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Information on EC 3.1.1.111 - phosphatidylserine sn-1 acylhydrolase and Organism(s) Homo sapiens and UniProt Accession Q53H76
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3.1.1.111 phosphatidylserine sn-1 acylhydrolaseIUBMB Comments
The enzyme, which has been described from mammals, is specific for phosphatidylserine and 2-lysophosphatidylserine, and does not act on phosphatidylcholine, phosphatidylethanolamine, phosphatidic acid or phosphatidylinositol.
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Word Map
- 3.1.1.111
- lysophosphatidylserine
- lysophospholipids
-
lysops
- lipases
-
lysophosphatidic
- melanoma
- phospholipid
- autotaxin
- triglyceride
-
mast
-
lupus
-
phosphatidic
- erythematosus
- medicine
-
ewing
-
reportedly
-
ps-specific
-
lipase-related
-
apolipoprotein
-
hypertriglyceridemia
- ns5a
- venom
-
bilayer
-
ewsr1-fli1
- lysophospholipase
- graves
- analysis
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
a phosphatidylserine
+
=
a 2-acyl-1-lyso-phosphatidylserine
+
a 1-acyl-2-lyso-phosphatidylserine
+
=
+
Synonyms
ps-pla1, phosphatidylserine-specific phospholipase a1, lipase member i, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
phosphatidylserine-specific phospholipase A1
-
-
-
-
PLA1A
-
-
-
-
PS-PLA1
-
-
-
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
3-sn-phosphatidyl-L-serine sn-1 acylhydrolase
The enzyme, which has been described from mammals, is specific for phosphatidylserine and 2-lysophosphatidylserine, and does not act on phosphatidylcholine, phosphatidylethanolamine, phosphatidic acid or phosphatidylinositol.
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
1-oleoyl-2-lyso-phosphatidic acid + H2O
sn-glycerol-1-phosphate + oleate
-
-
-
?
1-oleoyl-2-lyso-phosphatidylcholine + H2O
glycerophosphocholine + oleate
-
-
-
?
1-oleoyl-2-lyso-phosphatidylethanolamine + H2O
glycerophosphoethanolamine + oleate
-
-
-
?
1-oleoyl-2-lyso-phosphatidylserine + H2O
glycerophosphoserine + oleate
-
-
-
?
a 1-acyl-2-lyso-phosphatidylserine + H2O
glycerophosphoserine + a fatty acid
-
-
-
?
a phosphatidylserine + H2O
a 2-acyl-1-lyso-phosphatidylserine + a fatty acid
-
-
-
?
1-palmitoyl-2-oleoyl-sn-glycero-phosphatic acid + H2O
2-oleyl-1-lysophosphatidic acid + palmitate
-
-
-
?
additional information
?
-
an alternative splicing 376-amino acid product lacks two-thirds of the C-terminal domain of PS-PLA1 hydrolyzes exclusively lyso-phosphatidylserine but not phosphatidylserine appreciably. Phosphatidylcholine, phosphatidylethanolamine, phosphatidic acid, and their lyso derivatives are not hydrolyzed at all by the variant
-
-
?
additional information
?
-
-
an alternative splicing 376-amino acid product lacks two-thirds of the C-terminal domain of PS-PLA1 hydrolyzes exclusively lyso-phosphatidylserine but not phosphatidylserine appreciably. Phosphatidylcholine, phosphatidylethanolamine, phosphatidic acid, and their lyso derivatives are not hydrolyzed at all by the variant
-
-
?
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
a 1-acyl-2-lyso-phosphatidylserine + H2O
glycerophosphoserine + a fatty acid
-
-
-
?
a phosphatidylserine + H2O
a 2-acyl-1-lyso-phosphatidylserine + a fatty acid
-
-
-
?
additional information
?
-
an alternative splicing 376-amino acid product lacks two-thirds of the C-terminal domain of PS-PLA1 hydrolyzes exclusively lyso-phosphatidylserine but not phosphatidylserine appreciably. Phosphatidylcholine, phosphatidylethanolamine, phosphatidic acid, and their lyso derivatives are not hydrolyzed at all by the variant
-
-
?
additional information
?
