Any feedback?
Information on EC 3.1.1.4 - phospholipase A2 and Organism(s) Naja atra and UniProt Accession P00598
for references in articles please use BRENDA:EC3.1.1.4Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
3.1.1.4 phospholipase A2IUBMB Comments
Also acts on phosphatidylethanolamine, choline plasmalogen and phosphatides, removing the fatty acid attached to the 2-position. Requires Ca2+.
Specify your search results
Word Map
- 3.1.1.4
-
arachidonic
- phospholipid
- prostaglandin
-
cyclooxygenase
-
eicosanoids
-
leukotriene
- necrosis
- indomethacin
- agonist
- lysophosphatidylcholine
- endothelial
- neutrophil
- bromide
- phosphatidylethanolamine
- crotalus
- lipoxygenase
- cox-2
-
phorbol
-
ionophore
- pkc
- inositol
- artery
-
neurotoxic
- quinacrine
-
thromboxane
- peroxiredoxins
-
platelet-activating
- diacylglycerols
- nephropathy
- lysophospholipids
-
bilayer
- phosphatidylinositol
-
prelabeled
- edema
-
prostanoids
- phosphatidylserine
- pertussis
-
interfacial
-
phosphatidic
-
envenom
- glycerophospholipids
-
nordihydroguaiaretic
-
presynaptic
- synovial
- prostacyclin
- viper
-
micelle
- pharmacology
- analysis
- food industry
- biotechnology
-
lipoprotein-associated
- ndga
- industry
- drug development
- zymosan
- medicine
- synthesis
The taxonomic range for the selected organisms is: Naja atra
The enzyme appears in selected viruses and cellular organisms
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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
-
-
-
-
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
LITERATURE
hydrolysis of carboxylic ester
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -
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
9001-84-7
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,2-dipalmitoyl-phosphatidylcholine + H2O
1-palmitoyl-glycerophosphorylcholine + palmitic acid
-
-
-
?
additional information
?
-
native and mutated PLA2s induce apoptotic death of U937 cells
-
-
?
additional information
?
-
-
native and mutated PLA2s induce apoptotic death of U937 cells
-
-
?
additional information
?
-
-
the enzyme in venom effectively inhibits A-type K+ currents in mice and cause alterations of channel gating characters, such as the shifts of steadystate activation and inactivation curves to hyperpolarization direction and changes of V1/2 and slope factor, the effects are independent of the enzymatic activity as phospholipase, overview
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
native and mutated PLA2s induce apoptotic death of U937 cells
-
-
?
additional information
?
-
-
native and mutated PLA2s induce apoptotic death of U937 cells
-
-
?
additional information
?
-
-
the enzyme in venom effectively inhibits A-type K+ currents in mice and cause alterations of channel gating characters, such as the shifts of steadystate activation and inactivation curves to hyperpolarization direction and changes of V1/2 and slope factor, the effects are independent of the enzymatic activity as phospholipase, overview
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
-
induces apoptotic death of human leukemia K562 cells in a concentration- and time-dependent manner. Degradation of procaspases, production of tBid, loss of mitochondrial membrane potential, Bcl-2 degradation, mitochondrial translocation of Bax, and cytochrome c release in PLA2-treated cells. PLA2 treatment increases Fas and FasL protein expression and activates p38 MAPK (mitogen-activated protein kinase) and JNK (c-Jun NH2-terminal kinase) in K562 cells. SB202190 pretreatment promotes the cytotoxic effect of PLA2 toward K562 cells in a time-dependent manner. SP600125 (JNK inhibitor) abolishes the cytotoxic effect of PLA2 and PLA2-induced autocrine Fas death pathway
physiological function
-
