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Information on EC 3.1.1.4 - phospholipase A2 and Organism(s) Apis mellifera and UniProt Accession P00630
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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: Apis mellifera
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
(2'R,2S)-2,3-dihydroxypropyl 2'-octadecanoyloxy-5'-hexadecyloxy-5'-oxopentan-1'-yl phosphate + H2O
?
-
-
-
?
(2S,2'S,3R)-2,3-dihydroxypropyl 2',3'-octadecanoyloxy-nonadecyl phosphate + H2O
?
-
-
-
?
(2S,2'S,3S)-2,3-dihydroxypropyl 2',3'-octadecanoyloxy-nonadecyl phosphate + H2O
?
-
-
-
?
(R)-1-O-hexadecyl-2-palmitoyl-sn-glycero-3-phoshocholine + H2O
?
-
-
-
?
1,2-bis-(10-pyrenedecanoyl)-sn-glycero-3-phosphocholine + H2O
1-(10-pyrenedecanoyl)-glycero-3-phosphocholine + 10-pyrenedecanoate
-
-
-
?
1,2-dipalmitoyl-sn-glycero-3-phosphocholine + H2O
1-palmitoyl-sn-glycero-3-phosphorylcholine + palmitate
-
-
-
?
1,2-dipalmitoyl-sn-glycero-3-phosphoglycerol + H2O
1-palmitoyl-sn-glycero-3-phosphorylglycerol + palmitate
-
-
-
?
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine + H2O
1-palmitoyl-sn-glycero-3-phosphocholine + oleate
-
-
-
?
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoglycerol + H2O
1-palmitoyl-sn-glycero-3-phosphorylglycerol + oleate
-
-
-
?
1-palmitoyl-2-stearoyl-dibromo-sn-glycero-3-phosphocholine + H2O
?
-
-
-
?
1,2-diacyl-sn-glycero-3-phosphatide + H2O
1-acyl-sn-glycero-3-phosphatide + fatty acid
-
-
-
?
1,2-dihexanoyl-sn-glycero-3-phosphocholine + H2O
1-hexanoyl-sn-glycero-3-phosphocholine + hexanoate
-
-
-
?
1,2-dilauroyl-sn-glycero-3-phosphocholine + H2O
1-lauroyl-sn-glycero-3-phosphocholine + laureate
-
-
-
?
1,2-dimyristol-sn-glycero-phosphomethanol lithium salt + H2O
myristic acid + 1-myristoyl-sn-glycerophosphomethanol
-
-
-
?
1,2-dimyristoyl-sn-phosphatidylcholine + H2O
1-myristoyl-phosphorylcholine + myristic acid
-
-
-
?
1,2-dipalmitoyl-phosphatidylcholine + H2O
1-palmitoyl-glycerophosphorylcholine + palmitic acid
-
-
-
?
1-oleoyl-2-isolauroyl phosphatidylethanolamine + H2O
1-oleoyl phosphatidylethanolamine + isolauric acid
-
-
-
?
DBPA + H2O
?
-
fluorogenic Dabcyl- and BODIPY-containing phospholipd-analogue
-
-
?
DBPC + H2O
?
-
fluorogenic Dabcyl- and BODIPY-containing phospholipd-analogue
-
-
?
DBPE + H2O
?
-
fluorogenic Dabcyl- and BODIPY-containing phospholipd-analogue
-
-
?
DBPG + H2O
?
-
fluorogenic Dabcyl- and BODIPY-containing phospholipd-analogue
-
-
?
phosphatidylcholine + H2O
1-acylglycerophosphocholine + fatty acid
-
-
-
?
additional information
?
-
-
preference of substrates in decreasing order: phosphatidylcholines, phosphatidylglycerols, phosphatidylethanolamines, phosphatidic acids
-
-
?
additional information
?
-
-
the phospholipase A2 superfamily consists of many different groups of enzymes that catalyze the hydrolysis of the sn-2 ester bond in a variety of different phospholipids, products of the hydrolysis of the sn-2 ester bond of phospholipid are a free fatty acid and lysophospholipid
-
-
?
additional information
?
