Information on EC 3.1.1.4 - phospholipase A2 and Organism(s) Daboia russelii and UniProt Accession P59071

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This record set is specific for:
Daboia russelii
UNIPROT: P59071


The taxonomic range for the selected organisms is: Daboia russelii

The enzyme appears in selected viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.1.1.4
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RECOMMENDED NAME
GeneOntology No.
phospholipase A2
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of carboxylic ester
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
aspirin triggered resolvin D biosynthesis
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aspirin triggered resolvin E biosynthesis
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phosphatidylcholine acyl editing
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phospholipases
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phospholipid remodeling (phosphatidate, yeast)
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phospholipid remodeling (phosphatidylcholine, yeast)
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phospholipid remodeling (phosphatidylethanolamine, yeast)
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plasmalogen degradation
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resolvin D biosynthesis
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lipid metabolism
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Glycerophospholipid metabolism
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Ether lipid metabolism
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Arachidonic acid metabolism
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Linoleic acid metabolism
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alpha-Linolenic acid metabolism
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Metabolic pathways
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Biosynthesis of secondary metabolites
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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
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Russell's viper
Uniprot
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-nitro-3-(octanoyloxy) benzoic acid + H2O
?
show the reaction diagram
-
-
-
-
?
phosphatidylcholine + H2
1-acylglycerophosphocholine + fatty acid
show the reaction diagram
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-
-
-
?
phosphatidylcholine + H2O
?
show the reaction diagram
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the enzyme shows preferential hydrolysis of phosphatidylcholine
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-
?
phospholipids + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
phospholipids + H2O
?
show the reaction diagram
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-
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
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activates
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-[4'-(hydroxyimino-p-tolyl-methyl)-phenyl]-4-phenyl-sydnone
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in vivo edema inducing activity, overview
3-[4'-(hydroxyimino-p-tolyl-methyl)-phenyl]-sydnone
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in vivo edema inducing activity, overview
3-[4'-(hydroxyimino-phenyl-methyl)-phenyl]-4-phenyl-sydnone
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in vivo edema inducing activity, overview
3-[4'-(hydroxyimino-phenyl-methyl)-phenyl]-sydnone
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in vivo edema inducing activity, overview
3-[4-[hydroxyimino-(4'-n-butyl-phenyl)-methyl]-phenyl]-4-phenyl-sydnone
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in vivo edema inducing activity, overview
3-[4-[hydroxyimino-(4'-n-butyl-phenyl)-methyl]-phenyl]-sydnone
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in vivo edema inducing activity, overview
3-[4-[hydroxyimino-(4'-n-propyl-phenyl)-methyl]-phenyl]-4-phenylsydnone
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in vivo edema inducing activity, overview
3-[4-[hydroxyimino-(4'-n-propyl-phenyl)-methyl]-phenyl]-sydnone
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in vivo edema inducing activity, overview
4-bromophenacyl bromide
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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
dithiothreitol
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factor Xa
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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
iodoacetamide
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luffariellin B
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N-alpha-p-tosyl-L-lysine chloromethyl ketone
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N-tosyl-L-phenylalanyl chloromethyl ketone
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p-bromophenacyl bromide
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inhibits both the catalytic and anticoagulant activities. Inhibition of catalytic activity is approximately 6fold higher compared with inhibition of anticoagulant activity
phenylmethylsulfonyl fluoride
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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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.61 - 0.65
phosphatidylcholine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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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 37C, 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 hide
LITERATURE
7.5
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indirect hemolytic assay at
8
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enzymatic assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8 - 8.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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assay at
37 - 45
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
13840
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MALDI-TOF mass spectrometry
14000
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PAGE
28500
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2 * 28500, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
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2 * 28500, SDS-PAGE
monomer
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1* 13835, MALDI-TOF mass spectrometry, 1 * 14000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, five cycles of freezing-thawing do not affect the catalytic or anticoagulant activity
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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
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
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