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Information on EC 3.1.1.4 - phospholipase A2 and Organism(s) Bos taurus
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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: Bos taurus
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
PLA2-10
-
-
-
-
PLA2-VI
-
-
-
-
PLA2-VII
-
-
-
-
PLA2IID
-
-
-
-
platelet activating factor acetyl hydrolase
-
-
-
-
Pt-PLA1
-
-
-
-
Pt-PLA2
-
-
-
-
Secretory-type PLA, stroma-associated homolog
-
-
-
-
sPLA(2)-IID
-
-
-
-
sPLA(2)-IIE
-
-
-
-
sPLA(2)-IIF
-
-
-
-
TMV-K49
-
-
-
-
Toxin VI
-
-
-
-
Toxin VI:5
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of carboxylic ester
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
phosphatidylcholine 2-acylhydrolase
Also acts on phosphatidylethanolamine, choline plasmalogen and phosphatides, removing the fatty acid attached to the 2-position. Requires Ca2+.
CAS REGISTRY NUMBER
COMMENTARY
9001-84-7
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,2-diheptanoyl-sn-glycero-3-phophorylcholine + H2O
1-heptanoyl-sn-glycero-3-phophorylcholine + heptanoate
-
-
-
?
1,2-dioctanoyl-sn-glycero-3-phosphocholine + H2O
1-octanoyl-sn-glycero-3-phosphocholine + octanoate
-
-
-
?
1,2-dipalmitoyl-phosphatidylcholine + H2O
1-palmitoyl-glycerophosphorylcholine + palmitic acid
-
-
-
?
1,2-dipalmitoyl-sn-glycero-3-phosphocholine + H2O
1-palmitoyl-sn-glycero-3-phosphocholine + palmitic acid
-
-
-
?
1,2-dipalmitoyl-sn-phosphatidylcholine + H2O
1-palmitoyl-sn-phosphatidylcholine + palmitate
the catalytic site for aiPLA2 activity is an S32-H26-D140 triad
-
-
?
1-O-hexadecyl-2-arachidonyl-glycero-3-phosphocholine + H2O
1-O-hexadecyl-glycero-3-phosphocholine + arachidonic acid
-
-
-
?
1-palmitoyl-2-arachidonoylphosphatidylcholine + H2O
1-palmitoyl-glycerophosphorylcholine + arachidonic acid
1-palmitoyl-2-linoleoyl-sn-glycero-3-phosphocholine + H2O
1-palmitoyl-sn-glycero-3-phosphocholine + linolic acid
-
-
-
?
1-palmitoyl-2-oleoylphosphatidylcholine + H2O
1-palmitoyl-glycerophosphocholine + oleic acid
-
-
-
?
1-stearoyl-2-arachidonoyl-sn-glycero-3-phosphocholine + H2O
1-stearoyl-sn-glycero-3-phosphocholine + arachidonic acid
1-stearoyl-2-arachidonoyl-sn-glycero-3-phosphoethanolamine + H2O
1-stearoyl-sn-glycero-3-phosphoethanolamine + arachidonic acid
-
-
-
?
1-stearoyl-2-arachidonoyl-sn-glycero-3-phosphoinositol + H2O
1-stearoyl-sn-glycero-3-phosphoinositol + arachidonic 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
-
-
?
oxidized phosphatidylcholines + H2O
1-acylglycerophosphocholine + oxidized fatty acids
-
oxidized 1-palmitoyl-2-arachidonoylphosphatidylcholine for substrate
-
?
1-palmitoyl-2-arachidonoylphosphatidylcholine + H2O
1-palmitoyl-glycerophosphorylcholine + arachidonic acid
-
-
-
?
1-palmitoyl-2-arachidonoylphosphatidylcholine + H2O
1-palmitoyl-glycerophosphorylcholine + arachidonic acid
-
-
-
?
1-stearoyl-2-arachidonoyl-sn-glycero-3-phosphocholine + H2O
1-stearoyl-sn-glycero-3-phosphocholine + arachidonic acid
-
preferred substrate
-
?
1-stearoyl-2-arachidonoyl-sn-glycero-3-phosphocholine + H2O
1-stearoyl-sn-glycero-3-phosphocholine + arachidonic acid
-
good substrate
-
?
phospholipids + H2O
?
-
release of arachidonic acid: biosynthesis of leucotrienes, thromboxans and prostaglandins
-
-
?
additional information
?
-
-
enzyme is responsible for Ca2+-dependent release of arachidonic acid from red blood cells
-
?
additional information
?
-
-
preference of substrates in decreasing order: phosphatidylglycerols, phosphatidylethanolamines, phosphatidylcholines, phosphatidic acids
-
-
?
additional information
?
