BRENDA - Enzyme Database

Roles of acidic phospholipids and nucleotides in regulating membrane binding and activity of a calcium-independent phospholipase A2 isoform

Morrison, K.; Witte, K.; Mayers, J.R.; Schuh, A.L.; Audhya, A.; J. Biol. Chem. 287, 38824-38834 (2012)

Data extracted from this reference:

Activating Compound
EC Number
Activating Compound
Commentary
Organism
Structure
3.1.1.4
ADP
stimulation, presence promotes oligomerisation of enzyme
Caenorhabditis elegans
3.1.1.4
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; stimulation, presence promotes oligomerisation of enzyme. The effect of ATP becomes saturated at a concentration of 1mM, ATP hydrolysis is not required
Caenorhabditis elegans
3.1.1.4
cardiolipin
highly activating
Caenorhabditis elegans
3.1.1.4
additional information
neither ADP or a non-hydrolyzable analogue of ATP, AMP-PNP stimulates isozyme IPLA-1; the enzyme binds directly to multiple acidic phospholipids
Caenorhabditis elegans
3.1.1.4
phosphatidic acid
highly activating
Caenorhabditis elegans
3.1.1.4
phosphatidylglycerol
highly activating
Caenorhabditis elegans
3.1.1.4
phosphatidylserine
highly activating
Caenorhabditis elegans
3.1.1.4
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
3.1.1.4
phosphorylated phosphatidylinositol derivatives
highly activating
Caenorhabditis elegans
Cloned(Commentary)
EC Number
Commentary
Organism
3.1.1.4
isozyme IPLA-1, expression of GST-fusion enzyme in Escherichia coli strain Rosetta2 (DE3)
Caenorhabditis elegans
Inhibitors
EC Number
Inhibitors
Commentary
Organism
Structure
3.1.1.4
bromoenol lactone
; strong inhibition
Caenorhabditis elegans
3.1.1.4
methyl arachidonyl-fluorophosphonate
-
Caenorhabditis elegans
Localization
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
3.1.1.4
cytoplasm
-
Caenorhabditis elegans
5737
-
Metals/Ions
EC Number
Metals/Ions
Commentary
Organism
Structure
3.1.1.4
additional information
activity is independent of Ca2+; Ca2+-independent phospholipase A2 isoform, no effect by Mg2+ on enzyme activity or stability
Caenorhabditis elegans
Molecular Weight [Da]
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
3.1.1.4
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
3.1.1.4
87000
-
and dimer, 4 * 87000, calculated. Tetrameric complexes semm to be less stable and to disasemble over time; and tetramer, 2 * 87000, calculated
Caenorhabditis elegans
3.1.1.4
180000
-
sedimentation velocity centrifugation
Caenorhabditis elegans
3.1.1.4
190000
-
and 350000, gel filtration
Caenorhabditis elegans
3.1.1.4
350000
-
and 190000, gel filtration
Caenorhabditis elegans
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
3.1.1.4
phosphatidylcholine + H2O
Caenorhabditis elegans
-
1-acylglycerophosphocholine + a carboxylate
-
-
?
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
3.1.1.4
Caenorhabditis elegans
-
; calcium-independent phospholipase A2 isoform, IPLA-1
-
Purification (Commentary)
EC Number
Commentary
Organism
3.1.1.4
; 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]
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
3.1.1.4
0.847
-
pH 7.5, 40°C; pH 7.5, 40°C, recombinant enzyme
Caenorhabditis elegans
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3.1.1.4
1,2-dipalmitoyl-sn-glycero-3-phosphorylcholine + H2O
-
729999
Caenorhabditis elegans
1-palmitoyl-sn-glycero-3-phosphorylcholine + palmitic acid
-
-
-
?
3.1.1.4
1-palmitoyl-2-palmitoyl-sn-glycerophosphocholine + H2O
-
729999
Caenorhabditis elegans
1-palmitoyl-sn-glycerophosphocholine + palmitate
-
-
-
?
3.1.1.4
phosphatidylcholine + H2O
-
729999
Caenorhabditis elegans
1-acylglycerophosphocholine + a carboxylate
-
-
-
?
Subunits
EC Number
Subunits
Commentary
Organism
3.1.1.4
dimer
and tetramer, 2 * 87000, calculated
Caenorhabditis elegans
3.1.1.4
homotetramer
gel filtration, SDS-PAGE, and sequence calculation
Caenorhabditis elegans
3.1.1.4
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
3.1.1.4
tetramer
and dimer, 4 * 87000, calculated. Tetrameric complexes semm to be less stable and to disasemble over time
Caenorhabditis elegans
Temperature Optimum [°C]
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
3.1.1.4
40
-
assay at
Caenorhabditis elegans
pH Optimum
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
3.1.1.4
7.5
-
assay at
Caenorhabditis elegans
Activating Compound (protein specific)
EC Number
Activating Compound
Commentary
Organism
Structure
3.1.1.4
ADP
stimulation, presence promotes oligomerisation of enzyme
