Information on EC 3.1.1.32 - phospholipase A1

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
3.1.1.32
-
RECOMMENDED NAME
GeneOntology No.
phospholipase A1
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
phosphatidylcholine + H2O = 2-acylglycerophosphocholine + a carboxylate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of carboxylic ester
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
alpha-Linolenic acid metabolism
-
-
Biosynthesis of secondary metabolites
-
-
Glycerophospholipid metabolism
-
-
Metabolic pathways
-
-
phosphatidylcholine acyl editing
-
-
phospholipases
-
-
SYSTEMATIC NAME
IUBMB Comments
phosphatidylcholine 1-acylhydrolase
This enzyme has a much broader specificity than EC 3.1.1.4 phospholipase A2. Requires Ca2+.
CAS REGISTRY NUMBER
COMMENTARY hide
9043-29-2
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain 168
-
-
Manually annotated by BRENDA team
strain 168
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
Corticium centrifugum
-
-
-
Manually annotated by BRENDA team
hornet
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain IMSS 0989
-
-
Manually annotated by BRENDA team
strain IMSS 0989
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
enzyme precursor
SwissProt
Manually annotated by BRENDA team
precursor; a social wasp
UniProt
Manually annotated by BRENDA team
strain 576 and 579
-
-
Manually annotated by BRENDA team
strain 576 and 579
-
-
Manually annotated by BRENDA team
isolate HFKI0020
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
strain NT-1
-
-
Manually annotated by BRENDA team
strain NT-1
-
-
Manually annotated by BRENDA team
strain 427, from BALB/c mouse bloodstream
UniProt
Manually annotated by BRENDA team
strain 427, from BALB/c mouse bloodstream
UniProt
Manually annotated by BRENDA team
4 isoforms, Ves a 1.01-1.04
-
-
Manually annotated by BRENDA team
black-bellied hornet
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
-
intracellular phospholipase A1 and acyltransferase are involved in Caenorhabditis elegans stem cell divisions
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1(3)-monoolein + H2O
?
show the reaction diagram
-
-
-
-
?
1,2-didocosahexaenoyl-phosphatidylcholine + H2O
2-docosahexaenoyl-lysophosphatidylcholine + docosahexaenoic acid
show the reaction diagram
-
19% of activity with 1-oleoyl-2-palmitoyl-phosphatidylcholine
-
?
1,2-dimyristoyl-sn-glycero-3-phosphate + H2O
?
show the reaction diagram
1,2-dimyristoyl-sn-glycero-3-phosphocholine + H2O
2-myristoyl-sn-glycero-3-phosphocholine + myristic acid
show the reaction diagram
1,2-dioctadecenoylthio-sn-glycero-3-phosphocholine + H2O
1-thio-2-octadecenoylthio-sn-glycero-3-phosphocholine + octadecenoate
show the reaction diagram
-
-
-
?
1,2-dioctadecenoylthio-sn-glycero-3-phosphoethanolamine + H2O
1-thio-2-octadecenoylthio-sn-glycero-3-phosphoethanolamine + octadecenoate
show the reaction diagram
-
-
-
?
1,2-dioctadecenoylthio-sn-glycero-3-phosphoglycerol + H2O
1-thio-2-octadecenoylthio-sn-glycero-3-phosphoglycerol + octadecenoate
show the reaction diagram
-
-
-
?
1,2-dioleoyl-sn-glycero-3-phosphoethanolamine + H2O
?
show the reaction diagram
1,2-dioleoylphosphatidylcholine + H2O
oleic acid + 2-oleoylglycerophosphocholine
show the reaction diagram
-
-
-
?
1,2-dipalmitoyl-phosphatidylcholine + H2O
2-palmitoyl-sn-glycerophosphocholine + palmitate
show the reaction diagram
substrate from Glycine max
-
-
?
1,2-dipalmitoyl-sn-glycero-3-phosphocholine + H2O
?
show the reaction diagram
1- palmitoyl-2-oleoyl-phosphatidylcholine + H2O
2-oleoyl-lysophosphatidylcholine + palmitic acid
show the reaction diagram
-
-
-
?
1-acyl-2-lysophosphatidylserine + H2O
sn-glycerol-phosphoserine + a carboxylate
show the reaction diagram
-
-
-
?
