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Information on EC 3.1.1.4 - phospholipase A2 and Organism(s) Sus scrofa

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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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Select one or more organisms in this record: ?
This record set is specific for:
Sus scrofa
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Word Map
The taxonomic range for the selected organisms is: Sus scrofa
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
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
-
-
-
-
Ca2+-independent iPLA2
-
-
CaI-PLA2
-
-
-
-
Caudoxin
-
-
-
-
cPm09
-
-
-
-
cytosolic cPLA2
-
-
Enhancing factor
-
-
-
-
GIIC sPLA2
-
-
-
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GIID sPLA2
-
-
-
-
GIIE sPLA2
-
-
-
-
GIIF sPLA2
-
-
-
-
GIII sPLA2
-
-
-
-
Group IB phospholipase A2
-
-
-
-
Group IIA phospholipase A2
-
-
-
-
group IIA secretory PLA2
-
-
Group V phospholipase A2
-
-
-
-
Group VI phospholipase A2
-
-
-
-
GVI PLA2
-
-
-
-
GX sPLA2
-
-
-
-
GXII sPLA2
-
-
-
-
GXIII sPLA2
-
-
-
-
iPLA2
-
-
-
-
lecithinase A
-
-
-
-
lipoprotein-associated phospholipase A2
-
-
lipoprotein-associated PLA2
-
-
Lp-PLA2
-
-
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
-
-
-
-
PAF-AH
-
-
pancreatic phospholipase A2
-
pgPLA 1a/pgPLA 2a
-
-
-
-
phosphatidase
-
-
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-
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
Phospholipase A2 inhibitor
-
-
-
-
pkP5
-
-
-
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PLA2-10
-
-
-
-
PLA2-VI
-
-
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-
PLA2-VII
-
-
-
-
PLA2IID
-
-
-
-
platelet activating factor acetyl hydrolase
-
-
-
-
platelet-activating factor acetylhydrolase
-
-
Pt-PLA1
-
-
-
-
Pt-PLA2
-
-
-
-
secreted phospholipase A2
-
-
secreted sPLA2
-
-
secretory phospholipase A2
-
-
secretory phospholipase A2 type IB
-
Secretory-type PLA, stroma-associated homolog
-
-
-
-
sPLA(2)-IID
-
-
-
-
sPLA(2)-IIE
-
-
-
-
sPLA(2)-IIF
-
-
-
-
sPLA2
sPLA2 GIB
-
-
sPLA2 IB
-
sPLA2 type IIA
-
TMV-K49
-
-
-
-
Toxin VI
-
-
-
-
Toxin VI:5
-
-
-
-
type VIIA PLA2
-
-
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
(+/-)-3-O-(4-cyanomethylphenyl)-1,2-O-di-n-heptylglycerol + H2O
?
show the reaction diagram
-
-
-
-
?
(+/-)-3-O-(4-hydroxymethylphenyl)-1,2-O-di-n-heptylglycerol + H2O
?
show the reaction diagram
-
-
-
-
?
1,2-diacyl-sn-glycero-3-phosphatide + H2O
1-acyl-sn-glycero-3-phosphatide + fatty acid
show the reaction diagram
-
-
-
?
1,2-diacyl-sn-glycero-3-phosphatide + H2O
?
show the reaction diagram
-
-
-
-
?
1,2-diacyl-sn-glycero-3-phosphorylcholine + H2O
1-acyl-sn-glycero-3-phosphorylcholine + fatty acid
show the reaction diagram
-
-
-
?
1,2-didecanoyl-sn-glycero-3-phosphocholine + H2O
1-decanoyl-sn-glycero-3-phosphocholine + decanoate
show the reaction diagram
1,2-didodecanoyl-sn-glycero-3-phosphocholine + H2O
1-decanoyl-sn-glycero-3-phosphocholine + decanoate
show the reaction diagram
-
-
-
?
1,2-diheptanoyl-sn-glycero-3-phophorylcholine + H2O
1-heptanoyl-sn-glycero-3-phophorylcholine + heptanoate
show the reaction diagram
-
-
-
-
?
1,2-diheptanoyl-sn-glycero-3-sulfate + H2O
1-heptanoyl-sn-glycero-3-sulfate + heptanoate
show the reaction diagram
-
-
-
?
1,2-dihexadecanoyl-rac-glycero-3-phosphorac-(1-glycerol) + H2O
?
show the reaction diagram
pyrene-modified or unmodified phospholipid substrate
-
-
?
1,2-dihexanoyl-sn-glycero-3-phosphocholine + H2O
1-hexanoyl-sn-glycero-3-phosphocholine + hexanoate
show the reaction diagram
1,2-dilauroyl-sn-glycero-3-phosphocholine + H2O
1-lauroyl-sn-glycero-3-phosphocholine + laureate
show the reaction diagram
-
-
-
?
1,2-dimyristol-sn-glycero-phosphomethanol lithium salt + H2O
myristic acid + 1-myristoyl-sn-glycerophosphomethanol
show the reaction diagram
-
-
-
?
1,2-dimyristoyl-sn-phosphatidylcholine + H2O
1-myristoyl-phosphorylcholine + myristic acid
show the reaction diagram
-
-
-
?
1,2-dinonanoyl-sn-glycero-3-phosphocholine + H2O
1-nonanoyl-sn-glycero-3-phosphocholine + nonanoate
show the reaction diagram
-
-
-
?
1,2-dioctanoyl-sn-glycero-3-phosphocholine + H2O
1-octanoyl-sn-glycero-3-phosphocholine + octanoate
show the reaction diagram
1,2-dioctanoyl-sn-glycero-3-phosphoglycol + H2O
1-octanoyl-sn-glycero-3-phosphoglycol + octanoate
show the reaction diagram
-
-
-
?
1,2-dioleoyl-sn-phosphatidylcholine + H2O
1-oleoyl-sn-phosphatidylcholine + oleate
show the reaction diagram
-
-
-
?
1,2-dioleoyl-sn-phosphatidylethanolamine + H2O
1-oleoyl-sn-phosphatidylethanolamine + oleic acid
show the reaction diagram
-
-
-
?
1,2-dipalmitoyl-phosphatidylcholine + H2O
1-palmitoyl-glycerophosphocholine + palmitic acid
show the reaction diagram
-
1,2-dipalmitoyl-phosphatidylcholine, small unilamellar vesicles
-
-
?
1,2-dipalmitoyl-phosphatidylcholine + H2O
1-palmitoyl-glycerophosphorylcholine + palmitic acid
show the reaction diagram
1-acyl-2-linoleoyl-3-phosphoethanolamine + H2O
1-acyl-3-phosphoethanolamine + linolic acid
show the reaction diagram
-
-
-
?
1-hexadecanoyl-2-(1-pyrenedecanoyl)-sn-glycero-3-phosphogylcerol + H2O
1-hexadecanoyl-glycero-3-phosphoethanolamine + 1-pyrenedecanoate
show the reaction diagram
-
-
-
?
1-hexadecanoyl-2-9(cis)-octadecanoyl-rac-glycero-phosphorylcholine + H2O
?
show the reaction diagram
-
-
-
-
?
1-palmitoyl-2-(10-pyrenyldecanoyl)-sn-glycero-3-phosphate + H2O
10-pyrenyldecanoic acid + 1-palmitoyl-sn-glycero-3-phosphate
show the reaction diagram
-
-
-
-
?
