Information on EC 3.1.1.5 - lysophospholipase and Organism(s) Homo sapiens and UniProt Accession Q6P4A8

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This record set is specific for:
Homo sapiens
UNIPROT: Q6P4A8


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


The taxonomic range for the selected organisms is: Homo sapiens

EC NUMBER
COMMENTARY hide
3.1.1.5
-
RECOMMENDED NAME
GeneOntology No.
lysophospholipase
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of carboxylic ester
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hydrolysis of carboxylic ester
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
phospholipid remodeling (phosphatidylethanolamine, yeast)
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degradation of sugar alcohols
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Glycerophospholipid metabolism
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SYSTEMATIC NAME
IUBMB Comments
2-lysophosphatidylcholine acylhydrolase
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CAS REGISTRY NUMBER
COMMENTARY hide
9001-85-8
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,2-didecanoylphosphatidylcholine + H2O
?
show the reaction diagram
-
-
-
?
1,2-dipalmitoylphosphatidylcholine + H2O
?
show the reaction diagram
-
-
-
?
1-palmitoyl-2-lysophosphatidylcholine + H2O
?
show the reaction diagram
-
-
-
?
2-lysophosphatidylcholine + H2O
glycerophosphocholine + a carboxylate
show the reaction diagram
-
-
-
?
1-palmitoyl lysophosphatidylcholine + H2O
glycerophosphocholine + palmitate
show the reaction diagram
-
-
-
?
1-palmitoyl-2-lysophosphatidylcholine + H2O
glycerophosphocholine + palmitic acid
show the reaction diagram
-
-
-
-
-
2-lysophosphatidylcholine + H2O
glycerophosphocholine + a carboxylate
show the reaction diagram
C10:0-glycero-3-phosphocholine + H2O
?
show the reaction diagram
-
rank order for lysophospholipase activity C12:0-GPC higher than C14:0-GPC, C10:0-GPC higher than C18:0-GPC, C18:1-GPC, and C18:2-GPC higher than C8:0-GPC
-
-
?
C12:0-glycero-3-phosphocholine + H2O
?
show the reaction diagram
-
rank order for lysophospholipase activity C12:0-GPC higher than C14:0-GPC, C10:0-GPC higher than C18:0-GPC, C18:1-GPC, and C18:2-GPC higher than C8:0-GPC
-
-
?
C14:0-glycero-3-phosphocholine + H2O
?
show the reaction diagram
-
rank order for lysophospholipase activity C12:0-GPC higher than C14:0-GPC, C10:0-GPC higher than C18:0-GPC, C18:1-GPC, and C18:2-GPC higher than C8:0-GPC
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-
?
C18:0-glycero-3-phosphocholine + H2O
?
show the reaction diagram
-
rank order for lysophospholipase activity C12:0-GPC higher than C14:0-GPC, C10:0-GPC higher than C18:0-GPC, C18:1-GPC, and C18:2-GPC higher than C8:0-GPC
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-
?
C18:1-glycero-3-phosphocholine + H2O
?
show the reaction diagram
-
rank order for lysophospholipase activity C12:0-GPC higher than C14:0-GPC, C10:0-GPC higher than C18:0-GPC, C18:1-GPC, and C18:2-GPC higher than C8:0-GPC
-
-
?
C18:2-glycero-3-phosphocholine + H2O
?
show the reaction diagram
-
rank order for lysophospholipase activity C12:0-GPC higher than C14:0-GPC, C10:0-GPC higher than C18:0-GPC, C18:1-GPC, and C18:2-GPC higher than C8:0-GPC
-
-
?
C8:0-glycero-3-phosphocholine + H2O
?
show the reaction diagram
-
rank order for lysophospholipase activity C12:0-GPC higher than C14:0-GPC, C10:0-GPC higher than C18:0-GPC, C18:1-GPC, and C18:2-GPC higher than C8:0-GPC
-
-
?
lysophosphatidylcholine + H2O
glycerophosphorylcholine + unesterified fatty acid
show the reaction diagram
-
myristoyllysophosphatidylcholine is hydrolyzed 50% better than the longer chain palmitoyllysophosphatidylcholine
-
-
?
lysophosphatidylethanolamine + H2O
?
show the reaction diagram
-
-
-
-
?
palmitoyl-Gialpha1 + H2O
palmitic acid + Gialpha1
show the reaction diagram
-
thioesterase activity
-
?
palmitoyl-glycero-3-phosphocholine + H2O
glycerophosphocholine + palmitic acid
show the reaction diagram
-
-
-
-
?
palmitoyl-peptide + H2O
palmitate + peptide
show the reaction diagram
residue 3 to 14 of RGS4 protein with palmitoyl group attached at Cys12 of RGS4 protein
-
-
?
palmitoyl-SCoA + H2O
HS-CoA + palmitic acid
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
2-lysophosphatidylcholine + H2O
glycerophosphocholine + a carboxylate
show the reaction diagram
Q6P4A8
-
-
-
?
2-lysophosphatidylcholine + H2O
glycerophosphocholine + a carboxylate
