Any feedback?
Information on EC 3.1.1.32 - phospholipase A1 and Organism(s) Homo sapiens and UniProt Accession Q6XZB0
for references in articles please use BRENDA:EC3.1.1.32Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
3.1.1.32 phospholipase A1IUBMB Comments
This enzyme has a much broader specificity than EC 3.1.1.4 phospholipase A2. Requires Ca2+.
Specify your search results
Word Map
- 3.1.1.32
- phospholipid
- platelet
- phospholipases
- lysosomal
- lysophospholipase
- phosphatidylethanolamine
- venom
- lysophospholipids
- thrombocytopenia
- lysophosphatidylcholine
- lipases
-
arachidonic
-
alloimmune
- wasp
-
alloantigens
- purpura
-
platelet-specific
- hymenoptera
-
deacylation
-
lysophosphatidic
-
gpiiia
- hornet
- hypotrichosis
-
2-acyl
- vespula
-
vespid
-
posttransfusion
-
component-resolved
- plasmalogens
-
degumming
-
alloantibody
- monoacylglycerol
-
3.1.1.4
-
phospholipidosis
- lysophosphatidylinositol
-
woolly
-
glanzmann
- thrombasthenia
- degradation
- synthesis
- medicine
- lysophosphatidylethanolamine
- pharmacology
- food industry
- nutrition
- analysis
- industry
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Allergen Dol m 1.01
-
-
-
-
Allergen Dol m 1.02
-
-
-
-
OM PLA
-
-
-
-
OMPLA
-
-
-
-
Phosphatidylcholine 1-acylhydrolase
-
-
-
-
PLRP2
additional information
-
the isozymes belong to the pancreatic lipase gene family or to the phospholipase family
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
phosphatidylcholine + H2O = 2-acylglycerophosphocholine + a carboxylate
structure-function relationship
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of carboxylic ester
-
-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
-
-, -, -
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
9043-29-2
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
phosphatidic acid + H2O
2-acyl-lysophosphatidic acid + a carboxylate
-
-
?
dipalmitoylphosphatidylcholine + H2O
palmitic acid + 1-lyso-2-palmitoylphosphatidylcholine
-
-
-
-
?
phosphatidic acid + H2O
?
-
phosphatidic acid-specific isozymes mPA-PLA1alpha and mPA-PLA1beta
-
-
?
phosphatidylcholine + H2O
2-acylglycerophosphocholine + a fatty acid anion
-
-
-
-
?
phosphatidylethanolamine + H2O
lysophosphatidylethanolamine + a fatty acid anion
-
-
-
-
?
phosphatidylserine + H2O
2-acylglycerophosphoserine + a carboxylate
-
low activity
-
?
phosphatidic acid + H2O
2-acyl-lysophosphatidic acid + a carboxylate
-
-
-
?
phosphatidic acid + H2O
2-acyl-lysophosphatidic acid + a carboxylate
-
-
?
phosphatidic acid + H2O
2-acyl-lysophosphatidic acid + a carboxylate
-
best substrate
-
?
phosphatidic acid + H2O
2-acyl-lysophosphatidic acid + a carboxylate
-
preferred substrate in vitro
-
-
?
phosphatidylcholine + H2O
2-acylglycerophosphocholine + a carboxylate
-
-
-
?
phosphatidylcholine + H2O
2-acylglycerophosphocholine + a carboxylate
-
-
-
-
?
phosphatidylcholine + H2O
2-acylglycerophosphocholine + a carboxylate
-
very low activity
-
?
phosphatidylcholine + H2O
2-acylglycerophosphocholine + a carboxylate
-
phosphatidylcholine from shark liver
-
-
?
phosphatidylethanolamine + H2O
2-acylglycerophosphoethanolamine + a carboxylate
-
-
-
-
?
phosphatidylethanolamine + H2O
2-acylglycerophosphoethanolamine + a carboxylate
-
similar activity as with phosphatidic acid
-
?
phosphatidylethanolamine + H2O
?
-
docosahexaenoic acid-enriched phosphatidylethanolamine vesicles
-
-
?
phosphatidylserine + H2O
?
-
in short incubation, 1-3 h, 2-acyllysophosphatidylserine is produced, in longer incubations the cis-unsaturated fatty acid is also released
-
-
?
phosphatidylserine + H2O
?
-
docosahexaenoic acid-enriched phosphatidylserine vesicles
-
-
?
phosphatidylserine + H2O
?