1-palmitoyl-2-oleoylphosphatidylcholine + H2O
1-palmitoyl-glycerophosphocholine + oleic acid
show the reaction diagram
-
-
-
?
cardiolipin + H2O
?
show the reaction diagram
-
-
-
-
?
dihexanoyl-dithio-phosphatidylcholine + H2O
?
show the reaction diagram
proPLA2, monomeric substrate
-
-
?
dioctanoyl phosphatidylcholine + H2O
octanoyl phosphatidylcholine + octanoate
show the reaction diagram
-
-
-
?
dioleoyl phosphatidylglycerol + H2O
?
show the reaction diagram
-
-
-
-
?
oxidized phosphatidylcholine + H2O
lysophosphatidylcholine + fatty acid
show the reaction diagram
-
-
-
-
?
phosphatidic acid + H2O
1-acylglycerophosphate + fatty acid
show the reaction diagram
phosphatidylcholine + H2O
1-acylglycerophosphocholine + fatty acid
show the reaction diagram
phosphatidylcholine + H2O
lysophosphatidylcholine + a fatty acid
show the reaction diagram
-
-
-
-
?
phosphatidylethanolamine + H2O
1-acylglycerophosphorylethanolamine + fatty acid
show the reaction diagram
phosphatidylglycerol + H2O
1-acylglycerol + fatty acid
show the reaction diagram
phospholipids + H2O
?
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
1,2-diacyl-sn-glycero-3-phosphatide + H2O
?
show the reaction diagram
-
-
-
-
?
phosphatidylcholine + H2O
lysophosphatidylcholine + a fatty acid
show the reaction diagram
-
-
-
-
?
phospholipids + H2O
?
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Sr2+
-
diminishes susceptibility to trypsin attack and prevents p-bromophenacyl bromide inactivation
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(+-)-3-O-[4-(4,5-dihydro-5-oxo-1,2,4-4H-oxadiazol-3-yl)phenyl]-2-O-tetradecyl-1-O-triphenylmethylglycerol
-
-
1,2-Didecanoin
-
inhibition below the normal cutoff pressure of PLA2
1,2-dipalmitoyl-phosphatidylcholine
-
large unilamellar vesicles, inhibits hydrolysis of 1,2-dipalmitoyl-phosphatidylcholine small unilamellar vesicles
1-bromo-2-octanone
-
-
1-hexadecyl-3-(trifluoroethyl)-sn-glycero-2-phosphomethanol
i.e. MJ33
1-hexadecyl-3-trifluoroethylglycero-sn-2-phosphomethanol
-
MJ33, competitive inhibitor
1-sn-phosphoglycerides
-
-
3,3'-[[2-(pentyloxy)propane-1,3-diyl]bis(oxybenzene-4,1-diylethane-2,1-diyl)]bis(1,2,4-oxadiazol-5(4H)-one)
-
-
3,3'-[[2-(tetradecyloxy)propane-1,3-diyl]bis(oxybenzene-4,1-diylethane-2,1-diyl)]bis(1,2,4-oxadiazol-5(4H)-one)
-
-
3,3'-[[2-(tetradecyloxy)propane-1,3-diyl]bis(oxybenzene-4,1-diylmethanediyl)]bis(1,2,4-oxadiazol-5(4H)-one)
-
-
3,3'-[[3-(tetradecyloxy)propane-1,2-diyl]bis(oxybenzene-4,1-diylethane-2,1-diyl)]bis(1,2,4-oxadiazol-5(4H)-one)
-
-
3,3'-[[3-(tetradecyloxy)propane-1,2-diyl]bis(oxybenzene-4,1-diylmethanediyl)]bis(1,2,4-oxadiazol-5(4H)-one)
-
-
3,5-Dibromosalicylate
-
inhibition below the normal cutoff pressure of PLA2
3,5-diiodosalicylate
-
inhibition below the normal cutoff pressure of PLA2
3-(2-[4-[(4-tetradecylpiperazin-1-yl)carbonyl]phenyl]ethyl)-1,2,4-oxadiazol-5(4H)-one
-
-
3-(3-[4-[(4-tetradecylpiperazin-1-yl)carbonyl]phenyl]propyl)-1,2,4-oxadiazol-5(4H)-one
-
-
3-[4-(4-hexadecylpiperazin-1-yl)benzyl]-1,2,4-oxadiazol-5(4H)-one
-
-
3-[4-(4-octadecylpiperazin-1-yl)benzyl]-1,2,4-oxadiazol-5(4H)-one
-
-
3-[4-(4-tetradecylpiperazin-1-yl)benzyl]-1,2,4-oxadiazol-5(4H)-one
-
-
3-[4-(tetradecyloxy)benzyl]-1,2,4-oxadiazol-5(4H)-one
-
-
3-[4-[(4-docosylpiperazin-1-yl)carbonyl]benzyl]-1,2,4-oxadiazol-5(4H)-one
-
-
3-[4-[(4-hexadecylpiperazin-1-yl)carbonyl]benzyl]-1,2,4-oxadiazol-5(4H)-one
-
-
3-[4-[(4-hexadecylpiperazin-1-yl)carbonyl]phenyl]-1,2,4-oxadiazol-5(4H)-one
-
-
3-[4-[(4-hexadecylpiperazin-1-yl)methyl]benzyl]-1,2,4-oxadiazol-5(4H)-one
-
-
3-[4-[(4-hexadecylpiperazin-1-yl)methyl]phenyl]-1,2,4-oxadiazol-5(4H)-one
-
-
3-[4-[(4-icosylpiperazin-1-yl)carbonyl]benzyl]-1,2,4-oxadiazol-5(4H)-one
-
-
3-[4-[(4-octadecylpiperazin-1-yl)carbonyl]benzyl]-1,2,4-oxadiazol-5(4H)-one
-
-
3-[4-[(4-octadecylpiperazin-1-yl)carbonyl]phenyl]-1,2,4-oxadiazol-5(4H)-one
-
-
3-[4-[(4-octadecylpiperazin-1-yl)methyl]benzyl]-1,2,4-oxadiazol-5(4H)-one
-
-
3-[4-[(4-octadecylpiperazin-1-yl)methyl]phenyl]-1,2,4-oxadiazol-5(4H)-one
-
-
3-[4-[(4-tetradecylpiperazin-1-yl)carbonyl]benzyl]-1,2,4-oxadiazol-5(4H)-one
-
-
3-[4-[(4-tetradecylpiperazin-1-yl)carbonyl]phenyl]-1,2,4-oxadiazol-5(4H)-one
-
-
3-[4-[(4-tetradecylpiperazin-1-yl)methyl]benzyl]-1,2,4-oxadiazol-5(4H)-one
-
-
3-[4-[(4-tetradecylpiperazin-1-yl)methyl]phenyl]-1,2,4-oxadiazol-5(4H)-one
-
-
3-[4-[3-(4-butylphenoxy)-2-(tetradecyloxy)propoxy]benzyl]-1,2,4-oxadiazol-5(4H)-one
-
-
3-[4-[3-(4-methylphenoxy)-2-(tetradecyloxy)propoxy]benzyl]-1,2,4-oxadiazol-5(4H)-one
-
-
3-[4-[3-(decyloxy)-2-(tetradecyloxy)propoxy]benzyl]-1,2,4-oxadiazol-5(4H)-one
-
-
3-[4-[3-(diphenylmethoxy)-2-(tetradecyloxy)propoxy]benzyl]-1,2,4-oxadiazol-5(4H)-one
-
-
3-[4-[3-(pentyloxy)-2-(tetradecyloxy)propoxy]benzyl]-1,2,4-oxadiazol-5(4H)-one
-
-
3-[4-[3-ethoxy-2-(tetradecyloxy)propoxy]benzyl]-1,2,4-oxadiazol-5(4H)-one
-
-
Acetyl salicylate
-
inhibition below the normal cutoff pressure of PLA2
aristolochic acid
-
Cd2+
-
-
cholate
bile salt regulation of lipid metabolism via both activation and inhibition of PLA2, interaction and binding structure analysis, overview
darapladib
-
reduces development of advanced coronary atherosclerosis in diabetic and hypercholesterolemic swine, specifically reduces plaque area and necrotic core area and medial destruction, resulting in fewer lesions with an unstable phenotype
Dicetyl phosphate
-
inhibition below the normal cutoff pressure of PLA2
gallic acid
inhibitory in micromolar concentrations
glycochenodeoxycholate
bile salt regulation of lipid metabolism via both activation and inhibition of PLA2, interaction and binding structure analysis, overview
glycocholate