PLA2 induces caspase-dependent death in human SK-N-SH cells. PLA2 treatment induces Fas and FasL protein expression, leads to activation of p38 MAPK, inactivation of ERK, reactive oxygen species generation and elevation in intracellular Ca2+ concentration. PLA2-induced cell death is, in part, elicited by upregulation of Fas and FasL, which is regulated by Ca2+- and reactive oxygen species-evoked p38 MAPK activation, and suggests that non-catalytic PLA2 plays a role for the signaling pathway
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PA2A1_NAJAT
146
0
16013
Swiss-Prot
Secretory Pathway (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
analysis of the secondary structure of wild-type and N-terminal mutant enzymes, the structures are dominated by alpha-helical structure, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
N1M
site-directed mutagenesis, the mutants with an extra Met before Asn1 or substituting Asn1 with Met still retain approximately 40.9% and 82.9% membrane-damaging activity of the native enzyme, respectively. Mutations on the N-terminal region do not greatly affect the Ca2+-binding ability but cause a precipitous drop in PLA2 activity. The gross conformation of the mutant is altered compared to the native enzyme, overview. The enzymatic activity of the mutant is approximately 5.3% of that of native PLA2
additional information
additional information
removal of N-terminal heptapeptide causes a complete loss of membrane-damaging activity, whilst the mutants with an extra Met before Asn1 or substituting Asn1 with Met still retain approximately 40.9% and 82.9% membrane-damaging activity of the native enzyme, respectively. Mutations on the N-terminal region do not greatly affect the Ca2+-binding ability but cause a precipitous drop in PLA2 activity. The gross conformation of the mutants is altered compared to the native enzyme, overview. The enzymatic activity of mutants M-PLA2, PLA2(N1M) and PLA2(DELTAN7) are approximately 3.6%, 5.3% and 0.6% of that of native PLA2
additional information
-
removal of N-terminal heptapeptide causes a complete loss of membrane-damaging activity, whilst the mutants with an extra Met before Asn1 or substituting Asn1 with Met still retain approximately 40.9% and 82.9% membrane-damaging activity of the native enzyme, respectively. Mutations on the N-terminal region do not greatly affect the Ca2+-binding ability but cause a precipitous drop in PLA2 activity. The gross conformation of the mutants is altered compared to the native enzyme, overview. The enzymatic activity of mutants M-PLA2, PLA2(N1M) and PLA2(DELTAN7) are approximately 3.6%, 5.3% and 0.6% of that of native PLA2
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
native PLA2 is labeled with NTSB and then refolded according to the same procedure for refolding of mutated PLA2. The refolded PLA2 exhibited enzymatic activity and electrophoretic mobility indistinguishable from those of native PLA2
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Pan, F.M.; Chao, S.C.; Wu, S.H.; Chang, W.C.; Chiou, S.H.
Characterization of phospholipase A2 (PLA2) from Taiwan Cobra: Isoenzymes and their site-directed mutants
Biochem. Biophys. Res. Commun.
250
154-160
1998
Naja atra
Hu, P.; Sun, L.; Zhu, Z.Q.; Hou, X.W.; Wang, S.; Yu, S.S.; Wang, H.L.; Zhang, P.; Wang, M.; Niu, L.W.; Teng, M.K.; Ruan, D.Y.
Crystal structure of Natratoxin, a novel snake secreted phospholipaseA2 neurotoxin from Naja atra venom inhibiting A-type K+ currents
Proteins
72
673-683
2008
Naja atra
Chiou, Y.; Cheng, Y.; Kao, P.; Wang, J.; Chang, L.
Mutations on the N-terminal region abolish differentially the enzymatic activity, membrane-damaging activity and cytotoxicity of Taiwan cobra phospholipase A2
Toxicon
51
270-279
2008
Naja atra (P00598), Naja atra
Chen, K.C.; Kao, P.H.; Lin, S.R.; Chang, L.S.
Upregulation of Fas and FasL in Taiwan cobra phospholipase A2-treated human neuroblastoma SK-N-SH cells through ROS- and Ca2+-mediated p38 MAPK activation
J. Cell. Biochem.
106
93-102
2009
Naja atra
EXTERNAL LINKS (specific for EC-Number 3.1.1.4)
Transporter Classification Database (TCDB): 1.N.2.1.6, 1.B.84.1.6, 1.B.84.1.5, 1.B.84.1.3, 1.B.84.1.1, 1.B.84.1.4, 1.B.84.1.2
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