-
-
PLA2 shows low enzymatic activity toward positively charged vesicles due to a long lag period. PLA2 demonstrates a high degree of enzymatic activity toward negatively charged 1,2-dioleoyl-sn-glycero-3-phosphatidylcholine and 1,2-dioleoyl-sn-glycero-3-phosphatidylcholine/1,2-dioleoyl-sn-glycero-3-phosphatidylserine vesicles. Vesicle size distribution of zwitterionic 1,2-dioleoyl-sn-glycero-3-phosphatidylcholine changes faster than that of 1,2-dioleoyl-sn-glycero-3-phosphatidylcholine/1,2-dioleoyl-sn-glycero-3-phosphatidylserine 90:10
-
-
?
additional information
?
-
-
similar activity to phospholipids with different fatty acids in the sn-2 position, but with different preferences for the charge on the lipid surface
-
-
?
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
?
-
-
the phospholipase A2 superfamily consists of many different groups of enzymes that catalyze the hydrolysis of the sn-2 ester bond in a variety of different phospholipids, products of the hydrolysis of the sn-2 ester bond of phospholipid are a free fatty acid and lysophospholipid
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Ca2+
-
free Ca2+ is required for interaction between PLA2 and vesicles under catalytic conditions, Ca2+ addition for activation of PLA2 under initially noncatalytic conditions. Differences between enzymatic activity under initially catalytic and noncatalytic conditions, membrane binding under noncatalytic conditions must either cause PLA2 to adopt a less favorable conformation for enzymatic activity or prevent a Ca2+ ion (after Ca2+ addition) from entering the active site pocket
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
7-hydroxy-2-oxo-N-[(4Z,7Z,10Z,13Z)-19,19,19-trifluoro-18-oxononadeca-4,7,10,13-tetraen-1-yl]-2H-chromene-3-carboxamide
-
AnMIP
a PLA2 inhibitor isolated from Atropoides nummifer plasma, inhibitor protein DNA and amino acid sequence determination and phylogenetic analysis, 22247-22301 Da, pI 4.1-4.7, trimeric structure, inhibitory profile, overview
-
1-hexadecyl-3-trifluoroethylglycero-sn-2-phosphomethanol
-
MJ33, competitive inhibitor
manoalogue
-
synthetic analogue of the sea sponge-derived manoalide, time dependent irreversible loss of activity: modification of lysine residues
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0165
(6Z,9Z,12Z,15Z)-1,1,1-trifluorohenicosa-6,9,12,15-tetraen-2-one
Apis mellifera
pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
synthesis of fluorogenic substrate analogues for rapid determination of head group modification on cell signaling
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8
-
substrate: 1,2-dihexanoyl-sn-glycero-3-phosphocholine, in 75% propanol and 25% water
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
-
adsorption of PLA2 to model membranes is not primarily driven by electrostatic interactions. Subsequent lipid desorption, which is linked to the bilayer-disrupting activity of PLA2, is significantly affected by membrane electrostatics. Specifically, a nonhydrolytic bilayer-disrupting activity of PLA2 targets anionic membranes, triggering a change in bilayer topology
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). PA2_APIME
167
0
19058
Swiss-Prot
Secretory Pathway (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
-
dimerization occurs in concentrated aqueous solution, no data concerning MW
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with L-1-O-octyl-2-heptylphosphonyl-sn-glycero-3-phosphoethanolamine
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
bee venom-derived phospholipase A2 can be a promising treatment option for Parkinson's disease. It ameliorates motor dysfunction and modulates microglia activation in Parkinson's disease alpha-synuclein transgenic mice
pharmacology
bee venom-derived phospholipase A2 can be a promising treatment option for Parkinson's disease. It ameliorates motor dysfunction and modulates microglia activation in Parkinson's disease alpha-synuclein transgenic mice
drug development
-
new pharmaceutical approaches against PLA2 activity can be designed to prevent either membrane adsorption or nonhydrolytic bilayer-disrupting activity, both of which are necessary for enzymatic activity, opening up a new set of specific functional targets for inhibitor design
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ghomashchi, F.; Yu, B.Z.; Mihelich, E.D.; Jain, M.K.; Gelb, M.H.