-
phospholipase A2 hydrolyzes phospholipids at the sn-2 position to cleave the fatty-acid ester bond of L-glycerophospholipids. The catalytic dyad, formed by residues Asp99 and His48, along with a nucleophilic water molecule is responsible for enzyme hydrolysis
-
-
?
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
?
-
-
the lysosomal isozyme PLA2 contains a Ser-His-Asp catalytic triad
-
-
?
additional information
?
-
the secretory isozyme has a catalytic dyad formed by Asp99 and His48
-
-
?
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
phospholipids + H2O
?
-
release of arachidonic acid: biosynthesis of leucotrienes, thromboxans and prostaglandins
-
-
?
additional information
?
-
-
enzyme is responsible for Ca2+-dependent release of arachidonic acid from red blood cells
-
?
additional information
?
-
phospholipase A2 hydrolyzes phospholipids at the sn-2 position to cleave the fatty-acid ester bond of L-glycerophospholipids. The catalytic dyad, formed by residues Asp99 and His48, along with a nucleophilic water molecule is responsible for enzyme hydrolysis
-
-
?
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+
-
two Ca2+ binding sites, first Ca2+ is strongly bound and essential for enzyme activity, the second binds more weakly and improves the enzymes affinity for lipid-water interfaces
Ca2+
residue Asp49 in the calcium-binding loop is essential for controlling binding of the calcium ion and catalytic action of phospholipase A2
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-hexadecyl-3-trifluoroethylglycero-sn-2-phosphomethanol
-
MJ33, competitive inhibitor
acalyphin
from Acalypha indica, shows interaction with the amino acids at the active site of PLA2, interacts also with the Ca2+ ion in the active site of PLA2
aplysulphurin A
from Aplysilla sp., shows interaction with the amino acids at the active site of PLA2, interacts also with the Ca2+ ion in the active site of PLA2
chlorogenic acid
from Achillea millefolium, shows interaction with the amino acids at the active site of PLA2
curcumin
from Curcuma longa, shows interaction with the amino acids at the active site of PLA2
gracilin A
from Aplysilla sp., shows interaction with the amino acids at the active site of PLA2, interacts also with the Ca2+ ion in the active site of PLA2
stigmasterol
from Achillea millefolium, shows interaction with the amino acids at the active site of PLA2
tectoridin
from Belamcanda chinensis, shows interaction with the amino acids at the active site of PLA2
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.4
1,2-diheptanoyl-sn-glycero-3-phophorylcholine
-
micellar substrate, enzyme saturated with Ca2+
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0000115
-
particulate associated hormonally regulated PLA2, substrate: 1-palmitoyl-2-arachidonylphosphatidylcholine, mixed micelles with Triton X-100
0.0000538
-
particulate associated hormonally regulated PLA2, substrate: micellar 1-palmitoyl-2-arachidonylphosphatidylcholine
0.027
-
acidic iPLA2, substrate: 1-O-hexadecyl-2-arachidonoyl-glycero-3-phosphocholine
0.064
-
acidic iPLA2, substrate: 1-palmitoyl-2-arachidonylphosphatidylcholine or 1,2-dipalmitoyl-phosphatidylcholine
0.065
-
acidic iPLA2, substrate: oxidized 1-palmitoyl-2-arachidonylphosphatidylcholine
0.08
-
acidic iPLA2, pH 4.0, Ca2+-free medium, substrate: 1,2-dipalmitoyl-phosphatidylcholine
additional information
-
synthesis of fluorogenic substrate analogues for rapid determination of head group modification on cell signaling
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
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
-
binding of the GIVA PLA2 to the membrane is mediated through three mechanisms: Ca2+ mediated translocation, binding of secondary lipid messengers, and phosphorylation
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
the enzyme has important physiological roles in the turnover (synthesis and degradation) of lung surfactant phospholipids, in the repair of peroxidized cell membranes, and in the activation of NADPH oxidase type 2
