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Information on EC 3.1.1.4 - phospholipase A2 and Organism(s) Oryza sativa and UniProt Accession Q9XG81

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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:
Oryza sativa
UNIPROT: Q9XG81
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Word Map
The taxonomic range for the selected organisms is: Oryza sativa
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
class XIB phospholipase A2
-
14 kDa phospholipase A2
-
-
-
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Agkistrotoxin
-
-
-
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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
-
-
-
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Ca2+-independent iPLA2
-
-
CaI-PLA2
-
-
-
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Caudoxin
-
-
-
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cPm09
-
-
-
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cytosolic cPLA2
-
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Enhancing factor
-
-
-
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GIIC sPLA2
-
-
-
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GIID sPLA2
-
-
-
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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 IIA phospholipase A2
-
-
-
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Group V phospholipase A2
-
-
-
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Group VI phospholipase A2
-
-
-
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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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iPLA2
-
-
-
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lecithinase A
-
-
-
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MP-III 4R
-
-
-
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Muscarinic inhibitor
-
-
-
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Myotoxin
-
-
-
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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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Notechis 11'2
-
-
-
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Notexin
-
-
-
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NPLA
-
-
-
-
NPS-PLA2
-
-
-
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OHV A-PLA2
-
-
-
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OHV-APLA2
-
-
-
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pgPLA 1a/pgPLA 2a
-
-
-
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phosphatidase
-
-
-
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phosphatide 2-acylhydrolase
-
-
-
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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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-
-
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Phosphatidylcholine 2-acylhydrolase GIID
-
-
-
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Phosphatidylcholine 2-acylhydrolase GIIE
-
-
-
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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 inhibitor
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-
-
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pkP5
-
-
-
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PLA2
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PLA2-10
-
-
-
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PLA2-I
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PLA2-VI
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-
-
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PLA2-VII
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-
-
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PLA2IID
-
-
-
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platelet activating factor acetyl hydrolase
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-
-
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Pt-PLA1
-
-
-
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Pt-PLA2
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-
-
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secreted sPLA2
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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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TMV-K49
-
-
-
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Toxin VI
-
-
-
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Toxin VI:5
-
-
-
-
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
1-palmitoyl-2-oleoylglycerophosphocholine + H2O
?
show the reaction diagram
-
-
-
?
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
-
-
?
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
?
-
-
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 hide
LITERATURE
Ca2+
Ca2+-binding loop
Ca2+
-
required by sPLA2
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
33
construct A (Leu-1 mutated to an alanine) and construct B (extra glycine inserted between the start methionine and Leu-1)
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
green shoot, PLA2-I and PLA2-II
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
PLA2-I and PLA2-II
-
Manually annotated by BRENDA team
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
isoform 2 phospholipase A2, by the sitting drop, vapor-diffusion method, to 2.0 A resolution. The N-terminal half of the chain contains mainly loop structure, including the conserved Ca2+-binding loop, but starts with a short 3(10)-helix and also includes two short anti-parallel beta-strands. The C-terminal half is folded into three anti-parallel alpha-helices, of which the two first contain the conserved catalytic histidine and calcium liganding aspartate residues. The structure is stabilized by six disulfide bonds. The water structure around the calcium ion binding site suggests the involvement of a second water molecule in the mechanism for hydrolysis, the water-assisted calcium-coordinate oxyanion mechanism. The octanoate molecule in the complex structure is bound in a hydrophobic pocket, which extends to the likely membrane interface and is proposed to model the binding of the product fatty acid
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by centrifugation, sonication and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cDNA coding for the predicted mature PLA2 protein, amino acids 1-128 without the signal peptide, designed with optimized codons for high level expression in Escherichia coli strain Tuner (DE3) LacI
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Guy, J.E.; Stahl, U.; Lindqvist, Y.
Crystal structure of a class XIB phospholipase A2 (PLA2): rice (oryza sativa) isoform-2 pla2 and an octanoate complex
J. Biol. Chem.
284
19371-19379
2009
Oryza sativa (Q9XG81), Oryza sativa
Manually annotated by BRENDA team