bile salt regulation of lipid metabolism via both activation and inhibition of PLA2, interaction and binding structure analysis, overview
Guanidine HCl
-
-
LY311727
-
-
manoalogue
-
synthetic analogue of the sea sponge-derived manoalide, time dependent irreversible loss of activity: modification of lysine residues
Me-Indoxam
-
-
MJ33
i.e. 1-hexadecyl-3-(trifluoroethyl)-rac-glycero-2-phosphomethanol, an active-site-directed tetrahedral mimic
N-dodecyl-N,N-dimethyl-3-aminopropanesulfonate
-
-
N-tetradecyl-N,N-dimethyl-3-aminopropanesulfonate
-
-
omega-bromo-4-nitroacetophenone
-
-
p-bromophenacyl bromide
-
-
Pb2+
-
-
protocatechuic acid
inhibitory in micromolar concentrations
quercetin
-
quercetin-3-beta-D-glucoside
-
rilapladib
-
-
salicylic acid
-
inhibition below the normal cutoff pressure of PLA2
Sr2+
-
competitive inhibition
syringic acid
inhibitory in micromolar concentrations
taurochenodeoxycholate
bile salt regulation of lipid metabolism via both activation and inhibition of PLA2, interaction and binding structure analysis, overview
taurocholate
bile salt regulation of lipid metabolism via both activation and inhibition of PLA2, interaction and binding structure analysis, overview
vanillic acid
inhibitory in micromolar concentrations
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3,5-Dibromosalicylate
-
enhanced enzyme penetration, activation above the normal cutoff pressure of PLA2
3,5-diiodosalicylate
-
enhanced enzyme penetration, activation above the normal cutoff pressure of PLA2
Acetyl salicylate
-
enhanced enzyme penetration, activation above the normal cutoff pressure of PLA2
cholate
bile salt regulation of lipid metabolism via both activation and inhibition of PLA2, interaction and binding structure analysis, overview
Dicetyl phosphate
-
enhanced enzyme penetration, activation above the normal cutoff pressure of PLA2
glycochenodeoxycholate
bile salt regulation of lipid metabolism via both activation and inhibition of PLA2, interaction and binding structure analysis, overview
glycocholate
bile salt regulation of lipid metabolism via both activation and inhibition of PLA2, interaction and binding structure analysis, overview
salicylic acid
-
enhanced enzyme penetration, activation above the normal cutoff pressure of PLA2
taurochenodeoxycholate
bile salt regulation of lipid metabolism via both activation and inhibition of PLA2, interaction and binding structure analysis, overview
taurocholate
bile salt regulation of lipid metabolism via both activation and inhibition of PLA2, interaction and binding structure analysis, overview
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3
1,2-diheptanoyl-sn-glycero-3-phosphocholine
-
-
1.4
1,2-dihexanoyl-sn-glycero-3-phosphocholine
-
-
3.2
1,2-dioctanoyl-sn-glycero-3-phosphocholine
-
-
0.1
1,2-dioctanoyl-sn-glycero-3-phosphoglycol
-
-
2
1,2-dipalmitoyl-phosphatidylcholine, small unilamellar vesicles
-
25.6°C
-
4.9
lysophosphatidylcholine
-
constant water activity of 0.22
0.2 - 4.9
phosphatidylcholine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.917 - 1.42
1,2-dipalmitoyl-phosphatidylcholine
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00827
aspirin
pH 8.5, 37°C
0.00095
gallic acid
pH 8.5, 37°C
0.00129
protocatechuic acid
pH 8.5, 37°C
0.00171
syringic acid
pH 8.5, 37°C
0.00232
vanillic acid
pH 8.5, 37°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1
3,3'-[[2-(pentyloxy)propane-1,3-diyl]bis(oxybenzene-4,1-diylethane-2,1-diyl)]bis(1,2,4-oxadiazol-5(4H)-one)
Sus scrofa
-
above, pH 7.5, isozyme hGIB sPLA2
0.0399
3,3'-[[2-(tetradecyloxy)propane-1,3-diyl]bis(oxybenzene-4,1-diylethane-2,1-diyl)]bis(1,2,4-oxadiazol-5(4H)-one)
Sus scrofa
-
pH 7.5, isozyme hGIB sPLA2
0.1
3,3'-[[2-(tetradecyloxy)propane-1,3-diyl]bis(oxybenzene-4,1-diylmethanediyl)]bis(1,2,4-oxadiazol-5(4H)-one)
Sus scrofa
-
above, pH 7.5, isozyme hGIB sPLA2
0.0578
3,3'-[[3-(tetradecyloxy)propane-1,2-diyl]bis(oxybenzene-4,1-diylethane-2,1-diyl)]bis(1,2,4-oxadiazol-5(4H)-one)
Sus scrofa
-
pH 7.5, isozyme hGIB sPLA2
0.0636
3,3'-[[3-(tetradecyloxy)propane-1,2-diyl]bis(oxybenzene-4,1-diylmethanediyl)]bis(1,2,4-oxadiazol-5(4H)-one)
Sus scrofa
-
pH 7.5, isozyme hGIB sPLA2
0.1
3-(2-[4-[(4-tetradecylpiperazin-1-yl)carbonyl]phenyl]ethyl)-1,2,4-oxadiazol-5(4H)-one
Sus scrofa
-
-
0.1
3-(3-[4-[(4-tetradecylpiperazin-1-yl)carbonyl]phenyl]propyl)-1,2,4-oxadiazol-5(4H)-one
Sus scrofa
-
-
0.05
3-O-[4-(4,5-dihydro-5-oxo-1,2,4-4H-oxadiazol-3-yl)phenyl]-2-O-tetradecyl-1-O-triphenylmethylglycerol
Sus scrofa
-
pH 7.5, isozyme hGIB sPLA2
0.1
3-[4-(4-hexadecylpiperazin-1-yl)benzyl]-1,2,4-oxadiazol-5(4H)-one
Sus scrofa
-
-
0.1
3-[4-(4-octadecylpiperazin-1-yl)benzyl]-1,2,4-oxadiazol-5(4H)-one
Sus scrofa
-
-
0.1
3-[4-(4-tetradecylpiperazin-1-yl)benzyl]-1,2,4-oxadiazol-5(4H)-one
Sus scrofa
-
-
0.1
3-[4-(tetradecyloxy)benzyl]-1,2,4-oxadiazol-5(4H)-one
Sus scrofa
-
-
0.1
3-[4-[(4-docosylpiperazin-1-yl)carbonyl]benzyl]-1,2,4-oxadiazol-5(4H)-one
Sus scrofa
-
-
0.1
3-[4-[(4-hexadecylpiperazin-1-yl)carbonyl]benzyl]-1,2,4-oxadiazol-5(4H)-one
Sus scrofa
-
-
0.1
3-[4-[(4-hexadecylpiperazin-1-yl)carbonyl]phenyl]-1,2,4-oxadiazol-5(4H)-one
Sus scrofa
-
-
0.1
3-[4-[(4-hexadecylpiperazin-1-yl)methyl]benzyl]-1,2,4-oxadiazol-5(4H)-one
Sus scrofa
-
-
0.1
3-[4-[(4-hexadecylpiperazin-1-yl)methyl]phenyl]-1,2,4-oxadiazol-5(4H)-one
Sus scrofa
-
-
0.1
3-[4-[(4-icosylpiperazin-1-yl)carbonyl]benzyl]-1,2,4-oxadiazol-5(4H)-one
Sus scrofa
-
-
0.1
3-[4-[(4-octadecylpiperazin-1-yl)carbonyl]benzyl]-1,2,4-oxadiazol-5(4H)-one
Sus scrofa
-
-
0.1
3-[4-[(4-octadecylpiperazin-1-yl)carbonyl]phenyl]-1,2,4-oxadiazol-5(4H)-one
Sus scrofa
-
-
0.1
3-[4-[(4-octadecylpiperazin-1-yl)methyl]benzyl]-1,2,4-oxadiazol-5(4H)-one
Sus scrofa
-
-
0.1
3-[4-[(4-octadecylpiperazin-1-yl)methyl]phenyl]-1,2,4-oxadiazol-5(4H)-one