Caenorhabditis elegans
3.1.1.4
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; stimulation, presence promotes oligomerisation of enzyme. The effect of ATP becomes saturated at a concentration of 1mM, ATP hydrolysis is not required
Caenorhabditis elegans
3.1.1.4
cardiolipin
highly activating
Caenorhabditis elegans
3.1.1.4
additional information
neither ADP or a non-hydrolyzable analogue of ATP, AMP-PNP stimulates isozyme IPLA-1; the enzyme binds directly to multiple acidic phospholipids
Caenorhabditis elegans
3.1.1.4
phosphatidic acid
highly activating
Caenorhabditis elegans
3.1.1.4
phosphatidylglycerol
highly activating
Caenorhabditis elegans
3.1.1.4
phosphatidylserine
highly activating
Caenorhabditis elegans
3.1.1.4
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
3.1.1.4
phosphorylated phosphatidylinositol derivatives
highly activating
Caenorhabditis elegans
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
3.1.1.4
isozyme IPLA-1, expression of GST-fusion enzyme in Escherichia coli strain Rosetta2 (DE3)
Caenorhabditis elegans
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
Organism
Structure
3.1.1.4
bromoenol lactone
; strong inhibition
Caenorhabditis elegans
3.1.1.4
methyl arachidonyl-fluorophosphonate
-
Caenorhabditis elegans
Localization (protein specific)
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
3.1.1.4
cytoplasm
-
Caenorhabditis elegans
5737
-
Metals/Ions (protein specific)
EC Number
Metals/Ions
Commentary
Organism
Structure
3.1.1.4
additional information
activity is independent of Ca2+; Ca2+-independent phospholipase A2 isoform, no effect by Mg2+ on enzyme activity or stability
Caenorhabditis elegans
Molecular Weight [Da] (protein specific)
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
3.1.1.4
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
3.1.1.4
87000
-
and dimer, 4 * 87000, calculated. Tetrameric complexes semm to be less stable and to disasemble over time; and tetramer, 2 * 87000, calculated
Caenorhabditis elegans
3.1.1.4
180000
-
sedimentation velocity centrifugation
Caenorhabditis elegans
3.1.1.4
190000
-
and 350000, gel filtration
Caenorhabditis elegans
3.1.1.4
350000
-
and 190000, gel filtration
Caenorhabditis elegans
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
3.1.1.4
phosphatidylcholine + H2O
Caenorhabditis elegans
-
1-acylglycerophosphocholine + a carboxylate
-
-
?
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
3.1.1.4
; 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] (protein specific)
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
3.1.1.4
0.847
-
pH 7.5, 40°C; pH 7.5, 40°C, recombinant enzyme
Caenorhabditis elegans
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3.1.1.4
1,2-dipalmitoyl-sn-glycero-3-phosphorylcholine + H2O
-
729999
Caenorhabditis elegans
1-palmitoyl-sn-glycero-3-phosphorylcholine + palmitic acid
-
-
-
?
3.1.1.4
1-palmitoyl-2-palmitoyl-sn-glycerophosphocholine + H2O
-
729999
Caenorhabditis elegans
1-palmitoyl-sn-glycerophosphocholine + palmitate
-
-
-
?
3.1.1.4
phosphatidylcholine + H2O
-
729999
Caenorhabditis elegans
1-acylglycerophosphocholine + a carboxylate
-
-
-
?
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
3.1.1.4
dimer
and tetramer, 2 * 87000, calculated
Caenorhabditis elegans
3.1.1.4
homotetramer
gel filtration, SDS-PAGE, and sequence calculation
Caenorhabditis elegans
3.1.1.4
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
3.1.1.4
tetramer
and dimer, 4 * 87000, calculated. Tetrameric complexes semm to be less stable and to disasemble over time
Caenorhabditis elegans
Temperature Optimum [°C] (protein specific)
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
3.1.1.4
40
-
assay at
Caenorhabditis elegans
pH Optimum (protein specific)
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
3.1.1.4
7.5
-
assay at
Caenorhabditis elegans
General Information
EC Number
General Information
Commentary
Organism
3.1.1.4
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
3.1.1.4
additional information
isozyme IPLA-1 harbor numerous ankyrin repeats
Caenorhabditis elegans
3.1.1.4
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
General Information (protein specific)
EC Number
General Information
Commentary
Organism
3.1.1.4
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
3.1.1.4
additional information
isozyme IPLA-1 harbor numerous ankyrin repeats
Caenorhabditis elegans
3.1.1.4
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