1-acyl-2-oleoyl-sn-glycerophosphocholine + H2O
acyl-glycerophosphocholine + oleic acid
show the reaction diagram
-
labeled at the sn-2 position with [14C]oleic acid
-
-
?
1-acyl-lysophosphtidic acid + H2O
glycerol-3-phosphate + a carboxylate
show the reaction diagram
-
7% of activity with phosphatidic acid
-
?
1-acyl-sn-glycero-3-phosphocholine + H2O
fatty acid + glycero-3-phosphocholine
show the reaction diagram
-
-
-
-
?
1-myristoyl 2-oleyl phosphatidylcholine + H2O
2-oleylglycerophosphocholine + myristoate
show the reaction diagram
-
-
-
-
1-oleoyl-2-palmitoyl-phosphatidylcholine + H2O
2-palmitoyl-lysophosphatidylcholine + oleic acid
show the reaction diagram
-
-
-
?
1-oleoyl-2-stearoyl-3-sn-glycerophosphorylcholine + H2O
?
show the reaction diagram
-
-
-
?
1-palmitoyl-2-arachidonoyl-glycero-3-phosphoethanolamine + H2O
2-arachidonoyl-lysophosphatidylethanolamine + H2O
show the reaction diagram
1-palmitoyl-2-arachidonoylglycerophosphocholine + H2O
palmitic acid + 2-arachidonoylglycerophosphocholine
show the reaction diagram
1-palmitoyl-2-docosahexaenoyl-phosphatidylcholine + H2O
2-docosahexaenoyl-lysophosphatidylcholine + palmitic acid
show the reaction diagram
-
-
-
?
1-palmitoyl-2-linoleoyl phosphatidylcholine + H2O
?
show the reaction diagram
-
the enzyme is responsible for about two-thirds of plasma 1-palmitoyl-2-linoleoyl phosphatidylcholine disappearance
-
-
-
1-palmitoyl-2-linoleoyl-phosphatidyl choline + H2O
2-linoleoyl-lysophosphatidyl choline + palmitic acid
show the reaction diagram
-
-
?
1-palmitoyl-2-linoleoyl-phosphorylcholine + H2O
palmitic acid + 2-linoleoyl-1-lysophosphoryl choline
show the reaction diagram
-
-
-
?
1-palmitoyl-2-linoleoyl-sn-3-glycerophosphorylethanolamine + H2O
palmitic acid + 2-linoleoyl-sn-3-glycerophosphorylethanolamine
show the reaction diagram
-
-
-
-
?
1-palmitoyl-2-linoleoylglycerophosphocholine + H2O
?
show the reaction diagram
1-palmitoyl-2-linoleoylphosphatidylethanolamine + H2O
?
show the reaction diagram
-
-
-
-
?
1-palmitoyl-2-oleoyl-phosphatidylcholine + H2O
2-oleoyl-lysophosphatidylcholine + palmitic acid
show the reaction diagram
-
-
-
?
1-palmitoyl-2-oleoylglycerophosphocholine + H2O
palmitic acid + 2-oleoylglycerophosphocholine
show the reaction diagram
1-palmitoyl-2-palmitoylglycerophosphocholine + H2O
palmitic acid + 2-palmitoylglycerophosphocholine
show the reaction diagram
-
-
-
-
?
1-palmitoyllysophosphatidylcholine + H2O
palmitic acid + lysophosphatidylcholine
show the reaction diagram
-
weak activity
-
-
?
1-stearoyl-2-arachidonoylglycerophosphocholine + H2O
stearic acid + 2-arachidonoylglycerophosphocholine
show the reaction diagram
1-stearoyl-2-arachidonoylglycerophosphoinositol + H2O
stearic acid + 2-arachidonoylglycerophosphoinositol
show the reaction diagram
1-stearoyl-2-arachidonyl-sn-glycero-3-phosphoinositol + H2O
2-arachidonylglycero-3-phosphoinositol + ?
show the reaction diagram
-
-
no release of free arachidonate
?
1-stearoyl-2-oleoyl-3-sn-glycerophosphorylcholine + H2O
?
show the reaction diagram
-
-
-
?
2-acyl-sn-glycero-3-phosphocholine + H2O
fatty acid + glycerophosphocholine
show the reaction diagram
-
-
-
-
?
2-hexadecanoylthio-ethane-1-phosphocholine + H2O
thio-ethane-1-phosphocholine + hexadecanoate
show the reaction diagram
-
-
-
?
