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Information on EC 3.1.1.4 - phospholipase A2 and Organism(s) Gallus gallus

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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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This record set is specific for:
Gallus gallus
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The taxonomic range for the selected organisms is: Gallus gallus
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
-
-
-
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Basic protein I/II
-
-
-
-
BJ-PLA2
-
-
-
-
BJUPLA2
-
-
-
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BPI/BPII
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-
-
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CaI-PLA2
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-
-
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Caudoxin
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-
-
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cPm09
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-
-
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Enhancing factor
-
-
-
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GIIC sPLA2
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-
-
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GIID sPLA2
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-
-
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GIIE sPLA2
-
-
-
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GIIF sPLA2
-
-
-
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GIII sPLA2
-
-
-
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Group IB phospholipase A2
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-
-
-
group IB PLA2
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-
Group IIA phospholipase A2
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-
-
-
Group V phospholipase A2
-
-
-
-
Group VI phospholipase A2
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-
-
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GVI PLA2
-
-
-
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GX sPLA2
-
-
-
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GXII sPLA2
-
-
-
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GXIII sPLA2
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-
-
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iPLA2
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-
-
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lecithinase A
-
-
-
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MP-III 4R
-
-
-
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Muscarinic inhibitor
-
-
-
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Myotoxin
-
-
-
-
NAJPLA-2A
-
-
-
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NAJPLA-2B
-
-
-
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NAJPLA-2C
-
-
-
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Nigexine
-
-
-
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Non-pancreatic secretory phospholipase A2
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-
-
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Notechis 11'2
-
-
-
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Notexin
-
-
-
-
NPLA
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-
-
-
NPS-PLA2
-
-
-
-
OHV A-PLA2
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-
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OHV-APLA2
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-
-
-
peroxiredoxin 6
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pgPLA 1a/pgPLA 2a
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-
-
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phosphatidase
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-
-
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phosphatide 2-acylhydrolase
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-
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phosphatidolipase
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-
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Phosphatidylcholine 2-acylhydrolase
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-
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Phosphatidylcholine 2-acylhydrolase GIIC
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Phosphatidylcholine 2-acylhydrolase GIID
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Phosphatidylcholine 2-acylhydrolase GIIE
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-
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Phosphatidylcholine 2-acylhydrolase GIIF
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-
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Phosphatidylcholine 2-acylhydrolase GIII
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-
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Phosphatidylcholine 2-acylhydrolase GX
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-
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Phosphatidylcholine 2-acylhydrolase GXII
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-
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Phosphatidylcholine 2-acylhydrolase GXIII
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-
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phospholipase A
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-
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phospholipase A2
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Phospholipase A2 inhibitor
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-
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pkP5
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-
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PLA2-10
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-
-
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PLA2-VI
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-
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PLA2-VII
-
-
-
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PLA2IID
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-
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platelet activating factor acetyl hydrolase
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-
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Pt-PLA1
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-
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Pt-PLA2
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-
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secretory phospholipase A2
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Secretory-type PLA, stroma-associated homolog
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-
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sPLA(2)-IID
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-
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sPLA(2)-IIE
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-
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sPLA(2)-IIF
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-
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sPLA2
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TMV-K49
-
-
-
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Toxin VI
-
-
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Toxin VI:5
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of carboxylic ester
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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
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,2-dipalmitoyl-sn-phosphatidylcholine + H2O
1-palmitoyl-sn-phosphatidylcholine + palmitate
show the reaction diagram
the catalytic site for aiPLA2 activity is an S32-H26-D140 triad
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-
?
1-palmitoyl-2-linoleoyl-sn-glycerophosphorylethanolamine + H2O
1-palmitoyl-glycerophosphorylethanolamine + linoleic acid
show the reaction diagram
-
-
-
-
?
