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Information on EC 3.1.1.4 - phospholipase A2 and Organism(s) Bothrops asper and UniProt Accession P20474

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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:
Bothrops asper
UNIPROT: P20474
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The taxonomic range for the selected organisms is: Bothrops asper
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
phospholipase A2
-
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
-
-
-
-
myotoxin I
-
-
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
-
-
-
-
additional information
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
egg yolk phospholipid + H2O
?
show the reaction diagram
-
-
-
?
sn-3-phosphatidylcholine + 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
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Calcineurin
required for CTX myotoxic and neurotoxic activity, overview
-
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.9
2D electrophoresis
5.05
sequence analysis
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
acidic PLA2-II, in contrast to the basic Asp49 counterparts present in the same venom, lacks myotoxic, cytotoxic, and anticoagulant activities. It does not show hypotensive and anti-platelet aggregation activities and is not lethal to mice at intravenous doses up to 100 microg (5.9 microg/g), indicating its lack of neurotoxic activity. It shows a moderate induction of local edema in vivo. Acidic PLA2-II does not play a key role in the pathophysiology of envenomings, its purpose may be restricted to digestive functions. Acidic and basic PLA2s form two different antigenic groups in venom
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PA2B3_BOTAS
138
0
15751
Swiss-Prot
Secretory Pathway (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
14180
sequence analysis
14210
electrospray ionization
15000
1 * 15000, SDS-PAGE, 1 * 16000, SDS-PAGE, both under reducing and non-reducing conditions
16000
1 * 15000, SDS-PAGE, 1 * 16000, SDS-PAGE, both under reducing and non-reducing conditions
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 15000, SDS-PAGE, 1 * 16000, SDS-PAGE, both under reducing and non-reducing conditions
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cDNA cloned into the pGEM-T vector and transformed into Escherichia coli strain DH5alpha
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
C-terminal region of enzyme has bactericidal activity. Modulation of synthetic peptides based on the enzymic sequence, which have high bactericidal and endotoxin-neutralizing activity
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Santamaria, C.; Larios, S.; Angulo, Y.; Pizarro-Cerda, J.; Gorvel, J.P.; Moreno, E.; Lomonte, B.
Antimicrobial activity of myotoxic phospholipases A2 from crotalid snake venoms and synthetic peptide variants derived from their C-terminal region
Toxicon
45
807-815
2005
Bothrops asper
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
Miyabara, E.H.; Baptista, I.L.; Lomonte, B.; Selistre-de-Araujo, H.S.; Gutierrez, J.M.; Moriscot, A.S.
Effect of calcineurin inhibitors on myotoxic activity of crotoxin and Bothrops asper phospholipase A2 myotoxins in vivo and in vitro
Comp. Biochem. Physiol. C
143
284-294
2006
Bothrops asper (P20474), Bothrops asper
Manually annotated by BRENDA team
Fernandez, J.; Gutierrez, J.M.; Angulo, Y.; Sanz, L.; Juarez, P.; Calvete, J.J.; Lomonte, B.
Isolation of an acidic phospholipase A2 from the venom of the snake Bothrops asper of Costa Rica: biochemical and toxicological characterization
Biochimie
92
273-283
2010
Bothrops asper (P20474), Bothrops asper
Manually annotated by BRENDA team