
Myotoxin
-
-
-
-
NAJPLA-2A
-
-
-
-
NAJPLA-2B
-
-
-
-
NAJPLA-2C
-
-
-
-
Nigexine
-
-
-
-
NK-PLA2-I
-
-
NK-PLA2-II
-
-
Non-pancreatic secretory phospholipase A2
-
-
-
-
Notechis 11'2
-
-
-
-
Notexin
-
-
-
-
NPLA
-
-
-
-
NPS-PLA2
-
-
-
-
OHV A-PLA2
-
-
-
-
OHV-APLA2
-
-
-
-
pgPLA 1a/pgPLA 2a
-
-
-
-
phosphatidase
-
-
-
-
phosphatide 2-acylhydrolase
-
-
-
-
phosphatidolipase
-
-
-
-
Phosphatidylcholine 2-acylhydrolase
-
-
-
-
Phosphatidylcholine 2-acylhydrolase GIIC
-
-
-
-
Phosphatidylcholine 2-acylhydrolase GIID
-
-
-
-
Phosphatidylcholine 2-acylhydrolase GIIE
-
-
-
-
Phosphatidylcholine 2-acylhydrolase GIIF
-
-
-
-
Phosphatidylcholine 2-acylhydrolase GIII
-
-
-
-
Phosphatidylcholine 2-acylhydrolase GX
-
-
-
-
Phosphatidylcholine 2-acylhydrolase GXII
-
-
-
-
Phosphatidylcholine 2-acylhydrolase GXIII
-
-
-
-
phospholipase A
-
-
-
-
Phospholipase A2 inhibitor
-
-
-
-
pkP5
-
-
-
-
PLA2-10
-
-
-
-
PLA2-VI
-
-
-
-
PLA2-VII
-
-
-
-
PLA2IID
-
-
-
-
platelet activating factor acetyl hydrolase
-
-
-
-
Pt-PLA1
-
-
-
-
Pt-PLA2
-
-
-
-
Secretory-type PLA, stroma-associated homolog
-
-
-
-
sPLA(2)-IID
-
-
-
-
sPLA(2)-IIE
-
-
-
-
sPLA(2)-IIF
-
-
-
-
TMV-K49
-
-
-
-
Toxin VI
-
-
-
-
Toxin VI:5
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of carboxylic ester
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
phosphatidylcholine 2-acylhydrolase
Also acts on phosphatidylethanolamine, choline plasmalogen and phosphatides, removing the fatty acid attached to the 2-position. Requires Ca2+.
CAS REGISTRY NUMBER
COMMENTARY hide
9001-84-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
phosphatidylcholine + H2O
1-acylglycerophosphocholine + fatty acid
show the reaction diagram
-
preferred substrate for both isoenzymes, NK-PLA2-I and NK-PLA2-II
-
-
?
phosphatidylethanolamine + H2O
1-acylglycerophosphorylethanolamine + fatty acid
show the reaction diagram
-
-
-
-
?
phosphatidylserine + H2O
1-acylglycerophosphoserine + fatty acid
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
both isoenzymes NK-PLA2-I and NK-PLA2-II cause significantly more damage to mitochondrial membranes as compared to erythrocyte membranes
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-bromophenacyl bromide
selectively and irreversibly modifies the His48 residue in the active site
p-bromophenacylbromide
-
i.e. pBPB, 3.3 mM, 95% inhibition of isoenzyme NK-PLA2-I, 89% inhibition of isoenzyme NK-PLA2-II
additional information
-
not inhibitory to both isoenzymes: p-methylsulfonylfluoride, tosyl-L-phenylalaninchlormethylketon, N-bromosuccinamide, tosyl-L-lysinechlormethylketon
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
101.2
-
isoenzyme NK-PLA2-I, substrate phosphatidylserine, sn-2 fatty acid C18:1, 25°C
133
-
isoenzyme NK-PLA2-II, substrate phosphatidylcholine, sn-2 fatty acid C16:0, 25°C
153.9
-
isoenzyme NK-PLA2-II, substrate phosphatidylcholine, sn-2 fatty acid C18:0, 25°C
178.4
-
isoenzyme NK-PLA2-I, substrate phosphatidylcholine, sn-2 fatty acid C18:1, 25°C
202.3
-
isoenzyme NK-PLA2-I, substrate phosphatidylcholine, sn-2 fatty acid C18:2, 25°C
218.4
-
isoenzyme NK-PLA2-II, substrate phosphatidylcholine, sn-2 fatty acid C18:2, 25°C
220.5
-
isoenzyme NK-PLA2-I, substrate phosphatidylcholine, sn-2 fatty acid C16:0, 25°C
229.9
-
isoenzyme NK-PLA2-II, substrate phosphatidylcholine, sn-2 fatty acid C18:1, 25°C
243.1
-
isoenzyme NK-PLA2-I, substrate phosphatidylcholine, sn-2 fatty acid C18:0, 25°C
69.2
-
isoenzyme NK-PLA2-II, substrate phosphatidylethanolamine, sn-2 fatty acid C18:1, 25°C
76.3
-
isoenzyme NK-PLA2-II, substrate phosphatidylethanolamine, sn-2 fatty acid C18:2, 25°C
79
-
isoenzyme NK-PLA2-I, substrate phosphatidylethanolamine, sn-2 fatty acid C18:2, 25°C
89.3
-
isoenzyme NK-PLA2-I, substrate phosphatidylcholine, sn-2 fatty acid C20:4, 25°C
96.3
-
isoenzyme NK-PLA2-II, substrate phosphatidylserine, sn-2 fatty acid C18:1, 25°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PA2A1_NAJKA
146
0
16271
Swiss-Prot
Secretory Pathway (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
13100
-
PAGE
13346
-
1 * 13100, SDS-PAGE, 1 * 13346, MALDI-MS
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 13100, SDS-PAGE, 1 * 13346, MALDI-MS
additional information
-
N-terminal amino acid sequence is identical for both isoenzymes NK-PLA2-I and NK-PLA2-II
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100
-
45 min, isoenzyme NK-PLA2-I, 50% residual activity, isoenzyme NK-PLA2-II, 43% residual activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
isoenzyme NK-PLA2-II
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team