2-monoolein + H2O
?
show the reaction diagram
-
-
-
-
?
2-oleoylphosphatidylcholine + H2O
oleic acid + glycerophosphocholine
show the reaction diagram
-
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
show the reaction diagram
-
-
-
?
cardiolipin + H2O
?
show the reaction diagram
-
-
-
-
?
diacyl-sn-glycero-3-phosphorylcholine + H2O
fatty acid + lysophosphatidylcholine
show the reaction diagram
-
-
-
-
?
diacyl-sn-glycero-3-phosphorylethanolamine + H2O
fatty acid + lysophosphatidylethanolamine
show the reaction diagram
-
-
-
-
?
diacyl-sn-glycero-3-phosphorylserine + H2O
fatty acid + lysophosphatidylserine
show the reaction diagram
-
-
-
-
?
diolein + H2O
?
show the reaction diagram
-
-
-
-
?
dipalmitoylphosphatidylcholine + H2O
?
show the reaction diagram
-
-
-
-
?
dipalmitoylphosphatidylcholine + H2O
palmitic acid + 1-lyso-2-palmitoylphosphatidylcholine
show the reaction diagram
hexadecanoylthioethane-1-phosphocholine + H2O
hexadecanoate + thioethane-1-phosphocholine
show the reaction diagram
-
-
-
?
high-density lipoprotein + H2O
fatty acid + ?
show the reaction diagram
-
-
-
-
?
L-alpha-phosphatidyl-L-serine + H2O
2-acyl-1-glycerophosphoserine + a carboxylate
show the reaction diagram
substrate from Glycine max
-
-
?
L-alpha-phosphatidylcholine + H2O
2-acyl-1-glycerophosphocholine + a carboxylate
show the reaction diagram
PLA1 activity for egg yolk lecithin hydrolysis, substrate from egg yolk or Glycine max
-
-
?
L-alpha-phosphatidylglycerol + H2O
?
show the reaction diagram
-
-
-
?
L-alpha-phosphatidylinositol + H2O
2-acyl-1-glycerophosphoinositol + a carboxylate
show the reaction diagram
-
-
-
?
lecithin + H2O
?
show the reaction diagram
from Glycine max
-
-
?
lysophosphatidylcholine + H2O
?
show the reaction diagram
weak substrate
-
-
-
monogalactosyldiacylglycerol + H2O
1-lyso-2-acyl-3-galactosyl-sn-glycerol + a fatty acid anion
show the reaction diagram
-
-
-
?
phosphatidic acid + H2O
2-acyl-lysophosphatidic acid + a carboxylate
show the reaction diagram
phosphatidic acid + H2O
2-acylglycerol-3-phosphate + a carboxylate
show the reaction diagram
-
-
-
?
phosphatidic acid + H2O
2-acylglycerophosphatidic acid + a carboxylate
show the reaction diagram
phosphatidic acid + H2O
2-acyllysophosphatidic acid + a carboxylate
show the reaction diagram
-
phosphatidic acid-specific isozymes mPA-PLA1alpha and mPA-PLA1beta
-
-
?
phosphatidic acid + H2O
?
show the reaction diagram
phosphatidic acid + H2O
lysophosphatidic acid + a carboxylate
show the reaction diagram
-
-
-
?
phosphatidylcholine + 2-acylglycerophosphocholine
2-acylglycerophosphocholine + phosphatidylcholine
show the reaction diagram
-
regiospecific transacylation activity, PLA1 transfers a fatty acid at the sn-1 position of a donor phosphatidylcholine to the sn-1 position of an acceptor 2-acyl-lysophosphatidylcholine
-
?
phosphatidylcholine + H2O
1-acyl-2-oleoyl-sn-glycerophosphocholine + arachidonic acid
show the reaction diagram
-
labeled at the sn-2 position with [14C]arachadonic acid
-
-
?
phosphatidylcholine + H2O
2-acyl-1-glycerophosphocholine + a carboxylate
show the reaction diagram
phosphatidylcholine + H2O
2-acylglycerophosphocholine + a carboxylate
show the reaction diagram
phosphatidylcholine + H2O
2-acylglycerophosphocholine + a fatty acid anion
show the reaction diagram
phosphatidylcholine + H2O
2-acylglycerophosphocholine + eicosapentaenoic acid + docosapentaenoic acid + docosahexaenoic acid
show the reaction diagram
phosphatidylcholine + H2O
?