phosphatidylcholine + H2O
1-acylglycerophosphocholine + a carboxylate
show the reaction diagram
-
in the presence of substrate, the enzyme binds to the interface as an active form. This crucial step is mediated by a planar surface region of the protein. The corresponding hydrophobic surface involves hydrophobic residues (Leu2, Trp3, Phe19, Leu20, Leu31, Ile64, Leu65, Tyr69, Ile72, Tyr75, and Leu118), hydrophobic surface involved in lipid binding increases
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
essential for both catalysis and enzyme binding to the substrate. The catalytic Ca2+ may be coordinated in a tetrahedral environment formed by the oxygen atoms of Tyr28, Gly30, Gly32 and Asp49. Second Ca2+-binding site is conserved and is formed by four residues: Glu71, Ile72, Asn89, and Glu92. Optimal Ca2+ concentration is about 4 mM
additional information
Ca2+-independent enzyme
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
diethyl 4-nitrophenyl phosphate
-
additional information
no inhibition by bromoenol lactone
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
sodium taurodeoxycholate
-
maximum phospholipase activity at 1 mm sodium taurodeoxycholate. Displays 50% of its maximum activity in the absence of bile salt dependent
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.2
-
extraction at pH 8.5, in 10 mM Tris/HCl buffer, 10 mM CaCl2, 0.15 M NaCl
400
-
2000fold purified enzyme, at pH 9.5, 37°C, in the presence of 1 mM sodium taurodeoxycholate, 4 mM CaCl2 with phosphatidylcholine as substrate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9.5
-
with phosphatidylcholine as substrate in the presence of 4 mM Ca2+ and 1 mM sodium taurodeoxycholate
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 9.5
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-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
with phosphatidylcholine as substrate in the presence of 4 mM Ca2+ and 1 mM sodium taurodeoxycholate
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37 - 40
-
loses ca. 80% of its activity after 20 min of incubation at 40°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
mesenchymal cell
Manually annotated by BRENDA team
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_CHICK
224
0
24977
Swiss-Prot
other Location (Reliability: 1)
PA24A_CHICK
748
0
84979
Swiss-Prot
other Location (Reliability: 2)
E1C9K4_CHICK
158
1
17973
TrEMBL
Secretory Pathway (Reliability: 4)
F1N9G3_CHICK
111
0
12117
TrEMBL
other Location (Reliability: 2)
E1C202_CHICK
158
0
17751
TrEMBL
Secretory Pathway (Reliability: 2)
H8Y6B1_CHICK
138
1
15756
TrEMBL
Secretory Pathway (Reliability: 1)
H8Y6B2_CHICK
144
0
15985
TrEMBL
Secretory Pathway (Reliability: 2)
A0A1I7Q3Z2_CHICK
789
0
89806
TrEMBL
other Location (Reliability: 2)
D6NKG5_CHICK
141
1
15426
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1D5PS91_CHICK
711
0
80807
TrEMBL
other Location (Reliability: 1)
A0A3S5ZPL6_CHICK
141
1
15420
TrEMBL
Secretory Pathway (Reliability: 1)
F1NFV7_CHICK
1145
0
127314
TrEMBL
other Location (Reliability: 2)
F1N9G4_CHICK
148
0
16565
TrEMBL
Secretory Pathway (Reliability: 2)
B8QN52_CHICK
148
1
16579
TrEMBL
Secretory Pathway (Reliability: 2)
R4GGW5_CHICK
867
0
99713
TrEMBL
other Location (Reliability: 1)
R4GHN4_CHICK
812
0
92991
TrEMBL
other Location (Reliability: 5)
B3TZB9_CHICK
796
0
88396
TrEMBL
Mitochondrion (Reliability: 4)
F1NBV7_CHICK
796
0
88394
TrEMBL
Mitochondrion (Reliability: 4)
D6NKG6_CHICK
155
0
17631
TrEMBL
Secretory Pathway (Reliability: 2)
A0A1D5PBK8_CHICK
895
0
102210
TrEMBL
Mitochondrion (Reliability: 3)
A0A3Q2TS24_CHICK
746
0
83245
TrEMBL
Mitochondrion (Reliability: 4)
A0A1D5NTC1_CHICK
742
0
84283
TrEMBL
other Location (Reliability: 2)
E1BWG9_CHICK
815
0
94579
TrEMBL
other Location (Reliability: 5)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
14000
-
gel filtration
14170
-
calculated from sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
non-glycosylated protein, SDS-PAGE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
-
is inactivated after incubation for 30 min at pH values lower than 4
708480
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by ammonium sulfate and ethanol precipitation, followed by gel filtration and gel filtration, to homogeneity, with a yield of 16%, 2000fold
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
ligated into PCR-Blunt vector and transformed into Escherichia coli DH5alpha cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
secretion of sPLA2 during limb development
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Choi, Y.A.; Kim, D.K.; Bang, O.S.; Kang, S.S.; Jin, E.J.
Secretory phospholipase A2 promotes MMP-9-mediated cell death by degrading type I collagen via the ERK pathway at an early stage of chondrogenesis
Biol. Cell
102
107-119
2010
Gallus gallus
Manually annotated by BRENDA team
Karray, A.; Frikha, F.; Ben Bacha, A.; Ben Ali, Y.; Gargouri, Y.; Bezzine, S.
Biochemical and molecular characterization of purified chicken pancreatic phospholipase A2
FEBS J.
276
4545-4554
2009
Gallus gallus
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team