-
phosphatidylserine-specific PLA1 isozyme PS-PLA1 or PLA1A
-
-
?
additional information
?
-
-
isozyme mPA-PLA1beta is identical to the lipid defect locus lipase LPDL, encoded by gene lpd, homozygous insertion mutation leads to high levels of triacylglycerols in the plasma and hepatic steatosis
-
-
?
additional information
?
-
-
the enzyme plays an important role in the metabolism of high density lipoproteins, it may be responsible for the generation of docosahexaenoic acid DHA lysophospholipids in plasma, DHA is important in brain development and neurological function, the endothelial lipase is important in the delivery of DHA lysophospholipid carriers to the brain, overview
-
-
?
additional information
?
-
-
several isozymes with different substrate specificities, overview, endothelial lipase hepatic lipase, and PLRP2 also exhibit triacylglycerol-hydrolyzing activity
-
-
?
additional information
?
-
-
monoglyceride lipase does exhibit PLA1 activity
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
phosphatidic acid + H2O
2-acyl-lysophosphatidic acid + a carboxylate
-
-
?
phosphatidic acid + H2O
2-acyl-lysophosphatidic acid + a carboxylate
-
-
-
?
phosphatidic acid + H2O
2-acyl-lysophosphatidic acid + a carboxylate
-
-
?
phosphatidylcholine + H2O
2-acylglycerophosphocholine + a carboxylate
-
-
-
?
additional information
?
-
-
isozyme mPA-PLA1beta is identical to the lipid defect locus lipase LPDL, encoded by gene lpd, homozygous insertion mutation leads to high levels of triacylglycerols in the plasma and hepatic steatosis
-
-
?
additional information
?
-
-
the enzyme plays an important role in the metabolism of high density lipoproteins, it may be responsible for the generation of docosahexaenoic acid DHA lysophospholipids in plasma, DHA is important in brain development and neurological function, the endothelial lipase is important in the delivery of DHA lysophospholipid carriers to the brain, overview
-
-
?
additional information
?
-
-
monoglyceride lipase does exhibit PLA1 activity
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
H-Rev107 functions as a cytosolic Ca2+-independent PLA1/2
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Insulin
-
significantly reduces endothelial lipase mRNA and protein expression in a dose dependent manner
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
tumor necrosis factor-alpha
-
stimulates secretion of endothelial lipase, the stimulation can be inhibited by adiponectin
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
not expressed in SIMA cell, SH-SY5Y cell, IMR-5 cell, KELLY cell, NB-1 cell, NB-2 cell, NB-3 cell, Nb-4 cell, ERMS-7 cell, ERMS-8 cell, ERMS-10 cell, ARMS-7 cell, ARMS-8 cell, ARMS-9 cell, ARMS-10 cell, adrenal gland, prostate gland, uterus, salivary gland, skeletal muscle, thymus, adult brain, cerebellum, fetal liver kidney, bone marrow, liver, lung, heart, and placenta
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
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 37°C. At 15°C, intracellular PLA1gamma shows marked colocalization with ERGIC-53
-
-
the enzyme is secreted by the cells of the blood-brain barrier
-
-
associated, phosphatidic acid-specific isozymes mPA-PLA1alpha and mPA-PLA1beta
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
-
knockdown of intracellular PLA1gamma expression by RNAi does not affect the anterograde transport of ts045 vesicular stomatitis virus protein (VSVGts045) but dramatically delays two types of Golgi-to-endoplasmic reticulum retrograde membrane transport, i.e., transfer of the Golgi membrane into the endoplasmic reticulum in the presence of brefeldin A and delivery of cholera toxin B subunit from the Golgi complex to the endoplasmic reticulum. Knockdown of intracellular PLA1gamma does not impair coat protein complex I- and Rab6-dependent retrograde transports represented by ERGIC-53 recycling and endoplasmic reticulum delivery of Shiga toxin, respectively
malfunction
-
phosphatidic acid-preferring phospholipase A1 depletion causes mitochondrial elongation, leading to a loss of motility
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
physiological function
-
mediates a specific retrograde membrane transport pathway between the endoplasmic reticulum and the Golgi complex
physiological function
-
the phospholipase A1 activity of lysophospholipase A-I links platelet activation to LPA production during blood coagulation
physiological function
-