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). PRDX6_BOVIN
224
0
25067
Swiss-Prot
other Location (Reliability: 1)
PA2G3_BOVIN
501
0
55376
Swiss-Prot
Secretory Pathway (Reliability: 2)
PA2GA_BOVIN
144
1
16347
Swiss-Prot
Secretory Pathway (Reliability: 1)
PA21B_BOVIN
145
0
16002
Swiss-Prot
Secretory Pathway (Reliability: 3)
ABHD3_BOVIN
411
1
46527
Swiss-Prot
Mitochondrion (Reliability: 5)
PLPL2_BOVIN
486
1
53417
Swiss-Prot
Secretory Pathway (Reliability: 4)
PA24A_BOVIN
749
0
85350
Swiss-Prot
other Location (Reliability: 2)
PAG15_BOVIN
407
0
46062
Swiss-Prot
Secretory Pathway (Reliability: 1)
Q5W1P1_BOVIN
147
0
16669
TrEMBL
Secretory Pathway (Reliability: 1)
A0A3Q1MII9_BOVIN
147
0
16445
TrEMBL
other Location (Reliability: 1)
F1MNU5_BOVIN
845
0
94348
TrEMBL
Secretory Pathway (Reliability: 5)
Q3T154_BOVIN
147
0
16685
TrEMBL
Secretory Pathway (Reliability: 1)
A0A3Q1N0U8_BOVIN
204
0
23273
TrEMBL
Secretory Pathway (Reliability: 5)
F1MQ77_BOVIN
147
0
16578
TrEMBL
other Location (Reliability: 1)
F1MN86_BOVIN
151
0
16866
TrEMBL
Secretory Pathway (Reliability: 3)
F1MRH1_BOVIN
1136
0
127432
TrEMBL
Secretory Pathway (Reliability: 5)
Q0IIC8_BOVIN
144
1
16225
TrEMBL
Secretory Pathway (Reliability: 1)
A0A3Q1MFE1_BOVIN
197
0
22043
TrEMBL
other Location (Reliability: 2)
F1MFC1_BOVIN
821
0
93976
TrEMBL
Secretory Pathway (Reliability: 5)
A0A3Q1MNU5_BOVIN
204
0
23212
TrEMBL
Secretory Pathway (Reliability: 5)
Q5W1P0_BOVIN
147
0
16655
TrEMBL
Secretory Pathway (Reliability: 1)
E1BLF3_BOVIN
144
1
16346
TrEMBL
Secretory Pathway (Reliability: 1)
E1BGU4_BOVIN
159
0
17572
TrEMBL
Secretory Pathway (Reliability: 2)
Q5W1N8_BOVIN
147
0
16592
TrEMBL
other Location (Reliability: 1)
A0A3Q1LRP1_BOVIN
740
0
84261
TrEMBL
other Location (Reliability: 2)
A0A3Q1LV96_BOVIN
1108
0
123669
TrEMBL
Secretory Pathway (Reliability: 3)
Q5W1P3_BOVIN
133
0
15241
TrEMBL
other Location (Reliability: 1)
Q5W1N7_BOVIN
45
0
5416
TrEMBL
other Location (Reliability: 1)
A0A3Q1M6Q8_BOVIN
146
1
16493
TrEMBL
Secretory Pathway (Reliability: 1)
Q5W1P4_BOVIN
147
0
16616
TrEMBL
Secretory Pathway (Reliability: 1)
Q5W1N9_BOVIN
59
0
6618
TrEMBL
other Location (Reliability: 2)
G3N3U6_BOVIN
222
1
24955
TrEMBL
other Location (Reliability: 2)
F1MSG5_BOVIN
142
1
16001
TrEMBL
Secretory Pathway (Reliability: 1)
A0A3Q1LKD5_BOVIN
158
1
18328
TrEMBL
Secretory Pathway (Reliability: 3)
A0A3Q1LNM7_BOVIN
196
0
21816
TrEMBL
other Location (Reliability: 3)
A0A3Q1LSJ6_BOVIN
158
0
17508
TrEMBL
Secretory Pathway (Reliability: 1)
A0A3Q1LRH9_BOVIN
145
0
16159
TrEMBL
Secretory Pathway (Reliability: 1)
A0A3Q1LYR5_BOVIN
836
0
95787
TrEMBL
other Location (Reliability: 4)
A5PJC6_BOVIN
144
0
16376
TrEMBL
Secretory Pathway (Reliability: 1)
E1BD09_BOVIN
804
0
92052
TrEMBL
other Location (Reliability: 5)
E1BB89_BOVIN
846
0
94046
TrEMBL
other Location (Reliability: 1)
F1MG30_BOVIN
816
0
91488
TrEMBL
Mitochondrion (Reliability: 5)
E1BEG8_BOVIN
138
0
15954
TrEMBL
Secretory Pathway (Reliability: 1)
E1B9V3_BOVIN
147
0
16556
TrEMBL
Secretory Pathway (Reliability: 1)
A0A3Q1MB03_BOVIN
147
0
16509
TrEMBL
other Location (Reliability: 1)
A0A3Q1M5P6_BOVIN
165
1
18533
TrEMBL
Secretory Pathway (Reliability: 3)
A0A3Q1LN87_BOVIN
793
0
88259
TrEMBL
other Location (Reliability: 1)
E1BC49_BOVIN
784
0
88348
TrEMBL
Secretory Pathway (Reliability: 4)
A6QLC2_BOVIN
196
0
21835
TrEMBL
other Location (Reliability: 3)
A0A3Q1M361_BOVIN
790
0
88047
TrEMBL
other Location (Reliability: 1)
A0A3Q1LR65_BOVIN
819
0
91852
TrEMBL
Secretory Pathway (Reliability: 4)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
wild-type and mutant structure analysis and comparison, molecular-dynamics simulation, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and mutant enzymes, 0.005 ml of 15 mg/ml protein in 50 mM Tris-HCl buffer, pH 7.2, and 5.0 mM CaCl2, is mixed with 0.002 ml of 50% v/v 2-methyl-2,4-pentanediol and equilibrated against 60% v/v 2-methyl-2,4-pentanediol in 0.5 ml reservoir solution, hanging drop vapour diffusion method at room temperature, X-ray diffraction structure determination and analysis at 1.9 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D49K
