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Information on EC 3.1.1.4 - phospholipase A2 and Organism(s) Daboia russelii and UniProt Accession P59071
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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+.
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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: Daboia russelii
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
-
-
-
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Agkistrotoxin
-
-
-
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amdI1
-
-
-
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Ammodytin I2
-
-
-
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APLA
-
-
-
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APP-D-49
-
-
-
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ASPLA1
-
-
-
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ASPLA10
-
-
-
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ASPLA11
-
-
-
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ASPLA12
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-
-
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ASPLA13
-
-
-
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ASPLA14
-
-
-
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ASPLA15
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-
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ASPLA16
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-
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ASPLA17
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-
-
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ASPLA2
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-
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ASPLA3
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-
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ASPLA4
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-
-
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ASPLA5
-
-
-
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ASPLA6
-
-
-
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ASPLA7
-
-
-
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ASPLA8
-
-
-
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ASPLA9
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-
-
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ATX
-
-
-
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Basic protein I/II
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-
-
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BJ-PLA2
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-
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BJUPLA2
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-
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BPI/BPII
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-
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CaI-PLA2
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-
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Caudoxin
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-
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cPm09
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-
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Enhancing factor
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-
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GIIC sPLA2
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-
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GIID sPLA2
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-
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GIIE sPLA2
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-
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GIIF sPLA2
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-
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GIII sPLA2
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-
-
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Group IB phospholipase A2
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-
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Group IIA phospholipase A2
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-
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Group V phospholipase A2
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-
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Group VI phospholipase A2
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-
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GVI PLA2
-
-
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GX sPLA2
-
-
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GXII sPLA2
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-
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GXIII sPLA2
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-
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iPLA2
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-
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lecithinase A
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-
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MP-III 4R
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-
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Muscarinic inhibitor
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-
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Myotoxin
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-
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NAJPLA-2A
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-
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NAJPLA-2B
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-
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NAJPLA-2C
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-
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Nigexine
-
-
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Non-pancreatic secretory phospholipase A2
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-
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Notechis 11'2
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-
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Notexin
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-
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NPLA
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-
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NPS-PLA2
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-
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OHV A-PLA2
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-
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OHV-APLA2
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-
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pgPLA 1a/pgPLA 2a
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-
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phosphatidase
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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 A
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Phospholipase A2 inhibitor
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pkP5
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PLA2-10
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PLA2-VI
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PLA2-VII
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PLA2IID
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platelet activating factor acetyl hydrolase
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Pt-PLA1
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Pt-PLA2
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Secretory-type PLA, stroma-associated homolog