the phosphatidic acid-preferring phospholipase A1 regulates mitochondrial dynamics. When ectopically expressed in HeLa cells, it induces mitochondrial fragmentation, whereas its depletion causes mitochondrial elongation. The effects of the enzyme on mitochondrial morphology appear to counteract those of MitoPLD, a mitochondrion-localized phospholipase D that produces phosphatidic acid from cardiolipin
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
isozyme tertiary structure analysis, amino acid sequence comparison
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
N336Q
-
the mutant shows a significant phospholipase A1 activity on mixed phospholipid-bile salt micelles
additional information
additional information
-
gene lpd encoding isozyme mPA-PLA1beta, i.e. the lipid defect locus lipase LPDL, homozygous insertion mutation leads to high levels of triacylglycerols in the plasma and hepatic steatosis
additional information
-
construction of enzyme knockout mutant HeLa cells by treatment with specific siRNA, phenotype, overview
additional information
homozygous mutation c.395dup/p.Gly133Argfs*26 in DDHD1 results in a complex form of hereditary spastic paraplegia associated with retinal dystrophy and a pattern of neurodegeneration with brain iron accumulation
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme 1500fold from thrombin-activated platelets by anion exchange, hydrophobic interaction, and affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cDNA encoding C-terminally FLAG-tagged H-Rev107. Subcloned into the HindIII and EcoRI sites of pcDNA3.1 (+). Expression vector harboring H-Rev107 cDNA introduced into COS-7 cells
-
DNA and amino acid sequence analysis of isozymes, isozyme genetic structures, location of isozyme PS-PLA1 or PLA1A encoding gene on chromosome 3q13.2-q13.3, phylogenetic analysis of isozymes, overview
-
expression of FLAG-tagged wild-type and mutant enzymes in HeLa cells and in siRNA-treated knockout mutant HeLa cells. Upon overexpression of wild-type enzyme, the tubular structures become fragmented, expression of the mutant S537A has no effect
-
polypeptide (amino acid number 368-486 of intracellular PLA1gamma) expressed as a glutathione S-transferase fusion protein in Escherichia coli. Purified protein used to immunize rats. The cDNA encoding intracellular PLA1gamma cloned into pEGFP-C3 vector and stably expressed in CHO cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of intracellular PLA1gamma is suppressed by transfecting cells with siRNA against intracellular PLA1gamma. Expression of intracellular PLA1gamma protein is decreased to less than 10% that of control siRNA-treated cells
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
homozygous mutation c.395dup/p.Gly133Argfs*26 in DDHD1 results in a complex form of hereditary spastic paraplegia associated with retinal dystrophy and a pattern of neurodegeneration with brain iron accumulation
medicine
role of enzyme in oncogenesis and metastasis of colorectal cancer. Tumor depth and hematogenous metastasis independently positively correlate with phospholipase A1 expression. High expression is associated with shorter disease-free survival, although it is not an independent predictive factor
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lffler, B.M.; Kunze, H.
Fractionation, biochemical characterization and lysosomal phospholipases of human liver
FEBS Lett.
216
51-56
1987
Homo sapiens
Bellini, F.; Bruni, A.
Role of a serum phospholipase A1 in the phosphati dylserine-induced T cell inhibition
FEBS Lett.
316
1-4
1993
Bos taurus, Homo sapiens
Nakajima, K.; Sonoda, H.; Mizoguchi, T.; Aoki, J.; Arai, H.; Nagahama, M.; Tagaya, M.; Tani, K.
A novel phospholipase A1 with sequence homology to a mammalian Sec23p-interacting protein, p125
J. Biol. Chem.
277
11329-11335
2002
Homo sapiens
Sonoda, H.; Aoki, J.; Hiramatsu, T.; Ishida, M.; Bandoh, K.; Nagai, Y.; Taguchi, R.; Inoue, K.; Arai, H.
A novel phosphatidic acid-selective phospholipase A1 that produces lysophosphatidic acid
J. Biol. Chem.
277
34254-34263
2002
Homo sapiens (Q8WWY8), Homo sapiens
Hiramatsu, T.; Sonoda, H.; Takanezawa, Y.; Morikawa, R.; Ishida, M.; Kasahara, K.; Sanai, Y.; Taguchi, R.; Aoki, J.; Arai, H.
Biochemical and molecular characterization of two phosphatidic acid-selective phospholipase A1s, mPA-PLA1alpha and mPA-PLA1beta
J. Biol. Chem.
278
49438-49447
2003
Homo sapiens (Q6XZB0), Homo sapiens
Chen, S.; Subbaiah, P.V.
