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Information on EC 3.1.1.32 - phospholipase A1 and Organism(s) Rattus norvegicus and UniProt Accession P53817

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.1 Carboxylic-ester hydrolases
                3.1.1.32 phospholipase A1
IUBMB Comments
This enzyme has a much broader specificity than EC 3.1.1.4 phospholipase A2. Requires Ca2+.
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Select one or more organisms in this record: ?
This record set is specific for:
Rattus norvegicus
UNIPROT: P53817
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The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
phospholipase a1, pla1, ompla, h-rev107, ddhd1, outer membrane phospholipase a, pla1a, lipase h, ves v 1, ipla-1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospholipase A1/2
-
Allergen Dol m 1.01
-
-
-
-
Allergen Dol m 1.02
-
-
-
-
endothelial lipase
-
-
hepatic lipase
-
-
mPA-PLA1alpha
-
-
mPA-PLA1beta
-
-
OM PLA
-
-
-
-
OMPLA
-
-
-
-
pancreatic lipase-related protein 2
-
-
Phosphatidylcholine 1-acylhydrolase
-
-
-
-
additional information
-
the isozymes belong to the pancreatic lipase gene family or to the phospholipase family
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
phosphatidylcholine + H2O = 2-acylglycerophosphocholine + a carboxylate
show the reaction diagram
structure-function relationship
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of carboxylic ester
-
-
-
-
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
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
dipalmitoylphosphatidylcholine + H2O
palmitic acid + 1-lyso-2-palmitoylphosphatidylcholine
show the reaction diagram
-
-
-
?
phosphatidylcholine + H2O
2-acylglycerophosphocholine + a carboxylate
show the reaction diagram
-
-
-
?
phosphatidylethanolamine + H2O
2-acylglycerophosphoethanolamine + a carboxylate
show the reaction diagram
-
-
-
?
1,2-dioleoylphosphatidylcholine + H2O
oleic acid + 2-oleoylglycerophosphocholine
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-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-palmitoyllysophosphatidylcholine + H2O
palmitic acid + lysophosphatidylcholine
show the reaction diagram
-
weak activity
-
-
?
1-stearoyl-2-arachidonyl-sn-glycero-3-phosphoinositol + H2O
2-arachidonylglycero-3-phosphoinositol + ?
show the reaction diagram
-
-
no release of free arachidonate
?
2-oleoylphosphatidylcholine + H2O
oleic acid + glycerophosphocholine
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
-
-
-
-
?
dipalmitoylphosphatidylcholine + H2O
?
show the reaction diagram
-
-
-
-
?
phosphatidic acid + H2O
?
show the reaction diagram
-
phosphatidic acid-specific isozymes mPA-PLA1alpha and mPA-PLA1beta
-
-
?
phosphatidylcholine + H2O
2-acylglycerophosphocholine + a carboxylate
show the reaction diagram
-
-
-
-
?
phosphatidylcholine + H2O
?
show the reaction diagram
-
-
-
-
?
phosphatidylethanolamine + H2O
2-acylglycerophosphoethanolamine + a carboxylate
show the reaction diagram
-
-
-
-
?
phosphatidylethanolamine + H2O
?
show the reaction diagram
-
-
-
-
?
phosphatidylserine + H2O
?
show the reaction diagram
-
phosphatidylserine-specific PLA1 isozyme PS-PLA1 or PLA1A
-
-
?
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
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
-
-
?
