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Literature summary for 3.1.1.4 extracted from

  • Morrison, K.; Witte, K.; Mayers, J.R.; Schuh, A.L.; Audhya, A.
    Roles of acidic phospholipids and nucleotides in regulating membrane binding and activity of a calcium-independent phospholipase A2 isoform (2012), J. Biol. Chem., 287, 38824-38834.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
ADP stimulation, presence promotes oligomerisation of enzyme Caenorhabditis elegans
ATP addition of ATP and ADP promote oligomerization of the isozyme, which probably underlies the stimulatory effect of nucleotides on its activity. ATP hydrolysis is not required to promote isozyme IPLA-1 lipase activity in vitro Caenorhabditis elegans
ATP stimulation, presence promotes oligomerisation of enzyme. The effect of ATP becomes saturated at a concentration of 1mM, ATP hydrolysis is not required Caenorhabditis elegans
cardiolipin highly activating Caenorhabditis elegans
additional information neither ADP or a non-hydrolyzable analogue of ATP, AMP-PNP stimulates isozyme IPLA-1 Caenorhabditis elegans
additional information the enzyme binds directly to multiple acidic phospholipids Caenorhabditis elegans
phosphatidic acid highly activating Caenorhabditis elegans
phosphatidylglycerol highly activating Caenorhabditis elegans
phosphatidylserine highly activating Caenorhabditis elegans
Phospholipids IPLA-1 binds directly to multiple acidic phospholipids, including phosphatidylserine, phosphatidylglycerol, cardiolipin, phosphatidic acid, and phosphorylated derivatives of phosphatidylinositol. Presence of phospholipids in mixed micelles stimualtes activiy compared to micelles consisting of palmitoyl-sn-glycerophosphocholine Caenorhabditis elegans
phosphorylated phosphatidylinositol derivatives highly activating Caenorhabditis elegans

Cloned(Commentary)

Cloned (Comment) Organism
isozyme IPLA-1, expression of GST-fusion enzyme in Escherichia coli strain Rosetta2 (DE3) Caenorhabditis elegans

Inhibitors

Inhibitors Comment Organism Structure
bromoenol lactone strong inhibition Caenorhabditis elegans
methyl arachidonyl-fluorophosphonate
-
Caenorhabditis elegans

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
-
Caenorhabditis elegans 5737
-

Metals/Ions

Metals/Ions Comment Organism Structure
additional information activity is independent of Ca2+ Caenorhabditis elegans
additional information Ca2+-independent phospholipase A2 isoform, no effect by Mg2+ on enzyme activity or stability Caenorhabditis elegans

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
native isozyme IPLA-1 exhibits a Stokes radius of 6.2 nm similar to recombinant isozyme IPLA-1. Presence of ATP increases the experimental masses of the enzyme complexes to 430 and 250 kDa, which correspond to homopentameric and homotrimeric complexes, respectively Caenorhabditis elegans
87000
-
and dimer, 4 * 87000, calculated. Tetrameric complexes semm to be less stable and to disasemble over time Caenorhabditis elegans
87000
-
and tetramer, 2 * 87000, calculated Caenorhabditis elegans
180000
-
sedimentation velocity centrifugation Caenorhabditis elegans
190000
-
and 350000, gel filtration Caenorhabditis elegans
350000
-
and 190000, gel filtration Caenorhabditis elegans

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
phosphatidylcholine + H2O Caenorhabditis elegans
-
1-acylglycerophosphocholine + a carboxylate
-
?

Organism

Organism UniProt Comment Textmining
Caenorhabditis elegans
-
-
-
Caenorhabditis elegans
-
calcium-independent phospholipase A2 isoform, IPLA-1
-

Purification (Commentary)

Purification (Comment) Organism
-
Caenorhabditis elegans
recombinant GST-tagged isozyme IPLA-1 from Escherichia coli strain Rosetta2 (DE3) by glutathione affinity chromatography and gel filtration Caenorhabditis elegans

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.847
-
pH 7.5, 40°C Caenorhabditis elegans
0.847
-
pH 7.5, 40°C, recombinant enzyme Caenorhabditis elegans

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1,2-dipalmitoyl-sn-glycero-3-phosphorylcholine + H2O
-
Caenorhabditis elegans 1-palmitoyl-sn-glycero-3-phosphorylcholine + palmitic acid
-
?
1-palmitoyl-2-palmitoyl-sn-glycerophosphocholine + H2O
-
Caenorhabditis elegans 1-palmitoyl-sn-glycerophosphocholine + palmitate
-
?
phosphatidylcholine + H2O
-
Caenorhabditis elegans 1-acylglycerophosphocholine + a carboxylate
-
?

Subunits

Subunits Comment Organism
dimer and tetramer, 2 * 87000, calculated Caenorhabditis elegans
homotetramer gel filtration, SDS-PAGE, and sequence calculation Caenorhabditis elegans
More presence of ATP increases the experimental masses of the enzyme complexes to 430 and 250 kDa, which correspond to homopentameric and homotrimeric complexes, respectively Caenorhabditis elegans
tetramer and dimer, 4 * 87000, calculated. Tetrameric complexes semm to be less stable and to disasemble over time Caenorhabditis elegans

Synonyms

Synonyms Comment Organism
Ca2+-independent phospholipase A2
-
Caenorhabditis elegans
calcium-independent phospholipase A2
-
Caenorhabditis elegans
group VIA phospholipase A2
-
Caenorhabditis elegans
GVIA-iPLA2
-
Caenorhabditis elegans
IPLA-1
-
Caenorhabditis elegans
iPLA2
-
Caenorhabditis elegans

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
40
-
assay at Caenorhabditis elegans

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Caenorhabditis elegans

General Information

General Information Comment Organism
evolution the enzyme harbors a consensus motif common to members of the GVIA-iPLA2 subfamily, the group VIA phospholipase A2 (GVIA-iPLA2) subfamily of enzymes functions independently of calcium within the cytoplasm of cells. The Caenorhabditis elegans genome encodes multiple putative GVIAiPLA2 isoforms Caenorhabditis elegans
additional information isozyme IPLA-1 harbor numerous ankyrin repeats Caenorhabditis elegans
physiological function phospholipase A2 activity plays key roles in generating lipid second messengers and regulates membrane topology through the generation of asymmetric lysophospholipids. The Group VIA phospholipase A2 (GVIA-iPLA2) subfamily of enzymes is implicated in numerous cellular processes, including proliferation, apoptosis, and membrane transport steps. Role for acidic phospholipids in regulating GVIA-iPLA2 function. Membrane composition and the presence of nucleotides play key roles in recruiting and modulating the isozyme activity in cells Caenorhabditis elegans