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Information on EC 3.1.1.5 - lysophospholipase
for references in articles please use BRENDA:EC3.1.1.5
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EC Tree 3 Hydrolases
3.1 Acting on ester bonds
3.1.1 Carboxylic-ester hydrolases
3.1.1.5 lysophospholipase
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
- 3.1.1.5
- phospholipid
- venom
- lysophospholipids
-
arachidonic
-
organophosphorus
-
neurotoxic
- phosphatidylethanolamine
- snake
- acetylcholinesterase
-
organophosphate
-
lysophosphatidic
-
ache
-
neuropathic
-
phosphatidic
-
opidn
- polyneuropathy
- esterases
-
deacylation
- hyaluronidase
-
organophosphate-induced
- autotaxin
-
lipolytic
- bothrops
- crotalus
- viper
- lysophosphatidylethanolamine
-
3.1.1.4
- valerate
-
calcium-independent
- monoacylglycerols
- paraoxon
- glycerophosphocholine
- cobra
-
op-induced
- trimeresurus
- phosphorofluoridate
-
ptdcho
- methamidophos
-
patatin-like
-
lipoprotein-associated
-
antivenomics
- bungarus
- lysophosphatidylinositol
- phosphomonoesterase
- lysophosphatidylserine
- cpla2alpha
-
lysopc
-
gxsxg
-
axonopathy
- medicine
-
p-bromophenacyl
showSynonyms
phospholipase a, lysophospholipase, neuropathy target esterase, phospholipase b, lysopld, galectin-10, charcot-leyden crystal protein, lysophospholipase a, lysopl, cpla2gamma, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acyl-protein thioesterase 1
APT1
Charcot-Leyden crystal protein
-
-
-
-
Charcot-Leyden crystal protein homolog
-
-
-
-
CLC
-
-
-
-
cPLA2gamma
-
enzyme also possesses transacylation activity: with addition of lysophosphatidic acid/phosphatidic acid, pH above 8, and elevated temperature markedly increases transacylation activity
eosinophil lysophospholipases
FSH1
Galactin-10
-
-
-
-
Galectin-10
-
-
-
-
hLysoPLA
lecithinase B
-
-
-
-
lecitholipase
-
-
-
-
LPL
LPL1
LPLA
LPLase
LYPLA1
LYPLA2
Lysolecithin acylhydrolase
-
-
-
-
lysolecithinase
-
-
-
-
lysophopholipase L2
-
-
-
-
lysophosphatidase
-
-
-
-
lysophosphatidylcholine hydrolase
-
-
-
-
lysophospholipase
lysophospholipase A
lysophospholipase A1
-
-
-
-
lysophospholipase I
lysophospholipase II
LysoPL
lysoPL2
lysoPLA
lysoPLC
-
enzyme also possesses GPC phoshocholine phosphodiesterase activity and uses glycerophosphorylcholine as a substrate
phosphatidase B
-
-
-
-
phospholipase B
PLB
PLB1
PNPLA7
TAP
thioesterase I/protease I/lysophospholipase L1
additional information
-
lysophospholipase activity of lysophosphatidylcholine/transacylase is smaller than the transacylase activity
acyl-protein thioesterase 1
-
exhibits deacylation activity as well as lysophospholipase activity in vitro
acyl-protein thioesterase 1
-
exhibits deacylation activity as well as lysophospholipase activity in vitro
acyl-protein thioesterase 1
-
exhibits deacylation activity as well as lysophospholipase activity in vitro
APT1
-
APT1 exhibits deacylation activity as well as lysophospholipase activity in vitro
APT1
-
APT1 exhibits deacylation activity as well as lysophospholipase activity in vitro
APT1
-
APT1 exhibits deacylation activity as well as lysophospholipase activity in vitro
phospholipase B
-
-
-
-
phospholipase B
-
enzymes harbors three distinct activities: a sn-1 and sn-2 fatty acid ester hydrolase, a lysophospholipase and a transacylase activity