phosphatidylcholine + H2O
2-acylglycerophosphocholine + a carboxylate
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
H-Rev107 functions as a cytosolic Ca2+-independent PLA1/2
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
iodoacetic acid
-
Ca2+
-
10 mM CaCl2, 50-60% inhibition of lysosomal enzyme
choline plasmalogen
-
inhibits hydrolysis of phosphatidylethanolamine
cocaine
-
10 mM, below 10% residual activity
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
NaCl
-
100 mM, 20-30% inhibition of lysosomal enzyme
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
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dithiothreitol
required for full activity. Addition of 2 mM increases PLA1/2 activity 167fold
Triton X-100
-
stimulates
additional information
purified H-Rev107 exhibits an 88fold higher PLA1/2 activity than the cytosolic fraction
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.6
diacyl-sn-glycero-3-phosphorylcholine
-
-
0.92
diacyl-sn-glycero-3-phosphorylethanolamine
-
-
1.19
diacyl-sn-glycero-3-phosphorylserine
-
-
1.5 - 4
phosphatidylcholine
additional information
additional information
-
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
155
-
delipidated vesicles, pH 5.4, 37°C
20.6
-
enzyme from plasmalemma
6.383
-
lysosomal enzyme
80.2
-
native vesicles, pH 5.4, 37°C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.2 - 4
-
-
3.6 - 3.8
-
-
4
-
lysosomal enzyme
8 - 9
-
enzyme from plasmalemma
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
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
isozyme PS-PLA1 or PLA1A
Manually annotated by BRENDA team
-
fibroblast
Manually annotated by BRENDA team
-
isozyme endothelial lipase
Manually annotated by BRENDA team
-
cultured cells
Manually annotated by BRENDA team
-
isozyme PS-PLA1 or PLA1A
Manually annotated by BRENDA team
-
peritoneal, isozyme PS-PLA1 or PLA1A
Manually annotated by BRENDA team
-
pancreatic lipase-related protein 2
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
isozyme PLA1S
-
Manually annotated by BRENDA team
-
associated, phosphatidic acid-specific isozymes mPA-PLA1alpha and mPA-PLA1beta
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
H-Rev107 functions principally as a Ca2+-independent PLA1/2 with a higher PLA1 activity. Transient expression of H-Rev107 in COS-7 cells does not appear to influence cell proliferation
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PLAT3_RAT
160
1
17749
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
19000
x * 19000, SDS-PAGE
30000
-
gel filtration
32000
-
x * 32000, lysosomal enzyme, SDS-PAGE
34000
-
x * 34000, SDS-PAGE
45000
-
gel filtration
75000
-
x * 75000, enzyme from plasmalemma, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 19000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
side-chain modification
-
glycoprotein
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
deletion mutant of H-Rev107 lacking either N-terminal 8 or N-terminal 16 amino acids (DELTAN1, DELTAN2) or C-terminal 25 amino acids (DELTAC1). Expression of the mutants with the expected molecular masses. As for PLA1/2 activity, DELTAN1 shows very low activity (about 3% that of the wild-type), and DELTAN2 and DELTAC1 are entirely inactive
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
2 h, 20% loss of activity
70
-
5 min, 50% loss of activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, 50% glycerol, stable for 1 year
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
FLAG-tagged H-Rev107 by immunoprecipitation
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression vector harboring H-Rev107 with a FLAG tag at the N terminus. Expression vector harboring H-Rev107 cDNA introduced into COS-7 cells
DNA and amino acid sequence analysis
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
acidotropic accumulation of cocaine in lysosomes inhibits acid phospholipase A1 and inactivates acid sphingomyelinase, inducing a mixed lysosomal lipidosis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hostetler, K.Y.; Gardner, M.F.; Giordano, J.R.
Purification of lysosomal phospholipase A and demonstration of proteins that inhibit phospholipase A in a lysosomal fraction from rat kidney cortex
Biochemistry
25
6456-6461
1986
Rattus norvegicus
Manually annotated by BRENDA team
Nalbone, G.; Hostetler, K.Y.; Leonardi, J.; Trotz, M.; Lafont, H.
Partial characterization of rat heart cytosolic phospholipase A1 and demonstration of essential sulfhydryl groups
Biochim. Biophys. Acta
877
88-95
1986
Rattus norvegicus
Manually annotated by BRENDA team
Hostetler, K.Y.; Yazaki, P.J.; van den Bosch, H.
Purification of lysosomal phospholipase A. Evidence for multiple isoenzymes in rat liver
J. Biol. Chem.
257
13367-13373
1982
Rattus norvegicus
Manually annotated by BRENDA team
Ueda, H.; Kabayshi, T.; Kishimoto, M.; Tsutsumi, T.; Okuyama, H.
A possible pathway of phosphoinositide metabolism through EDTA-insensitive phospholipase A1 followed by lysophosphoinositide-specific phospholipase C in rat brain
J. Neurochem.
61
1874-1881
1993
Rattus norvegicus
Manually annotated by BRENDA team
Waite, M.; Rao, R.H.; Griffin, H.; Franson, R.; Miller, C.; Sisson, P.; Frye, J.