show the reaction diagram
-
-
-
?
additional information
?
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Q05315
combined activities of secretory phospholipases and eosinophil lysophospholipases induce pulmonary surfactant dysfunction by phospholipid hydrolysis
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
activity independent of Ca2+ and Mg2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-palmitoyl lysophosphatidylcholine
competitive inhibitor for acylprotein thioesterase activity
DNA containing thymine glycol
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lysophosphatidic acid
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inhibition in a dose-dependent manner
methyl (5Z,8Z,11Z,14Z)-icosa-5,8,11,14- tetraenylphosphonofluoridate
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palmitoyl-peptide
competitive inhibitor for lysophospholipase activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.1
1,2-didecanoylphosphatidylcholine
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0.0273
1-palmitoyl lysophosphatidylcholine
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0.00349
palmitoyl-peptide
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0222
1-palmitoyl lysophosphatidylcholine
for acylprotein thioesterase activity
0.0323
palmitoyl-peptide
for lysophospholipase activity
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.62
substrate 1-palmitoyl lysophosphatidylcholine
2.448
-
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27.3
substrate palmitoyl-peptide
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 9.3
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pH 5.0: about 30% of maximal activity, pH 9.3: about 35% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
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assay at
40
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lysophospholipase reaction proceeds even at 0C and its rate increases with temperature up to roughly 50C, the optimal temperature is near 40 C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
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Manually annotated by BRENDA team
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hLysoPLA I expression is induced by phorbol 12-myristate 13-acetate
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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fetal
Manually annotated by BRENDA team
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enzyme is also located in mitochondria even in the absence of prenylation
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
42000
determined by SDS-PAGE and Western Blot analysis
130000
determined by gel filtration
25000
x * 25000, SDS-PAGE (52000 for GST-fusion protein)
60000
-
x * 60000, SDS-PAGE
61000
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SDS-PAGE, Flag-tagged fusion protein
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80C, 50 mM Tris/HCl, pH 7.4, more than one year, stable
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
using Sephadex G-75, Mono-S cation-exchange and hydroxyapatite columns
GST affinity chromatography, GST-tag cleaved from GST-fusion protein
using membranes and an anti-Flag column
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed as an N-terminal myc-tagged and C-terminal Flag-tagged fusion protein in HeLa or HEK293 cells. C-terminal Flag-tag is inserted into the prenylation site
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expressed in Escherichia coli BL21(DE3) cells
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expression in HL-60 cells
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GST-fusion protein expressed in Escherichia coli BL21, expressed in HEK-293 cell
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
lipopolysaccharide suppresses APT1 mRNA and protein expression
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S119A
part of the catalytic triad, no activity
additional information
-
C-terminal Flag-tag is inserted into the prenylation site. Mutant enzyme shows lysophospholipase activity indicating that C-terminal processing is not essential for activity
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
the phospholipases and lysophospholipases expressed by eosinophils or other airway cells may represent therapeutic targets for blocking surfactant degradation, dysfunction and peripheral airway closure in asthma