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sPLA(2)-IID
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sPLA(2)-IIE
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sPLA(2)-IIF
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TMV-K49
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-
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Toxin VI
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Toxin VI:5
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-
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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
phosphatidylcholine + H2O
?
-
the enzyme shows preferential hydrolysis of phosphatidylcholine
-
-
?
additional information
?
-
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determination of the cytolytic activity od sPLA2 using oleate-labelled, autoclaved Escherichia coli cells as substrate, overview
-
-
?
additional information
?
-
-
acidic PLA2 non-inhibits the factor Xa in a non-enzymatic mechanism
-
-
?
additional information
?
-
-
the enzyme does not show any proteolytic, ATPase and AchEase activity at a dose of 750 mM
-
-
?
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
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-[4'-(hydroxyimino-p-tolyl-methyl)-phenyl]-4-phenyl-sydnone
-
in vivo edema inducing activity, overview
3-[4'-(hydroxyimino-p-tolyl-methyl)-phenyl]-sydnone
-
in vivo edema inducing activity, overview
3-[4'-(hydroxyimino-phenyl-methyl)-phenyl]-4-phenyl-sydnone
-
in vivo edema inducing activity, overview
3-[4'-(hydroxyimino-phenyl-methyl)-phenyl]-sydnone
-
in vivo edema inducing activity, overview
3-[4-[hydroxyimino-(4'-n-butyl-phenyl)-methyl]-phenyl]-4-phenyl-sydnone
-
in vivo edema inducing activity, overview
3-[4-[hydroxyimino-(4'-n-butyl-phenyl)-methyl]-phenyl]-sydnone
-
in vivo edema inducing activity, overview
3-[4-[hydroxyimino-(4'-n-propyl-phenyl)-methyl]-phenyl]-4-phenylsydnone
-
in vivo edema inducing activity, overview
3-[4-[hydroxyimino-(4'-n-propyl-phenyl)-methyl]-phenyl]-sydnone
-
in vivo edema inducing activity, overview
acalyphin
from Acalypha indica, shows interaction with the amino acids (Asp-49, Lys-69 and Gly-30) at the active site of PLA2
AIPLAI
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PLA2 inhibitor isolated from the methanol extract of Azadirachta indica
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aplysulphurin A
from Aplysilla sp., shows interaction with the amino acids at the active site of PLA2
chlorogenic acid
from Achillea millefolium, shows interaction with the amino acids (Asp-49, Lys-69, Trp-31 and Trp-A31) at the active site of PLA2
curcumin
from Curcuma longa, shows interaction with the amino acids (Asp-49 and Gly-30) at the active site of PLA2
gracilin A
from Aplysilla sp., shows interaction with the amino acids (Asp-49, His-48, Trp-31 and Gly-30) at the active site of PLA2
p-bromophenacyl bromide
-
inhibits both the catalytic and anticoagulant activities. Inhibition of catalytic activity is approximately 6fold higher compared with inhibition of anticoagulant activity
stigmasterol
from Achillea millefolium, shows interaction with the amino acids (His-48) at the active site of PLA2
tectoridin
from Belamcanda chinensis, shows interaction with the amino acids (Asp-49 and Lys-69) at the active site of PLA2
4-bromophenacyl bromide
alkylation with 4-bromophenacyl bromide leads to the complete loss of its enzymatic activity signifying the crucial role of histidine residue in catalysis
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
crude enzyme has a specific activity of 0.00012 units/mg, after 7fold purification the enzyme has a specific activity of 0.00084 units/mg, at pH 8.0 and 37°C, one unit of activity is defined as the amount of protein which produces a decrease in 0.01 absorbance in 10 min at 740 nm
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE 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
-
the enzyme inhibits the blood coagulation cascade non-enzymatically by binding with coagulation factor Xa, even in the absence of phospholipids and Ca2+ and thus slows down the blood coagulation by partially inhibiting the prothrombin activation
physiological function
-
enzyme shows strong anticoagulant effect via thrombin inhibition with a Ki value of 380 nM as well as by binding to pro-coagulant phospholipids of plasma. In ex-vivo conditionsthe enzyme at 1.0 microM is non-hemolytic and non-cytotoxic to mammalian cells. It does not inhibit the collagen-induced aggregation of platelets. At a dose of 5 mg/kg, the enzyme is not lethal to mice after 48 h of injection
physiological function
the crude venom of Daboia r. russelii has prominent cytotoxic effect on HEK-293 and MCF-7 cells in a dose dependent manner. Phospholipase A2 enzyme from Indian viper (Daboia russelii russelii) venom targets both factor X and factor Xa for its anticoagulant activity
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). PA2B8_DABRR
121
0
13611
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, five cycles of freezing-thawing do not affect the catalytic or anticoagulant activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
reverse phase C18-mu-Nova pack column chromatography, CM Sephadex C-50 gel filtration and DEAE Sephadex A-50 gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
isozymes DrK-aI, DrK-aII, DrK-bI, and DrK-bII, DNA and amino acid sequence determination and analysis, phylogenetic analysis
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
herbal compounds (acalyphin, chlorogenic acid, stigmasterol, curcumin and tectoridin) and marine compounds (gracilin A and aplysulphurin A) show favorable interactions with the amino acid residues at the active site of PLA2, thereby substantiating their proven efficacy as anti-inflammatory compounds and antidotes
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tsai, I.; Tsai, H.; Wang, Y.; Tun-P, T.; Warrell, D.A.
Venom phospholipases of Russells vipers from Myanmar and eastern India-Cloning, characterization and phylogeographic analysis
Biochim. Biophys. Acta
1774
1020-1028
2007
Daboia russelii, Daboia siamensis
Kamble, R.R.; Belgur, S.S.; Aladkatti, R.; Khazi, I.A.
Synthesis and evaluation of benzophenone oximes derivatized with sydnone as inhibitors of secretory phospholipase A2 with anti-inflammatory activity
Chem. Pharm. Bull.
57
16-21
2009
Naja naja, Daboia russelii, Trimeresurus malabaricus
Nirmal, N.; Praba, G.O.; Velmurugan, D.
Modeling studies on phospholipase A2-inhibitor complexes
Indian J. Biochem. Biophys.
45
256-262
2008
Bos taurus (P00593), Bos taurus, Daboia russelii (P59071), Daboia russelii
Saikia, D.; Thakur, R.; Mukherjee, A.
An acidic phospholipase A2 (RVVA-PLA2-I) purified from Daboia russelli venom exerts its anticoagulant activity by enzymatic hydrolysis of plasma phospholipids and by non-enzymatic inhibition of factor Xa in a phospholipids/Ca2+ independent manner
Toxicon
57
841-850
2011
Daboia russelii
Mukherjee, A.K.
A major phospholipase A2 from Daboia russelii russelii venom shows potent anticoagulant action via thrombin inhibition and binding with plasma phospholipids
Biochimie
99
153-161
2014
Daboia russelii
Sharma, M.; Iyer, J.K.; Shih, N.; Majumder, M.; Mattaparthi, V.S.; Mukhopadhyay, R.; Doley, R.
Daboxin P, a major phospholipase A2 enzyme from the Indian Daboia russelii russelii venom targets factor X and factor Xa for its anticoagulant activity
PLoS ONE
11
e0153770
2016
Daboia russelii (C0HK16)
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
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Release 2023.1 (January 2023)
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