Sus scrofa
-
-
0.1
3-[4-[(4-tetradecylpiperazin-1-yl)carbonyl]benzyl]-1,2,4-oxadiazol-5(4H)-one
Sus scrofa
-
-
0.1
3-[4-[(4-tetradecylpiperazin-1-yl)carbonyl]phenyl]-1,2,4-oxadiazol-5(4H)-one
Sus scrofa
-
-
0.1
3-[4-[(4-tetradecylpiperazin-1-yl)methyl]benzyl]-1,2,4-oxadiazol-5(4H)-one
Sus scrofa
-
-
0.1
3-[4-[(4-tetradecylpiperazin-1-yl)methyl]phenyl]-1,2,4-oxadiazol-5(4H)-one
Sus scrofa
-
-
0.0022
3-[4-[3-(4-butylphenoxy)-2-(tetradecyloxy)propoxy]benzyl]-1,2,4-oxadiazol-5(4H)-one
Sus scrofa
-
pH 7.5, isozyme hGIB sPLA2
0.025
3-[4-[3-(4-methylphenoxy)-2-(tetradecyloxy)propoxy]benzyl]-1,2,4-oxadiazol-5(4H)-one
Sus scrofa
-
pH 7.5, isozyme hGIB sPLA2
0.1
3-[4-[3-(decyloxy)-2-(tetradecyloxy)propoxy]benzyl]-1,2,4-oxadiazol-5(4H)-one
Sus scrofa
-
pH 7.5, isozyme hGIB sPLA2
0.0056
3-[4-[3-(diphenylmethoxy)-2-(tetradecyloxy)propoxy]benzyl]-1,2,4-oxadiazol-5(4H)-one
Sus scrofa
-
pH 7.5, isozyme hGIB sPLA2
0.1
3-[4-[3-(pentyloxy)-2-(tetradecyloxy)propoxy]benzyl]-1,2,4-oxadiazol-5(4H)-one
Sus scrofa
-
pH 7.5, isozyme hGIB sPLA2
0.04
3-[4-[3-ethoxy-2-(tetradecyloxy)propoxy]benzyl]-1,2,4-oxadiazol-5(4H)-one
Sus scrofa
-
pH 7.5, isozyme hGIB sPLA2
0.01
aristolochic acid
Sus scrofa
pH 7.4, 37°C, isozyme sPLA2 IB
0.008742
aspirin
Sus scrofa
pH 8.5, 37°C
0.001
gallic acid
Sus scrofa
pH 8.5, 37°C
0.008
LY311727
Sus scrofa
-
-
0.00134
protocatechuic acid
Sus scrofa
pH 8.5, 37°C
0.01
quercetin
Sus scrofa
pH 7.4, 37°C, isozyme sPLA2 IB
0.02
quercetin-3-beta-D-glucoside
Sus scrofa
pH 7.4, 37°C, isozyme sPLA2 IB
0.00181
syringic acid
Sus scrofa
pH 8.5, 37°C
0.00245
vanillic acid
Sus scrofa
pH 8.5, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1 - 10
-
phospholipid/Triton X-100: 1/2,1/3,und 1/4, phospholipid concentration up to 30 mM
1.6
-
PLA2 zymogen, substrate: egg yolk emulsion
10
substrate: monomeric dihexanoyl-dithio-phosphatidylcholine, proPLA2
1000
-
substrate: egg yolk emulsion
1050
-
10 mM phosphocholine, N-phosphocholine/N-sodiumcholate: 1.42
1150
-
substrate: egg yolk emulsion, PLA2 isoenzyme
1180
-
substrate: egg yolk emulsion, PLA2 isoenzyme
125
-
substrate: 1,2-dinonanoyl-sn-glycero-3-phosphocholine
1270
-
active PLA2, substrate: egg yolk emulsion
150
-
5 mM phosphocholine, N-phosphocholine/N-sodiumcholate: 0.36
16000
-
substrate: 1,2-dioctanoyl-sn-glycero-3-phosphoglycol
162
-
substrate: 1,2-dioctanoyl-sn-glycero-3-phosphocholine
1648
-
pH6, micellar 1,2-dioctanoyl-sn-glycero-3-phosphocholine, isoenzyme of e-amidinated PLA, 0.71 mM Ca2+
2000
substrate: micellar 1,2-dioctanoyl-sn-glycero-3-phosphocholine, active PLA2
2038
-
pH6, micellar 1,2-dioctanoyl-sn-glycero-3-phosphocholine, 0.64 mM Ca2+
2170
-
pH8, micellar 1,2-dioctanoyl-sn-glycero-3-phosphocholine, iso-AMPA, 0.30 mM Ca2+
29
-
substrate: 1,2-dipalmitoyl-phosphatidylcholine
295
-
substrate: dioleolyl-sn-phosphatidylethanolamine
320
-
substrate: dioleolyl-sn-phosphatidylcholine
330
-
freshly dialyzed PLA2
383
-
5 mM phosphocholine, N-phosphocholine/N-sodiumcholate: 0.67
460
-
7.5 mM phosphocholine, N-phosphocholine/N-sodiumcholate: 0.67
520
-
10 mM phosphocholine, N-phosphocholine/N-sodiumcholate: 0.67
576
-
5 mM phosphocholine, N-phosphocholine/N-sodiumcholate: 1.0
615
-
substrate: dioleolyl phosphatidylglycerol
68
-
substrate: dimyristoyl-sn-phosphatidylcholine
741
-
5 mM phosphocholine, N-phosphocholine/N-sodiumcholate: 1.42
775
-
7.5 mM phosphocholine, N-phosphocholine/N-sodiumcholate: 1.0
80
-
substrate: 1,2-dilaureoyl-sn-glycero-3-phosphocholine
800
-
isoenzyme b-PLA2, substrate: egg yolk emulsion
804
-
10 mM phosphocholine, N-phosphocholine/N-sodiumcholate: 1.0
81
-
substrate: 1,2-didecanoyl-sn-glycero-3-phosphocholine
82
-
5 mM phosphocholine, N-phosphocholine/N-sodiumcholate: 0.20
870
-
7.5 mM phosphocholine, N-phosphocholine/N-sodiumcholate: 1.42
933
-
5 mM phosphocholine, N-phosphocholine/N-sodiumcholate: 2.0
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
assay at
7.5
-
assay at
8.5
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
-
highest enzyme activity rate, but decrease of substrate occurs
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PRDX6_PIG
224
0
25037
Swiss-Prot
other Location (Reliability: 1)
PA21B_PIG
146
0
16279
Swiss-Prot
Secretory Pathway (Reliability: 2)
PA22_PIG
124
0
13969
Swiss-Prot
other Location (Reliability: 3)
A0A8D1DRF6_PIG
852
0
94776
TrEMBL
Mitochondrion (Reliability: 4)
A0A4X1V0Q2_PIG
852
0
94737
TrEMBL
Mitochondrion (Reliability: 4)
A0A8D0PXK1_PIG
812
0
91073
TrEMBL
other Location (Reliability: 5)
A0A8D0SCA6_PIG
1462
1
162248
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8D0IZK5_PIG
215
0
24302
TrEMBL
other Location (Reliability: 1)
I3L8W8_PIG
782
0
86962
TrEMBL
other Location (Reliability: 2)
A0A287BF92_PIG
693
0
77051
TrEMBL
other Location (Reliability: 2)
A0A8D1ZUG7_PIG
97
0
10999
TrEMBL
other Location (Reliability: 3)
A0A8D0ZEW1_PIG
780
0
88372
TrEMBL
Secretory Pathway (Reliability: 4)
A0A8D1VCV5_PIG
150
0
17068
TrEMBL
other Location (Reliability: 4)
A0A8D1GQN2_PIG
137
0
15538
TrEMBL
Secretory Pathway (Reliability: 4)
A0A8D0NSL4_PIG
1383
1
153322
TrEMBL
other Location (Reliability: 2)
A0A4X1VDC5_PIG
224
0
25053
TrEMBL
other Location (Reliability: 1)
I3LAK1_PIG
730
0
82929
TrEMBL
Mitochondrion (Reliability: 3)
A0A8D1VE37_PIG
141
0
15293
TrEMBL
Secretory Pathway (Reliability: 1)
A0A4X1W493_PIG
138
0
15754
TrEMBL
Secretory Pathway (Reliability: 1)
A0A4X1U1X0_PIG
188
0
20691
TrEMBL
Mitochondrion (Reliability: 5)
A0A4X1W6R2_PIG
62
1
6674
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8D0LTR8_PIG
215
0
24299
TrEMBL
other Location (Reliability: 1)
I3LLM3_PIG
721
0
81998
TrEMBL
other Location (Reliability: 2)
A0A8D1HHM6_PIG
302
0
33067
TrEMBL
other Location (Reliability: 2)