-
-
an alternative splicing 376-amino acid product lacks two-thirds of the C-terminal domain of PS-PLA1 hydrolyzes exclusively lyso-phosphatidylserine but not phosphatidylserine appreciably. Phosphatidylcholine, phosphatidylethanolamine, phosphatidic acid, and their lyso derivatives are not hydrolyzed at all by the variant
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
mRNAs for both wild-type and splicing variant are detected in human fibroblast, keratinocyte, melanoma, HepG2, and HeLa cells
additional information
-
mRNAs for both wild-type and splicing variant are detected in human fibroblast, keratinocyte, melanoma, HepG2, and HeLa cells
additional information
transcripts are detected in various human tissues, including skeletal muscle, kidney, small intestine, spleen, and testis. The amount of the splicing variant in these tissues is about 10 to 20% that of the wild-type
additional information
-
transcripts are detected in various human tissues, including skeletal muscle, kidney, small intestine, spleen, and testis. The amount of the splicing variant in these tissues is about 10 to 20% that of the wild-type
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
isoform Ps-PLA1beta shows high affinity to heparin
physiological function
both wild-type and the natural splicing variant bind to heparin. The heparin binding site is located in N-terminal region of the enzyme
physiological function
PLA1A is upregulated by hepatitis C virus HCV infection, and PLA1A knockdown significantly reduces J399EM (genotype 2a) HCV propagation at the assembly step but not the entry, RNA replication, and protein translation steps of the life cycle. PLA1A has a role in the interaction of viral proteins NS2-E2 and NS2-NS5A. PLA1A stabilizes the nonstructural proteins NS2/NS5A dotted structure during infection
physiological function
review on extracellular PLA1s including phosphatidylserine-specific PLA1, membrane-associated phosphatidic acid-selective mPA-PLA1alpha and mPA-PLA1beta. The tertiary structures of lipases show two surface loops, the lid and the beta9 loop. The lid and the beta9 loop cover the active site in its closed conformation. Phosphatidylserine-specific PLA1, membrane-associated phosphatidic acid-selective mPA-PLA1alpha and mPA-PLA1beta have short lids and short loops. They specifically hydrolyze phospatidylserine and phosphatidic acid, respectively, producing their corresponding lysophospholipids
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). PLA1A_HUMAN
456
0
49715
Swiss-Prot
Secretory Pathway (Reliability: 1)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
membrane-associated mPA-PLA1 is insoluble in solubilization by 1% Triton X-100 and is detected in Triton X-100-insoluble buoyant fractions of sucrose gradients
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
corticosteroids, prednisolone, 6alpha-methylprednisolone, dexamethasone, and beclomethasone inhibite PS-PLA1 expression with half-maximal inhibitory concentrations less than 3.0 nM. Methotrexate, cyclosporine A, tacrolimus, 6-mercaptopurine, and mycophenoic acid show either a weak or moderate inhibition
expression is enhanced in THP-1 derived macrophages stimulated with lipopolysaccharide. Other toll-like receptor ligands (TLR2, 3, 5, 7, and 9) do not show a significant induction of PS-PLA1 mRNA
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
immunoassay for determination of enzyme in blood serum samples. The mean standard deviation of the serum PS-PLA1 antigen concentration in 191 healthy subjects is 33.8 +- 16.6 microg/l. The concentration is significantly higher among men (13.8-80.6 microg/l) than among women (12.1-68.8 microg/l)
medicine
medicine
blood serum PS-PLA1 level is significantly higher in systemic lupus erythematosus (SLE) patients than in healthy controls, active rheumatoid arthritis and Sjoegren's syndrome patients. Although PS-PLA1 is significantly elevated in systemic sclerosis and Sjoegren's syndrome patients compared with healthy controls, PS-PLA1 is significantly higher in untreated SLE patients than in treated SLE patients and disease control patients. A cut-off value of 18.2 ng/ml distinguishes untreated SLE from disease control, with sensitivity and specificity of 71.4% and 57.5%, respectively. PS-PLA1 is significantly correlated with SLE Disease Activity Index (SLEDAI) and immunoglobulin G (IgG), and inversely correlated with white blood cell counts, lymphocyte counts, total complement hemolytic activity (CH50), complements C3, and C4 in SLE patients overall
medicine
during infection with hepatitis C virus, PLA1A plays an important role in bridging the membrane-associated NS2-E2 complex and the NS5A-associated replication complex via its interaction with E2, NS2, and NS5A
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Homo sapiens (Q53H76)
Hosono, H.; Homma, M.; Ogasawara, Y.; Makide, K.; Aoki, J.; Niwata, H.; Watanabe, M.; Inoue, K.; Ohkohchi, N.; Kohda, Y.
Expression of phosphatidylserine-specific phospholipase A1 mRNA in human THP-1-derived macrophages
Cell Transplant.
19
759-764
2010
Homo sapiens (Q53H76)
Nakamura, K.; Igarashi, K.; Ohkawa, R.; Saiki, N.; Nagasaki, M.; Uno, K.; Hayashi, N.; Sawada, T.; Syukuya, K.; Yokota, H.; Arai, H.; Ikeda, H.; Aoki, J.; Yatomi, Y.
A novel enzyme immunoassay for the determination of phosphatidylserine-specific phospholipase A1 in human serum samples
Clin. Chim. Acta
411
1090-1094
2010
Homo sapiens (Q53H76)
Sawada, T.; Kurano, M.; Shirai, H.; Iwasaki, Y.; Tahara, K.; Hayashi, H.; Igarashi, K.; Fujio, K.; Aoki, J.; Yatomi, Y.
Serum phosphatidylserine-specific phospholipase A1 as a novel biomarker for monitoring systemic lupus erythematosus disease activity
Int. J. Rheum. Dis.
22
2059-2066
2019
Homo sapiens (Q53H76), Homo sapiens
Nagai, Y.; Aoki, J.; Sato, T.; Amano, K.; Matsuda, Y.; Arai, H.; Inoue, K.
An alternative splicing form of phosphatidylserine-specific phospholipase A1 that exhibits lysophosphatidylserine-specific lysophospholipase activity in humans
J. Biol. Chem.
274
11053-11059
1999
Homo sapiens (Q53H76), 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)
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