Kinetic characterization of phospholipase A2 modified by manoalogue
Biochemistry
30
9559-9569
1991
Apis mellifera, Naja naja, Sus scrofa
Cottrell, R.C.
Phospholipase A2 from bee venom
Methods Enzymol.
71
698-702
1981
Apis mellifera
Valentin, E.; Lambeau, G.
What can venom phospholipases A2 tell us about the functional diversity of mammalian secreted phospholipases A2?
Biochimie
82
815-831
2000
Crotalus atrox, Mammalia, Exaiptasia diaphana, Pandinus imperator, Pseudonaja textilis, Apis mellifera (P00630)
Rose, T.M.; Prestwich, G.D.
Fluorogenic phospholipids as head group-selective reporters of phospholipase A activity
ACS Chem. Biol.
1
83-92
2006
Streptomyces violaceoruber, Apis mellifera, Bos taurus, Homo sapiens, Naja mossambica
Pande, A.H.; Qin, S.; Nemec, K.N.; He, X.; Tatulian, S.A.
Isoform-specific membrane insertion of secretory phospholipase A2 and functional implications
Biochemistry
45
12436-12447
2006
Apis mellifera (P00630), Apis mellifera, Homo sapiens (P14555), Homo sapiens
Quiros, S.; Alape-Giron, A.; Angulo, Y.; Lomonte, B.
Isolation, characterization and molecular cloning of AnMIP, a new alpha-type phospholipase A2 myotoxin inhibitor from the plasma of the snake Atropoides nummifer (Viperidae: Crotalinae)
Comp. Biochem. Physiol. B
146
60-68
2007
Bothrops asper, Oxyuranus scutellatus, Apis mellifera (P00630)
Burke, J.E.; Dennis, E.A.
Phospholipase A2 biochemistry
Cardiovasc. Drugs Ther.
23
49-59
2009
Apis mellifera, Bitis gabonica, Bos taurus, Crotalus sp., Homo sapiens, Mus musculus, Naja naja, Oryza sativa, Rattus norvegicus, Sus scrofa, Protoparvovirus
Burke, J.; Dennis, E.
Phospholipase A2 structure/function, mechanism, and signaling
J. Lipid Res.
50 Suppl
S237-S242
2009
Apis mellifera, Homo sapiens, Mus musculus, Naja naja
Jackman, J.A.; Cho, N.J.; Duran, R.S.; Frank, C.W.
Interfacial binding dynamics of bee venom phospholipase A2 investigated by dynamic light scattering and quartz crystal microbalance
Langmuir
26
4103-4112
2010
Apis mellifera
Madsen, J.J.; Linderoth, L.; Subramanian, A.K.; Andresen, T.L.; Peters, G.H.
Secretory phospholipase A2 activity toward diverse substrates
J. Phys. Chem. B
115
6853-6861
2011
Agkistrodon piscivorus piscivorus, Apis mellifera (P00630), Homo sapiens (P14555)
Ng, C.Y.; Kwok, T.X.; Tan, F.C.; Low, C.M.; Lam, Y.
Fluorogenic probes to monitor cytosolic phospholipase A2 activity
Chem. Commun. (Camb.)
53
1813-1816
2017
Apis mellifera (P00630)
Ye, M.; Chung, H.S.; Lee, C.; Hyun Song, J.; Shim, I.; Kim, Y.S.; Bae, H.
Bee venom phospholipase A2 ameliorates motor dysfunction and modulates microglia activation in Parkinsons disease alpha-synuclein transgenic mice
Exp. Mol. Med.
48
e244
2016
Apis mellifera (P00630), Apis mellifera
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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