Phospholipid and fatty acid specificity of endothelial lipase: Potential role of the enzyme in the delivery of docosahexaenoic acid (DHA) to tissues
Biochim. Biophys. Acta
1771
1319-1328
2007
Homo sapiens
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
Qiu, G.; Hill, J.S.
Endothelial lipase promotes apolipoprotein AI-mediated cholesterol efflux in THP-1 macrophages
Arterioscler. Thromb. Vasc. Biol.
29
84-91
2009
Homo sapiens
Shiu, S.W.; Tan, K.C.; Huang, Y.; Wong, Y.
Type 2 diabetes mellitus and endothelial lipase
Atherosclerosis
198
441-447
2008
Homo sapiens
Eydoux, C.; Spinelli, S.; Davis, T.L.; Walker, J.R.; Seitova, A.; Dhe-Paganon, S.; De Caro, A.; Cambillau, C.; Carriere, F.
Structure of human pancreatic lipase-related protein 2 with the lid in an open conformation
Biochemistry
47
9553-9564
2008
Homo sapiens
Badellino, K.O.; Wolfe, M.L.; Reilly, M.P.; Rader, D.J.
Endothelial lipase is increased in vivo by inflammation in humans
Circulation
117
678-685
2008
Homo sapiens
Keller, P.M.; Rust, T.; Murphy, D.J.; Matico, R.; Trill, J.J.; Krawiec, J.A.; Jurewicz, A.; Jaye, M.; Harpel, M.; Thrall, S.; Schwartz, B.
A high-throughput screen for endothelial lipase using HDL as substrate
J. Biomol. Screen.
13
468-475
2008
Homo sapiens
Foell, J.L.; Hesse, M.; Volkmer, I.; Schmiedel, B.J.; Neumann, I.; Staege, M.S.
Membrane-associated phospholipase A1 beta (LIPI) is an ewing tumour-associated cancer/testis antigen
Pediatr. Blood Cancer
51
228-234
2008
Homo sapiens
Morikawa, R.K.; Aoki, J.; Kano, F.; Murata, M.; Yamamoto, A.; Tsujimoto, M.; Arai, H.
Intracellular phospholipase A1gamma (iPLA1gamma) is a novel factor involved in coat protein complex I- and Rab6-independent retrograde transport between the endoplasmic reticulum and the Golgi complex
J. Biol. Chem.
284
26620-26630
2009
Homo sapiens
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)
Bolen, A.L.; Naren, A.P.; Yarlagadda, S.; Beranova-Giorgianni, S.; Chen, L.; Norman, D.; Baker, D.L.; Rowland, M.M.; Best, M.D.; Sano, T.; Tsukahara, T.; Liliom, K.; Igarashi, Y.; Tigyi, G.
The phospholipase A1 activity of lysophospholipase A-I links platelet activation to LPA production during blood coagulation
J. Lipid Res.
52
958-970
2011
Homo sapiens
Baba, T.; Kashiwagi, Y.; Arimitsu, N.; Kogure, T.; Edo, A.; Maruyama, T.; Nakao, K.; Nakanishi, H.; Kinoshita, M.; Frohman, M.A.; Yamamoto, A.; Tani, K.
Phosphatidic acid (PA)-preferring phospholipase A1 regulates mitochondrial dynamics
J. Biol. Chem.
289
11497-11511
2014
Homo sapiens, Mus musculus
Iida, Y.; Sunami, E.; Yamashita, H.; Hiyoshi, M.; Ishihara, S.; Yamaguchi, H.; Inoue, A.; Makide, K.; Tsuno, N.H.; Aoki, J.; Kitayama, J.; Watanabe, T.
Phosphatidylserine-specific phospholipase A1 (PS-PLA1) expression in colorectal cancer correlates with tumor invasion and hematogenous metastasis
Anticancer Res.
35
1459-1464
2015
Homo sapiens (Q53H76)
Dard, R.; Meyniel, C.; Touitou, V.; Stevanin, G.; Lamari, F.; Durr, A.; Ewenczyk, C.; Mochel, F.
Mutations in DDHD1, encoding a phospholipase A1, is a novel cause of retinopathy and neurodegeneration with brain iron accumulation
Eur. J. Med. Genet.
60
639-642
2017
Homo sapiens (Q8NEL9)
EXTERNAL LINKS (specific for EC-Number 3.1.1.32)
Transporter Classification Database (TCDB): 1.B.84.1.6, 1.B.84.1.5, 1.B.84.1.3, 1.B.84.1.1, 1.B.84.1.4, 1.B.84.1.2
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