A0A8D0ZTU4_PIG
124
0
13414
TrEMBL
other Location (Reliability: 4)
A0A8D0PHH4_PIG
836
0
92831
TrEMBL
other Location (Reliability: 2)
A0A480NGH1_PIG
573
0
64821
TrEMBL
other Location (Reliability: 2)
A0A8D1C220_PIG
146
0
16263
TrEMBL
Secretory Pathway (Reliability: 2)
A0A8D1WZC7_PIG
812
0
91132
TrEMBL
other Location (Reliability: 5)
A0A8D1G5S2_PIG
146
0
16254
TrEMBL
Secretory Pathway (Reliability: 2)
A0A8D0NU16_PIG
729
0
83332
TrEMBL
other Location (Reliability: 2)
A0A8D0R5M1_PIG
125
0
14018
TrEMBL
Mitochondrion (Reliability: 5)
F1SFK4_PIG
852
0
94764
TrEMBL
Mitochondrion (Reliability: 4)
A0A8D1HH31_PIG
147
0
16544
TrEMBL
other Location (Reliability: 4)
A0A8D0IB44_PIG
204
0
22545
TrEMBL
Mitochondrion (Reliability: 4)
A0A8D0JT96_PIG
810
0
90955
TrEMBL
other Location (Reliability: 5)
A0A8D1L9I2_PIG
209
0
23083
TrEMBL
other Location (Reliability: 1)
A0A8D1TLJ3_PIG
729
0
82801
TrEMBL
Mitochondrion (Reliability: 3)
A0A4X1V1H8_PIG
847
0
96959
TrEMBL
other Location (Reliability: 2)
A0A8D1HHI7_PIG
125
0
14189
TrEMBL
other Location (Reliability: 3)
A0A4X1V018_PIG
812
0
91152
TrEMBL
other Location (Reliability: 5)
A0A8D0K4P5_PIG
852
0
94669
TrEMBL
Mitochondrion (Reliability: 4)
A0A8D0ZDP3_PIG
812
0
91224
TrEMBL
other Location (Reliability: 5)
A0A8D0MW73_PIG
124
0
14187
TrEMBL
other Location (Reliability: 4)
A0A8D1QM43_PIG
238
1
26386
TrEMBL
Secretory Pathway (Reliability: 3)
A0A8D1JYF0_PIG
154
0
16456
TrEMBL
Secretory Pathway (Reliability: 5)
A0A8D0ZND2_PIG
730
0
82971
TrEMBL
Mitochondrion (Reliability: 3)
A0A8D0VV69_PIG
148
0
16555
TrEMBL
Secretory Pathway (Reliability: 2)
A0A8D1K5M9_PIG
812
0
91145
TrEMBL
other Location (Reliability: 5)
A0A8D1FYN7_PIG
782
0
86962
TrEMBL
other Location (Reliability: 2)
A0A4X1T7H7_PIG
70
0
7598
TrEMBL
Secretory Pathway (Reliability: 2)
A0A8D0WRJ6_PIG
847
0
96946
TrEMBL
other Location (Reliability: 2)
A0A8D1P6S2_PIG
141
0
15214
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8D0WN55_PIG
780
0
88330
TrEMBL
Secretory Pathway (Reliability: 4)
A0A480XKF8_PIG
891
0
99309
TrEMBL
other Location (Reliability: 3)
A0A286ZM79_PIG
302
0
33095
TrEMBL
other Location (Reliability: 2)
A0A8D1VCD6_PIG
302
0
33085
TrEMBL
other Location (Reliability: 3)
A0A8D1DQC1_PIG
730
0
82887
TrEMBL
Mitochondrion (Reliability: 3)
A0A286ZWY3_PIG
806
0
89753
TrEMBL
Mitochondrion (Reliability: 4)
A0A8D1DRW4_PIG
766
0
86851
TrEMBL
Mitochondrion (Reliability: 3)
A0A8D0ZK53_PIG
852
0
94766
TrEMBL
Mitochondrion (Reliability: 4)
A0A8D1GPB1_PIG
144
0
16478
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8D1QQQ7_PIG
836
0
92877
TrEMBL
other Location (Reliability: 2)
A0A8D1KXK5_PIG
142
1
15910
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8D1QR80_PIG
139
0
15635
TrEMBL
Mitochondrion (Reliability: 3)
A0A481BWF8_PIG
881
0
98234
TrEMBL
other Location (Reliability: 3)
A0A8D0WQ96_PIG
846
0
96818
TrEMBL
other Location (Reliability: 2)
A0A8D1TS04_PIG
218
1
24088
TrEMBL
Secretory Pathway (Reliability: 3)
A0A8D0M5I4_PIG
1462
1
162118
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8D1TS02_PIG
204
0
22827
TrEMBL
other Location (Reliability: 3)
A0A287AV88_PIG
188
0
20622
TrEMBL
Mitochondrion (Reliability: 5)
A0A8D0LI03_PIG
141
1
15878
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8D1ZFE3_PIG
852
0
94785
TrEMBL
Mitochondrion (Reliability: 4)
A0A8D0MPC9_PIG
302
0
33069
TrEMBL
other Location (Reliability: 3)
A0A4X1V0R9_PIG
780
0
88329
TrEMBL
Secretory Pathway (Reliability: 4)
A0A480LVA8_PIG
738
0
83965
TrEMBL
other Location (Reliability: 2)
A0A8D1UBL5_PIG
766
0
86893
TrEMBL
Mitochondrion (Reliability: 3)
A0A8D1KED7_PIG
760
0
86203
TrEMBL
other Location (Reliability: 2)
A0A8D0HW54_PIG
782
0
86937
TrEMBL
other Location (Reliability: 2)
A0A8D1G1N3_PIG
743
1
82481
TrEMBL
other Location (Reliability: 2)
A0A4X1VPF6_PIG
752
0
83853
TrEMBL
Mitochondrion (Reliability: 4)
A0A8D1PAY9_PIG
302
0
33095
TrEMBL
other Location (Reliability: 2)
A0A480MPD8_PIG
836
0
92894
TrEMBL
other Location (Reliability: 3)
A0A8D0V8U0_PIG
782
0
86990
TrEMBL
other Location (Reliability: 2)
A0A287BBG6_PIG
872
0
99674
TrEMBL
Mitochondrion (Reliability: 2)
A0A8D0T1D9_PIG
747
2
83607
TrEMBL
other Location (Reliability: 2)
A0A4X1W477_PIG
356
0
39173
TrEMBL
other Location (Reliability: 2)
A0A8D1XP58_PIG
1462
1
162273
TrEMBL
Secretory Pathway (Reliability: 1)
A0A4X1V0P2_PIG
730
0
82929
TrEMBL
Mitochondrion (Reliability: 3)
A0A4X1VN98_PIG
806
0
89753
TrEMBL
Mitochondrion (Reliability: 4)
A0A8D0V8G9_PIG
836
0
92859
TrEMBL
other Location (Reliability: 2)
A0A286ZPB0_PIG
1462
1
162273
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8D0PD64_PIG
125
1
13376
TrEMBL
Secretory Pathway (Reliability: 2)
A0A287BRJ6_PIG
758
0
86620
TrEMBL
other Location (Reliability: 5)
A0A8D1DRX2_PIG
780
0
88287
TrEMBL
Secretory Pathway (Reliability: 4)
A0A4X1TRG4_PIG
749
0
85376
TrEMBL
other Location (Reliability: 2)
A0A8D1WZL2_PIG
730
0
82929
TrEMBL
Mitochondrion (Reliability: 3)
A0A8D1Z4N4_PIG
154
0
16426
TrEMBL
Mitochondrion (Reliability: 5)
A0A8D1SBL1_PIG
812
0
91196
TrEMBL
other Location (Reliability: 5)
A0A4X1W5F3_PIG
218
1
24146
TrEMBL
Secretory Pathway (Reliability: 3)
A0A8D1QDW1_PIG
204
0
22526
TrEMBL
Mitochondrion (Reliability: 4)
A0A8D1S4X9_PIG
852
0
94764
TrEMBL
Mitochondrion (Reliability: 4)
A0A8D0K6L2_PIG
213
0
24099
TrEMBL
other Location (Reliability: 1)
A0A8D1NBH1_PIG
852
0
94763
TrEMBL
Mitochondrion (Reliability: 4)
A0A8D0X741_PIG
204
0
22529
TrEMBL
Mitochondrion (Reliability: 4)
A0A8D0ZHX6_PIG
713
0
81289
TrEMBL
other Location (Reliability: 2)
A0A8D1GF37_PIG
1462
1
162157
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8D1P2U7_PIG
292
0
31139
TrEMBL
other Location (Reliability: 2)
A0A8D0ZJ45_PIG
729
0
82843
TrEMBL
Mitochondrion (Reliability: 3)
A0A8D1FE73_PIG
124