Phospholipases A1 from lysosomes and plasma membranes of rat liver
Methods Enzymol.
71
674-689
1981
Rattus norvegicus
Manually annotated by BRENDA team
Woelk, H.; Peiler-Ichikawa, K.; Binaglia, L.; Goracci, G.; Porcellati, G.
Distribution and properties of phospholipases A1 and A2 in synaptosomes and subsynaptosomal fractions of rat brain
Hoppe-Seyler's Z. Physiol. Chem.
355
1535-1542
1974
Rattus norvegicus
Manually annotated by BRENDA team
Woelk, H.; Porcellati, G.
Subcellular distribution and kinetic properties of rat brain phospholipases A1 and A2
Hoppe-Seyler's Z. Physiol. Chem.
354
90-100
1973
Rattus norvegicus
Manually annotated by BRENDA team
Hostetler, K.Y.; Gardner, M.F.
Purification of rat kidney lysosomal phospholipase A1
Methods Enzymol.
197
325-330
1991
Rattus norvegicus
Manually annotated by BRENDA team
Schmidt, M.; Lffler, B.M.; Kunze, H.
Protease inhibitors reduce lysosomal acid phospholipase A1 activity in cultured rat hepatocates
Biochem. Int.
20
337-342
1990
Rattus norvegicus
Manually annotated by BRENDA team
Scagnelli, G.P.; Cooper, P.S.; VandenBroek, J.M.; Berman, W.F.; Schwartz, C.C.
Plasma 1-palmitoyl-2-linoleoyl phosphatidylcholine. Evidence for extensive phospholipase A1 hydrolysis and hepatic metabolism of the product
J. Biol. Chem.
266
18002-18011
1991
Rattus norvegicus
Manually annotated by BRENDA team
Hostetler, K.Y.; Jellison, E.J.
Inhibition of kidney lysosomal phospholipase A1 by aminoglycosides is a novel variant of substrate depletion inhibition
J. Pharmacol. Exp. Ther.
254
188-191
1990
Rattus norvegicus
Manually annotated by BRENDA team
Uchiyama, S.I.; Miyazaki, Y.; Amakasu, Y.; Kuwata, H.; Nakatani, Y.; Atsumi, G.I.; Murakami, M.; Kudo, I.
Characterization of heparin low-affinity phospholipase A1 present in brain and testicular tissue
J. Biochem.
125
1001-1010
1999
Bos taurus, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Piret, J.; Schanck, A.; Delfosse, S.; Van Bambeke, F.; Kishore, B.K.; Tulkens, P.M.; Mingeot-Leclercq, M.P.
Modulation of the in vitro activity of lysosomal phospholipase A1 by membrane lipids
Chem. Phys. Lipids
133
1-15
2005
Rattus norvegicus
Manually annotated by BRENDA team
Nassogne, M.C.; Lizarraga, C.; N'Kuli, F.; Van Bambeke, F.; Van Binst, R.; Wallemacq, P.; Tulkens, P.M.; Mingeot-Leclercq, M.P.; Levade, T.; Courtoy, P.J.
Cocaine induces a mixed lysosomal lipidosis in cultured fibroblasts, by inactivation of acid sphingomyelinase and inhibition of phospholipase A1
Toxicol. Appl. Pharmacol.
194
101-110
2004
Rattus norvegicus
Manually annotated by BRENDA team
Aoki, J.; Inoue, A.; Makide, K.; Saiki, N.; Arai, H.
Structure and function of extracellular phospholipase A1 belonging to the pancreatic lipase gene family
Biochimie
89
197-204
2007
Bombyx mori, Cavia porcellus, Drosophila melanogaster, Homo sapiens, Mus musculus, Rattus norvegicus, Dolichovespula maculata
Manually annotated by BRENDA team
Uyama, T.; Morishita, J.; Jin, X.H.; Okamoto, Y.; Tsuboi, K.; Ueda, N.
The tumor suppressor gene H-Rev107 functions as a novel Ca2+-independent cytosolic phospholipase A1/2 of the thiol hydrolase type
J. Lipid Res.
50
685-693
2009
Homo sapiens, Mus musculus, Rattus norvegicus (P53817)
Manually annotated by BRENDA team