show the reaction diagram
phosphatidylcholine + H2O
lysophosphatidylcholine + fatty acid
show the reaction diagram
phosphatidylcholine + H2O
lysophosphocholine + a carboxylate
show the reaction diagram
phosphatidylethanolamine + H2O
2-acylglycerophosphoethanolamine + a carboxylate
show the reaction diagram
phosphatidylethanolamine + H2O
?
show the reaction diagram
phosphatidylethanolamine + H2O
lysophosphatidylethanolamine + a carboxylate
show the reaction diagram
-
milk, whey, and soy bean substrates
-
-
?
phosphatidylethanolamine + H2O
lysophosphatidylethanolamine + a fatty acid anion
show the reaction diagram
phosphatidylglycerol + H2O
?
show the reaction diagram
phosphatidylinositol + H2O
?
show the reaction diagram
phosphatidylinositol + H2O
lysophosphatidylinositol + a carboxylate
show the reaction diagram
-
1% of activity with phosphatidic acid, at 0.1% Triton X-100
-
?
phosphatidylserine + H2O
2-acyl-1-glycerophosphoserine + a carboxylate
show the reaction diagram
phosphatidylserine + H2O
2-acylglycerophosphoserine + a carboxylate
show the reaction diagram
phosphatidylserine + H2O
?
show the reaction diagram
phosphatidylserine + H2O
lysophosphatidylserine + fatty acid
show the reaction diagram
sphingomyelin + H2O
?
show the reaction diagram
-
-
-
-
?
triacetin + H2O
?
show the reaction diagram
-
-
-
-
?
tributyrin + H2O
?
show the reaction diagram
-
-
-
-
?
triolein + H2O
?
show the reaction diagram
-
-
-
-
?
triolein + H2O
oleic acid + 1,2-dioleoylglycerol
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
1-palmitoyl-2-linoleoyl phosphatidylcholine + H2O
?
show the reaction diagram
-
the enzyme is responsible for about two-thirds of plasma 1-palmitoyl-2-linoleoyl phosphatidylcholine disappearance
-
-
-
1-palmitoyl-2-oleoyl-phosphatidylcholine + H2O
2-oleoyl-lysophosphatidylcholine + palmitic acid
show the reaction diagram
-
-
-
?
phosphatidic acid + H2O
2-acyl-lysophosphatidic acid + a carboxylate
show the reaction diagram
phosphatidic acid + H2O
2-acylglycerophosphatidic acid + a carboxylate
show the reaction diagram
-
-
-
?
phosphatidylcholine + H2O
2-acylglycerophosphocholine + a carboxylate
show the reaction diagram
phosphatidylcholine + H2O
2-acylglycerophosphocholine + eicosapentaenoic acid + docosapentaenoic acid + docosahexaenoic acid
show the reaction diagram
phosphatidylcholine + H2O
lysophosphocholine + a carboxylate
show the reaction diagram
phosphatidylserine + H2O
2-acyl-1-glycerophosphoserine + a carboxylate
show the reaction diagram
-
PS-PLA1 stimulates histamine release from peritoneal mast cells through production of 2-acyl-1-glycerophosphoserine
-
?