0
13428
TrEMBL
other Location (Reliability: 4)
A0A8D0PWC7_PIG
770
0
84635
TrEMBL
Mitochondrion (Reliability: 5)
A0A8D0SZ31_PIG
959
0
106013
TrEMBL
Mitochondrion (Reliability: 4)
A0A286ZJ06_PIG
125
0
14219
TrEMBL
other Location (Reliability: 3)
A0A8D0HW72_PIG
806
0
89698
TrEMBL
Mitochondrion (Reliability: 4)
A0A8D1DRS7_PIG
847
0
96945
TrEMBL
other Location (Reliability: 2)
A0A4X1W594_PIG
147
0
16376
TrEMBL
other Location (Reliability: 2)
A0A4X1TLW3_PIG
758
0
86620
TrEMBL
other Location (Reliability: 5)
A0A8D0PMX2_PIG
693
0
77051
TrEMBL
other Location (Reliability: 2)
A0A287AQ26_PIG
749
0
85376
TrEMBL
other Location (Reliability: 2)
F1SSW8_PIG
780
0
88329
TrEMBL
Secretory Pathway (Reliability: 4)
A0A8D0WP91_PIG
766
0
86893
TrEMBL
Mitochondrion (Reliability: 3)
A0A287A3L1_PIG
161
1
18190
TrEMBL
Secretory Pathway (Reliability: 3)
F1SSX2_PIG
812
0
91196
TrEMBL
other Location (Reliability: 5)
A0A8D1UT09_PIG
146
0
16299
TrEMBL
Secretory Pathway (Reliability: 2)
A0A8D0WN76_PIG
812
0
91149
TrEMBL
other Location (Reliability: 5)
A0A4X1TKN8_PIG
1460
1
161934
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8D0SZT9_PIG
735
0
81203
TrEMBL
other Location (Reliability: 2)
A0A8D1J2E6_PIG
782
0
86978
TrEMBL
other Location (Reliability: 2)
A0A8D1ZP17_PIG
729
0
82801
TrEMBL
Mitochondrion (Reliability: 3)
A0A8D1VEY7_PIG
125
0
14219
TrEMBL
other Location (Reliability: 3)
A0A8D1MT60_PIG
1462
1
162276
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8D0P9M2_PIG
146
0
16278
TrEMBL
Secretory Pathway (Reliability: 2)
A0A8D1SUT2_PIG
154
0
16519
TrEMBL
Mitochondrion (Reliability: 5)
A0A8D1BT96_PIG
749
0
85260
TrEMBL
other Location (Reliability: 3)
A0A8D1P6M1_PIG
149
0
16978
TrEMBL
other Location (Reliability: 3)
A0A8D0IPE1_PIG
149
0
16906
TrEMBL
other Location (Reliability: 4)
I3LV50_PIG
146
0
16254
TrEMBL
Secretory Pathway (Reliability: 2)
A0A4X1W585_PIG
161
1
18190
TrEMBL
Secretory Pathway (Reliability: 3)
A0A8D2BQ22_PIG
1463
1
162482
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8D0M5X4_PIG
146
0
16267
TrEMBL
Secretory Pathway (Reliability: 2)
A0A8D0WFX4_PIG
1462
1
162090
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8D0MPE4_PIG
305
0
32762
TrEMBL
other Location (Reliability: 3)
A0A8D1AWD9_PIG
125
0
14145
TrEMBL
other Location (Reliability: 3)
A0A8D0U6M8_PIG
148
0
16569
TrEMBL
Secretory Pathway (Reliability: 2)
A0A4X1T6X5_PIG
145
0
16172
TrEMBL
Secretory Pathway (Reliability: 2)
A0A8D1HKT9_PIG
154
0
16495
TrEMBL
Mitochondrion (Reliability: 5)
A0A4X1VZJ0_PIG
147
0
16770
TrEMBL
Secretory Pathway (Reliability: 1)
A0A4X1W4B6_PIG
142
1
15982
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8D0HY84_PIG
738
0
82085
TrEMBL
Mitochondrion (Reliability: 4)
A0A8D1K5M3_PIG
846
0
96817
TrEMBL
other Location (Reliability: 2)
A0A8D0V712_PIG
716
0
81568
TrEMBL
other Location (Reliability: 2)
A0A8D0R5A3_PIG
224
0
25083
TrEMBL
other Location (Reliability: 1)
A0A8D0M5Z7_PIG
159
0
17589
TrEMBL
Secretory Pathway (Reliability: 2)
A0A8D1GT71_PIG
144
0
16161
TrEMBL
Secretory Pathway (Reliability: 2)
A0A287AW04_PIG
142
1
15910
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8D1CU28_PIG
148
0
16571
TrEMBL
Secretory Pathway (Reliability: 2)
A0A8D1NXD6_PIG
779
0
85985
TrEMBL
other Location (Reliability: 2)
A0A8D1NYK6_PIG
740
0
81828
TrEMBL
Mitochondrion (Reliability: 4)
A0A4X1W6Q0_PIG
156
0
17718
TrEMBL
other Location (Reliability: 5)
A0A5G2Q6U2_PIG
62
1
6674
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8D0Q6M7_PIG
780
0
88273
TrEMBL
Secretory Pathway (Reliability: 4)
A0A8D0Q579_PIG
729
0
82745
TrEMBL
Mitochondrion (Reliability: 3)
A0A8D1B0B6_PIG
302
0
33125
TrEMBL
other Location (Reliability: 2)
A0A4X1T816_PIG
161
0
17778
TrEMBL
Secretory Pathway (Reliability: 2)
A0A8D0X428_PIG
124
0
14140
TrEMBL
other Location (Reliability: 3)
A0A8D1NC21_PIG
812
0
91121
TrEMBL
other Location (Reliability: 5)
A0A4X1V1I3_PIG
883
0
100760
TrEMBL
Mitochondrion (Reliability: 2)
A0A8D0WKP9_PIG
852
0
94767
TrEMBL
Mitochondrion (Reliability: 4)
A0A8D0S2F1_PIG
812
0
91154
TrEMBL
other Location (Reliability: 5)
A0A8D1HMW6_PIG
292
0
31183
TrEMBL
other Location (Reliability: 2)
A0A286ZX54_PIG
138
0
15754
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8D1DWF9_PIG
1463
1
162316
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8D1P4J7_PIG
803
0
88774
TrEMBL
Mitochondrion (Reliability: 4)
A0A5G2QZC5_PIG
70
0
7598
TrEMBL
Secretory Pathway (Reliability: 2)
A0A8D1S011_PIG
846
0
96831
TrEMBL
other Location (Reliability: 2)
A0A5G2R574_PIG
146
0
16286
TrEMBL
Secretory Pathway (Reliability: 2)
A0A4X1TRI6_PIG
756
0
86234
TrEMBL
other Location (Reliability: 4)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
13950
-
amino acid composition analysis
14000
15000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
only the dimer is catalytically active, no data concerning MW
homotetramer
crystal form-1, crystallography
monomer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
10-2.2 A resolution, R-factor of 17.6%
-
2.6 resolution, R-factor of 0.241, 4295 reflections
-
group-IB secreted sPLA2 complexed with 12 molecules of octyl sulfate (C8S), by hanging drop vapor diffusion method at 25°C, to 2.7 A resolution. Crystal form-1 belongs to space group P212121 with unit cell paramteters a = 66.0 A, b = 82.1 A, c = 123.8 A, with four protein subunits in the asymmetric unit. Crystal form-2 belongs to space group P3121 with unit cell paramteters a = 66.1 A, b = 69.1 A, c = 68.8 A, with one subunit in the asymmetric unit. Main difference of crystallization conditions between the two crystal forms is the presence of 20% (v/v) isopropanol in crystal form-2. Alkyl tails of the C8S molecules are centered in the middle of the tetrameric cluster of sPLA2 subunits. Three of the four sPLA2 subunits contain a C8S molecule in the active site pocket. Sulfate oxygen of a C8S ligand is complexed to the active site calcium in three of the four protein active sites. Interactions of the alkyl sulfate head group with Arg-6 and Lys-10, as well as the backbone amide of Met-20. Cluster of three anions in the structure is postulated to be the site for nucleating the binding of anionic amphiphiles to the interfacial surface of the protein, and therefore this binding interaction has implications for interfacial activation of the enzyme