site-directed mutagenesis, the tertiary structures of the active site mutant is similar to that of the trigonal recombinant enzyme, but the mutant lacks a Ca2+ in the active site. Molecular-dynamics simulation, proton transfer is not possible from the catalytic water to the mutated residue
D49N
site-directed mutagenesis, the tertiary structures of the active site mutant is similar to that of the trigonal recombinant enzyme, but the mutant lacks a Ca2+ in the active site. Molecular-dynamics simulation, proton transfer is not possible from the catalytic water to the mutated residue
H48N
site-directed mutagenesis, the tertiary structures of the active site mutant is similar to that of the trigonal recombinant enzyme. Molecular-dynamics simulation, proton transfer is not possible from the catalytic water to the mutated residue
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
pharmacology
application of pancreatic phospholipase A2 for treatment of bovine mastitis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Akiba, S.; Dodia, C.; Chen, X.; Fisher, A.B.
Characterization of acidic Ca2+-independent phospholipase A2 of bovine lung
Comp. Biochem. Physiol. B
120
393-404
1998
Bos taurus, Homo sapiens
Yang, H.C.; Farooqui, A.A.; Horrocks, L.A.
Characterization of plasmalogen-selective phospholipase A2 from bovine brain
Adv. Exp. Med. Biol.
416
309-313
1996
Bos taurus, Homo sapiens
Hada, S.; Fujii, S.; Inoue, S.; Ikeda, K.; Teshima, K.
Hydrolysis of micellar diheptanoylphosphatidylcholine catalyzed by bovine pancreatic phospholipase A2: Kinetic characterization of group I and II enzymes
J. Biochem.
113
13-18
1993
Bos taurus
Paglin, S.; Roy, R.; Polgar, P.
Characterization of hormonally regulated and particulate-associated phospholipase A2 from bovine endothelial cells
J. Biol. Chem.
268
11697-11702
1993
Bos taurus
Hanasaki, K.; Arita, H.
Purification and characterization of a high-affinity binding protein for pancreatic-type phospholipase A2
Biochim. Biophys. Acta
1127
233-241
1992
Bos taurus
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
Shin, H.S.; Chin, M.R.; Kim, J.S.; Chung, J.H.; Ryu, C.K.; Jung, S.Y.; Kim, D.K.
Purification and characterization of a cytosolic, 42-kDa and Ca2+-dependent phospholipase A2 from bovine red blood cells: its involvement in Ca2+-dependent release of arachidonic acid from mammalian red blood cells
J. Biol. Chem.
277
21086-21094
2002
Bos taurus, Homo sapiens
Sekar, K.; Vaijayanthi Mala, S.; Yogavel, M.; Velmurugan, D.; Poi, M.J.; Vishwanath, B.S.; Gowda, T.V.; Jeyaprakash, A.A.; Tsai, M.D.
Crystal structures of the free and anisic acid bound triple mutant of phospholipase A2
J. Mol. Biol.
333
367-376
2003
Bos taurus (P00593), Bos taurus
Farooqui, A.A.; Ong, W.Y.; Horrocks, L.A.; Farooqui, T.
Brain cytosolic phospholipase A2: localization, role, and involvement in neurological diseases
Neuroscientist
6
169-180
2000
Bos taurus, Homo sapiens, Mammalia, Rattus norvegicus
-
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
Kanaujia, S.P.; Sekar, K.
Structures and molecular-dynamics studies of three active-site mutants of bovine pancreatic phospholipase A2
Acta Crystallogr. Sect. D
64
1003-1011
2008
Bos taurus (P00593)
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
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
Fisher, A.B.
The phospholipase A2 activity of peroxiredoxin 6
J. Lipid Res.
59
1132-1147
2018
Trematomus bernacchii, Xenopus tropicalis (B1WAZ6), Mus musculus (O08709), Rattus norvegicus (O35244), Bos taurus (O77834), Homo sapiens (P30041), Gallus gallus (Q5ZJF4), Arabidopsis thaliana (Q8S8N6)
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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