phosphatidylserine + H2O
2-acylglycerophosphoserine + a carboxylate
show the reaction diagram
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ba2+
-
divalent cation required
Mn2+
-
divalent cation required
Sr2+
-
divalent cation required
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
weak inhibition
Al3+
Corticium centrifugum
-
inhibition of phospholipase A1 activity and lysophospholipase activity
arachidonyl trifluoromethyl ketone analogue
-
-
Cationic amphiphilic drugs
-
-
-
Cd2+
complete inhibition at 2 mM
CHAPS
-
-
chlorpromazine
-
1 mM, 50% inhibition
choline plasmalogen
-
inhibits hydrolysis of phosphatidylethanolamine
Co2+
43% inhibition at 2 mM
cocaine
-
10 mM, below 10% residual activity
Cr3+
51.4% relative activity at 5 mM
DFP
-
-
di-isopropyl fluorophosphate
TbPLA1 possesses an active-site serine residue, but is relatively insensitive to serine-modifying reagents such as di-isopropyl fluorophosphate and PMSF
diethyl-p-nitrophenyl phosphate
-
diisopropyl fluorophosphate
-
IC50: 8 mM
dithiothreitol
-
1 mM, complete inhibition
DNA containing thymine glycol
ethanolamine plasmalogen
-
inhibits hydrolysis of phosphatidylethanolamine
gentamycin
-
the inhibition by aminoglycosides appears to be due to substrate depletion caused by binding of aminoglycosides to the negatively charged phospholipid and can be overcome by raising the substrate concentration
GSK264220A
-
-
guanosine 5'-[gamma-thio]triphosphate
-
-
Insulin
-
significantly reduces endothelial lipase mRNA and protein expression in a dose dependent manner
-
iodoacetic acid
KCl
-
2 M, inactivation of the soluble enzyme, no inactivation of the membrane-bound enzyme
lauryldimethylbenzyl ammonium chloride
-
-
liponox DCH
-
1%, i.e. polyoxyethylene alkylether
-
methyl arachidonyl fluorophosphonate
-
blocks phospholipase A1 as well as phospholipase A2 activity
Mg2+
13.5% relative activity at 5 mM
MgCl2
-
slight
N-bromosuccinimide
Corticium centrifugum
-
-
Na+
54.7% relative activity at 5 mM
NaCl
-
100 mM, 20-30% inhibition of lysosomal enzyme
Ni2+
57% inhibition at 2 mM
octyl-beta-glucoside
-
-
p-Diazobenzenesulfonic acid
Corticium centrifugum
-
-
palmitoyl trifluoromethyl ketone analogue
-
-
rabbit anti-phospholipase A antibodies
-
-
-
Rosenthal's inhibitor
-
-
Sodium deoxycholate
-
-
Sodium vanadate
0.01 mM, 50% inhibition
taurodeoxycholate
-
-
tetrahydrolipstatin
-
-
thiol reagents
-
protected by 2-mercaptoethanol
tobramycin
-
the inhibition by aminoglycosides appears to be due to substrate depletion caused by binding of aminoglycosides to the negatively charged phospholipid and can be overcome by raising the substrate concentration
Triton X-100
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-propanol
Corticium centrifugum
-
stimulates phospholipase A1 activity and inhibits lysophospholipase 1 activity
dithiothreitol
Rab22
-
a guanine nucleotide binding protein, activates the VipD phospholipase A1, C-terminal binding
-
Rab5
-
a guanine nucleotide binding protein, activates the VipD phospholipase A1, C-terminal binding, enzyme activity with constitutively active conformation of Rab5, Rab5a Q79L or Rab5c Q80L, is compared with the constitutively inactive forms Rab5a S34N or Rab5c S35N. Active Rab5 stimulates phospholipase activity only in full-length VipD, not in the truncated enzyme comprising residues 2-621
-
sn-1-alkyl-2-oleoyl phosphatidic acid
-
activates
-
Sodium deoxycholate
Triton X-100
tumor necrosis factor-alpha
-
stimulates secretion of endothelial lipase, the stimulation can be inhibited by adiponectin
-
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.5
1-palmitoyl-2-arachidonylglycerophosphocholine
-
-
0.6
diacyl-sn-glycero-3-phosphorylcholine
-
-
0.92
diacyl-sn-glycero-3-phosphorylethanolamine
-
-
1.19
diacyl-sn-glycero-3-phosphorylserine
-
-
2.38
phosphatidic acid
pH 7.2, 50C, recombinant enzyme
0.11 - 4
phosphatidylcholine
0.0003
phosphatidylglycerol
-
-
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.1
high-density lipoprotein
Homo sapiens
-
-
-
630
phosphatidic acid
Streptomyces albidoflavus
K0J3J2
pH 7.2, 50C, recombinant enzyme
0.057 - 0.65
phosphatidylcholine
Serratia sp.