pancreatic PLA2 in complex with five different naturally occurring bile salts, i.e. cholate, taurocholate, glycocholate, glycochenodeoxycholate, and taurochenodeoxycholate, in presence or absence of active-site-directed tetrahedral mimic MJ33, hanging drop vapour diffusion method, 15 mg/ml protein solution with 10 mM CaCl2, 3 mM MJ33, and 3 mM bile salt, is mixed with an equal volume of 0.001 ml of cyrstallization solution containing 0.2 M CaCl2, 0.1 M HEPES, pH 7.5, and 28% v/v PEG 400 or 0.1 M sodium cacodylate, pH 6.5, and 1.4 M sodium acetate, 1 week to 2 months, X-ray diffraction structure determination and analysis at 1.85-2.20 A resolution, modeling
prePLA2
-
wild-type and mutant A12T/H15D/M20L/E71N, in ligand-free form and in complex with inhibitor MJ33
x-ray crystal structure, Y52F mutant: R-factor of 18.1% and 7-2.3 A resolution, Y73F mutant: R-factor of 19.1% and 7-2.4 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A12T/H15D/M20L/E71N
catalytic activity similar to wild-type
F63V
-
-
Y52F
-
-
Y73F
-
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100
-
pH 5.0, heated in boiling water for 15 min
98
-
for 5 min., pH 4.0, no loss of activity, for 1 h, pH 4.0, 45% of activity are recovered
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
toluene
-
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C
-
-20°C, lyophilized enzyme, for years
-
4°C, 1 mg PLA2 per ml
-
4°C, aqueous solution of 1 mg protein per ml, pH 6, more than 90% of enzymes activity remains after 2-3 weeks
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
column chromatography
-
isoenzyme b-PLA2, ion-exchange chromatography
-
on CM ion exchange resin, over 90% pure
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
group-IB sPLA2 expressed from Escherichia coli
into pBR322 and pCI1857, transformation of Escherichia coli strains HB101 and AB1157
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
S-sulfonation method
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
development of a spectrophotometric assay to measure, continuously and specifically, phospholipase A1 or phospholipase A2 activities using synthetic glycerophosphatidylcholines containing alpha-eleostearic acid. Substrates 1-alpha-eleostearoyl-2-octadecyl-rac-glycero-3-phosphocholine or 1-octadecyl-2-alpha-eleostearoyl-rac-glycero-3-phosphocholine differentiate, with excellent accuracy, between PLA1 and PLA2 activity
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Egger, D.; Wehtje, E.; Adlercreutz, P.
Characterization and optimation of phospholipase A2 catalyzed synthesis of phosphatidylcholine
Biochim. Biophys. Acta
1343
76-84
1997
Sus scrofa
Manually annotated by BRENDA team
Franken, P.A.; van den Berg, L.; Huang, J.; Gunyuzlu, P.; Lugtigheid, R.B.; Verheij, H.M.; de Haas, G.H.
Purification and characterization of a mutant human platelet phospholipase A2 expressed in Escherichia coli
Eur. J. Biochem.
203
89-98
1992
Homo sapiens, Naja melanoleuca, Sus scrofa
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
De Geus, P.; van den Bergh, C.J.; Kuipers, O.; Verheij, H.M.; Hockstra, W.P.M.; de Haas, G.H.
Expression of porcine pancreatic phospholipase A2. Generation of active enzyme by sequence-specific cleavage of a hybrid protein from Escherichia coli
Nucleic Acids Res.
15
3743-3759
1987
Sus scrofa (P00592), Sus scrofa
Manually annotated by BRENDA team
Romero, G.; Thompson, K.; Biltonen, R.L.
The activation of porcine pancreatic phospholipase A2 by dipalmitoylphosphatidylcholine large unilamellar vesicles
J. Biol. Chem.
262
13476-13482
1987
Sus scrofa
Manually annotated by BRENDA team
Menashe, M.
Hydrolysis of dipalmitoylphosphatidylcholine small unilamellar vesicles by porcine pancreatic phospholipase A2
J. Biol. Chem.
261
5328-5333
1986
Sus scrofa
Manually annotated by BRENDA team
Lichtenberg, D.; Romero, G.; Menashe, M.; Biltonen, R.L.
Hydrolysis of dipalmitoylphosphatidylcholine large unilamellar vesicles by porcine pancreatic phospholipase A2
J. Biol. Chem.
261
5334-5340
1986
Sus scrofa
Manually annotated by BRENDA team
Hoffman, W.J.; Vahey, M.; Hajdu, J.
Pancreatic porcine phospholipase A2 catalyzed hydrolysis of phosphatidylcholine in lecithin-bile salt mixed micelles: Kinetic studies in a lecithin-sodium cholate system
Arch. Biochem. Biophys.
221
361-370
1983
Naja naja, Sus scrofa
Manually annotated by BRENDA team
Donne-Op den Kelder, G.M.; de Haas, G.H.; Egmond, M.R.
Localization of the second calcium ion binding site in porcine and equine phospholipase A2
Biochemistry
22
2470-2478
1983
Bos taurus, Equus caballus, Homo sapiens, Sus scrofa
Manually annotated by BRENDA team
Dijkstra, B.W.; Renetseder, R.; Kalk, K.H.; Hol, W.G.J.; Drenth, J.
Structure of porcine pancreatic phospholipase A2 at 2.6 A resolution and comparison with bovine phospholipase A2
J. Mol. Biol.
168
163-179
1983
Sus scrofa
Manually annotated by BRENDA team
Hendrickson, H.S.; Trygstad, W.M.; Loftness, T.L.; Sailer, S.L.
Phospholipase A2 activity on mixed lipid monolayers: Activation of phospholipase A2 from porcine pancreas and Crotalus adamanteus by anionic and neutral amphophiles
Arch. Biochem. Biophys.
212
508-514
1981
Crotalus adamanteus, Sus scrofa
Manually annotated by BRENDA team
Slotboom, A.J.; Jansen, E.H.J.M.; Vlijm, H.; Pattus, F.; de Araujo, P.S.; de Haas, G.H.
Ca2+ binding to porcine pancreatic phospholipase A2 and its function in enzyme-lipid interaction
Biochemistry
17
4593-4600
1978
Sus scrofa
Manually annotated by BRENDA team
Drenth, J.; Enzing, C.M.; Kalk, K.H.; Vessies, J.C.A.
Structure of porcine pancreatic phospholipase A2
Nature
264
373-377
1976
Sus scrofa
Manually annotated by BRENDA team
Van Wezel, F.M.; de Haas, G.H.
Phospholipase A2 isoenzyme from porcine pancreas. Purification and some properties
Biochim. Biophys. Acta
410
299-309
1975
Sus scrofa
Manually annotated by BRENDA team
Pieterson W.A.; Volwerk, J.J.; de Haas, G.H.
Interaction of phospholipase A2 and its zymogen with divalent metal ions
Biochemistry
13
1439-1445
1974
Sus scrofa
Manually annotated by BRENDA team
Nieuwenhuizen, W.; Kunze, H.; de Haas, G.H.
Phospholipase A2 (phosphatide acylhydrolase, EC 3.1.1.4) from porcine pancreas
Methods Enzymol.
32
147-154
1974
Sus scrofa
Manually annotated by BRENDA team
Volwerk, J.J.; Pieterson, W.A.; de Haas, G.H.
Histidine at the active site of phospholipase A2
Biochemistry
13
1446-1454
1974
Sus scrofa
Manually annotated by BRENDA team
Pieterson, W.A.; Vidal, J.C.; Volwerk, J.J.; de Haas, G.H.
Zymogen-catalyzed hydrolysis of monomeric substrates and the presence of a recognition site for lipid-water interfaces in phospholipase A2
Biochemistry
13
1455-1460
1974
Sus scrofa
Manually annotated by BRENDA team
Rahman, Y.E.; Cerny, E.A.; Peraino, C.
Purification and some properties of rat spleen phospholipase A
Biochim. Biophys. Acta
321
526-535
1973
Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Nieuwenhuizen, W.; Steenbergh, P.; de Haas, G.H.
The isolation and properties of two phospholipases A2 from porcine pancreas
Eur. J. Biochem.
40
1-7
1973
Sus scrofa
Manually annotated by BRENDA team
Yamaguchi, T.; Okawa, Y.; Sakaguchi, K.
Two thermostable phospholipases A in porcine pancreas
J. Biochem.
73
187-190
1973
Sus scrofa
Manually annotated by BRENDA team
Hanahan, D.J.
Phospholipases
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
5
71-85
1971
Crotalus adamanteus, Crotalus atrox, Rattus norvegicus, Sus scrofa
-
Manually annotated by BRENDA team
Thunissen, M.M.; Franken, P.A.; de Haas, G.H.; Drenth, J.; Kalk, K.H.; Verheij, H.M.; Dijkstra, B.W.
Crystal structure of a porcine pancreatic phospholipase A2 mutant. A large conformational change caused by the F63V mutant
J. Mol. Biol.
232
839-855
1993
Sus scrofa
Manually annotated by BRENDA team
Thunissen, M.M.; Franken, P.A.; de Haas, G.H.; Drenth, J.; Kalk, K.H.; Verheij, H.M.; Dijkstra, B.W.
Site-directed mutagenesis and X-ray crystallography of two phospholipase A2 mutants: Y52F and Y73F
Protein Eng.
5
597-603
1992
Sus scrofa
Manually annotated by BRENDA team
Yamazaki, K.; Imai, M.; Suzuki, I.
Soybean lecithin hydrolysis using hog pancreas phospholipase A2 influenced by the hydrophobic character of W/O microemulsion systems
Biochem. Eng. J.
19
171-179
2004
Sus scrofa
-
Manually annotated by BRENDA team
Yu, B.Z.; Pan, Y.H.; Janssen, M.J.; Bahnson, B.J.; Jain, M.K.
Kinetic and structural properties of disulfide engineered phospholipase A2: insight into the role of disulfide bonding patterns
Biochemistry
44
3369-3379
2005
Sus scrofa (P00592), Sus scrofa
Manually annotated by BRENDA team
Boehl, M.; Ketscher, L.; Tietboehl, C.; Gutzeit, H.O.
Phospholipase A2 inhibition at different substrate concentrations
Anal. Biochem.
359
280-282
2006
Sus scrofa (P00592)
Manually annotated by BRENDA team
Touaibia, M.; Djimde, A.; Cao, F.; Boilard, E.; Bezzine, S.; Lambeau, G.; Redeuilh, C.; Lamouri, A.; Massicot, F.; Chau, F.; Dong, C.Z.; Heymans, F.
Inhibition of secreted phospholipase A2. 4-glycerol derivatives of 4,5-dihydro-3-(4-tetradecyloxybenzyl)-1,2,4-4H-oxadiazol-5-one with broad activities
J. Med. Chem.
50
1618-1626
2007
Homo sapiens, Sus scrofa
Manually annotated by BRENDA team
Pan, Y.H.; Bahnson, B.J.
Structural basis for bile salt inhibition of pancreatic phospholipase A2
J. Mol. Biol.
369
439-450
2007
Sus scrofa (P00592)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Zarai, Z.; Bacha, A.B.; Horchani, H.; Bezzine, S.; Zouari, N.; Gargouri, Y.; Mejdoub, H.
A novel hepatopancreatic phospholipase A2 from Hexaplex trunculus with digestive and toxic activities
Arch. Biochem. Biophys.
494
121-129
2010
Camelus dromedarius, Struthio camelus, Sus scrofa, Hexaplex trunculus
Manually annotated by BRENDA team
Pan, Y.H.; Bahnson, B.J.
Structure of a premicellar complex of alkyl sulfates with the interfacial binding surfaces of four subunits of phospholipase A2
Biochim. Biophys. Acta
1804
1443-1448
2010
Sus scrofa (P00592), Sus scrofa
Manually annotated by BRENDA team
Boukli, L.; Touaibia, M.; Meddad-Belhabich, N.; Djimde, A.; Park, C.; Kim, J.; Yoon, J.; Lamouri, A.; Heymans, F.
Design of new potent and selective secretory phospholipase A2 inhibitors. Part 5: Synthesis and biological activity of 1-alkyl-4-[4,5-dihydro-1,2,4-[4H]-oxadiazol-5-one-3-ylmethylbenz-4'-yl(oyl)] piperazines
Bioorg. Med. Chem.
16
1242-1253
2008
Homo sapiens, Sus scrofa
Manually annotated by BRENDA team
Garcia-Garcia, H.M.; Serruys, P.W.
Phospholipase A2 inhibitors
Curr. Opin. Lipidol.
20
327-332
2009
Homo sapiens, Sus scrofa
Manually annotated by BRENDA team
El Alaoui, M.; Soulere, L.; Noiriel, A.; Popowycz, F.; Khatib, A.; Queneau, Y.; Abousalham, A.
A continuous spectrophotometric assay that distinguishes between phospholipase A1 and A2 activities
J. Lipid Res.
57
1589-1597
2016
Sus scrofa
Manually annotated by BRENDA team
Karkabounas, A.; Georgiadou, D.G.; Argitis, P.; Psycharis, V.; Nakos, G.; Kosmas, A.M.; Lekka, M.E.
Immobilization of lipid substrates application on phospholipase A2 determination
Lipids
50
1259-1271
2015
Sus scrofa (P00592)
Manually annotated by BRENDA team
Dileep, K.V.; Remya, C.; Cerezo, J.; Fassihi, A.; Perez-Sanchez, H.; Sadasivan, C.
Comparative studies on the inhibitory activities of selected benzoic acid derivatives against secretory phospholipase A2, a key enzyme involved in the inflammatory pathway
Mol. Biosyst.
11
1973-1979
2015
Sus scrofa (P00592)
Manually annotated by BRENDA team