Q9X9D8
37C, pH 8.0
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
265
phosphatidic acid
Streptomyces albidoflavus
K0J3J2
pH 7.2, 50C, recombinant enzyme
491
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8
diisopropyl fluorophosphate
Sus scrofa
-
IC50: 8 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.42
-
-
1.8
-
-
2.6
-
phosphatidylserine hydrolysis
2.8
-
recombinant PS-PLA1
2.95
-
-
3 - 8
recombinant enzyme
3.1
-
1-acyl-2-lysophosphatidylserine hydrolysis
6.383
-
lysosomal enzyme
8.72
-
-
20.6
-
enzyme from plasmalemma
80.2
-
native vesicles, pH 5.4, 37C
84
-
substrate hexadecanoylthioethane-1-phosphocholine
155
-
delipidated vesicles, pH 5.4, 37C
202.3
recombinant enzyme, after 8.5fold purification, at pH 9.0 and 35C
588 - 2873
pH 7.2, 50C, purified recombinant enzyme
1192
-
pH 8.0, 37C
2898
purified enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.2 - 4
-
-
3.6 - 3.8
-
-
3.7
-
hydrolysis of cardiolipin
4 - 4.5
Corticium centrifugum
-
-
4 - 5
-
-
4
-
lysosomal enzyme
4.5
-
hydrolysis of phosphatidylglycerol
6.5 - 7
7.5 - 8.5
-
hydrolysis of 1-palmitoyl-2-arachidonoyl-glycero-3-phosphoethanolamine, in presence of Mg2+
7.5
-
assay at
7.6
-
phosphatidylglycerol
8 - 9
-
enzyme from plasmalemma
8.5 - 9.5
-
-
8.8
-
-
9 - 9.5
-
hydrolysis of diolein
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.6 - 5.2
-
pH 2.6: 83% of maximal activity, pH 4.5: 50% of maximal activity, pH 5.2: 10% of maximal activity
2.7 - 4.8
-
pH 2.7: 40-60% of maximal activity, pH 4.8: 20-40% of maximal activity
3 - 5
-
50% of maximal activity at pH 3.0 and at pH 5.0, lysosomal enzyme
3 - 7
-
approx. 50% of maximal activity at pH 3.0, approx. 20% of maximal activity at pH 6.0
3.5 - 4.5
-
pH 3.5: about 30% of maximal activity, pH 4.5: about 25% of maximal activity
4 - 11
activity range, profile overview
5 - 10
-
activity range
5.2 - 8.4
-
pH 5.2: 10% of maximal activity, pH 6.5: about 50% of maximal activity, pH 8.4: optimum
6 - 8
-
about 25% of maximal activity at pH 6.0 and at pH 8.0
6.2 - 9.5
-
approx. 6% of maximal activity at pH 6.2, approx. 23% of maximal activity at pH 9.5
7.8 - 9.3
-
pH 7.8: about 55% of maximal activity, pH 9.3: 90% of maximal activity
8 - 10
-
pH 8.0: about 50% of maximal activity, pH 10.0: about 45% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35
recombinant enzyme
36.5
-
assay at
40
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 40
-
4C: about 50% of maximal activity, 40C: 35% of maximal activity
4
-
50% of maximal activity
20 - 70
activity range, profile overview
27 - 60
-
27C: about 25% of maximal activity, 60C: about 55% of maximal activity, strain 576. About 35% of maximal activity at 27C and at 60C, strain 579
35 - 65
additional information
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.1
calculated from amino acid sequence
8.85
-
isozme Ves a 1.04, sequence calculation
9.58
-
isozyme Ves a 1.02, sequence calculation
9.96
-
isozyme Ves a 1.03, sequence calculation
10
-
isozyme Ves a 1.01, sequence calculation
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
fibroblast
Manually annotated by BRENDA team
-
cultured cells
Manually annotated by BRENDA team
upper parts of stamen filaments in middle-stage flower buds
Manually annotated by BRENDA team
-
peritoneal, isozyme PS-PLA1 or PLA1A
Manually annotated by BRENDA team
-
enzyme is the major phospholipase activity present in oviductal fluid
Manually annotated by BRENDA team
-
northern analysis
Manually annotated by BRENDA team
the enzyme is selectively expressed in young roots at days 4-5 after germination and rapidly declines thereafter
Manually annotated by BRENDA team
-
seminal plasma, containing several phospholipase activities
Manually annotated by BRENDA team
-
northern analysis
Manually annotated by BRENDA team
-
isozyme mPA-PLA1beta
Manually annotated by BRENDA team
-
low expression
Manually annotated by BRENDA team
-
high expression
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
cis-Golgi and endoplasmic reticulum-Golgi intermediate compartment (ERGIC). Endogenous intracellular PLA1gamma does not appear to be localized to the ERGIC at 37C. At 15C, intracellular PLA1gamma shows marked colocalization with ERGIC-53
-
Manually annotated by BRENDA team
additional information
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)