phospholipase B
enzymes harbors three distinct activities: a sn-1 and sn-2 fatty acid ester hydrolase, a lysophospholipase and a transacylase activity
phospholipase B
-
enzymes harbors three distinct activities: a sn-1 and sn-2 fatty acid ester hydrolase, a lysophospholipase and a transacylase activity
phospholipase B
-
enzymes harbors three distinct activities: a sn-1 and sn-2 fatty acid ester hydrolase, a lysophospholipase and a transacylase activity
TAP
multifunctional enzyme with thioesterase, esterase, arylesterase, protease and lysophosphilipase activities
TAP
multifunctional lysophospholipasethioesterase I/protease I/lysophospholipase L1
thioesterase I/protease I/lysophospholipase L1
multifunctional enzyme with thioesterase, esterase, arylesterase, protease and lysophosphilipase activities
thioesterase I/protease I/lysophospholipase L1
multifunctional lysophospholipase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of carboxylic ester
hydrolysis of carboxylic ester
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
phospholipid remodeling (phosphatidylethanolamine, yeast)
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SYSTEMATIC NAME
IUBMB Comments
2-lysophosphatidylcholine acylhydrolase
-
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CAS REGISTRY NUMBER
COMMENTARY
9001-85-8
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,2-didecanoyl-sn-glycero-3-phosphocholine + H2O
?
-
Substrates: -
Products: -
Products: -
?
1,2-didodecanoyl-sn-glycero-3-phosphocholine + H2O
?
Substrates: -
Products: -
Products: -
?
1,2-dioleoylphosphatidylcholine + H2O
monooleoyl-lysophosphatidylcholine + oleic acid
-
Substrates: 129% of activity with 1,2-dipalmitoylphosphatidylcholine
Products: -
Products: -
?
1,2-dioleoylphosphatidylethanolamine + H2O
monooleoyl-lysophosphatidylethanolamine + oleic acid
-
Substrates: -
Products: 33.5% of activity with 1,2-dipalmitoylphosphatidylcholine
Products: 33.5% of activity with 1,2-dipalmitoylphosphatidylcholine
?
1,2-dioleoylphosphatidylserine + H2O
monooleoyl-lysophosphatidylserine + oleic acid
-
Substrates: -
Products: 22.5% of activity with 1,2-dipalmitoylphosphatidylcholine
Products: 22.5% of activity with 1,2-dipalmitoylphosphatidylcholine
?
1,2-dipalmitoyl-sn-glycero-3-phosphocholine + H2O
1-palmitoyl-sn-glycero-3-phosphocholine + palmitate
-
Substrates: -
Products: -
Products: -
?
1,2-palmitylphosphatidylcholine + H2O
1-palmityl-lysophosphatidylcholine + palmitic acid
-
Substrates: low activity after activating of ExoU with an unknown eukaryotic cell factor
Products: -
Products: -
?
1-acyl-2-lysophosphatidylcholine + H2O
fatty acid + glycerophosphocholine
Substrates: -
Products: -
Products: -
?
1-acyl-2-oleoyl-phosphatidylcholine + H2O
?
-
Substrates: -
Products: -
Products: -
?
1-acyl-glycerophosphoglycerol + H2O
fatty acid + glcyerophosphoglycerol
-
Substrates: -
Products: -
Products: -
?
1-acyl-lysophosphatidylcholine + 1-alkyllysophosphatidylcholine
1-alkyl-2-acyl-phosphatidylcholine + glycerylphosphocholine
-
Substrates: -
Products: -
Products: -
?
1-acyl-sn-glycero-3-phosphate + H2O
fatty acid + glyceryl phosphate
-
Substrates: -
Products: -
Products: -
?
1-arachidonoyl-2-lysophosphatidylcholine + H2O
lysophosphatidylcholine + arachidonic acid
-
Substrates: -
Products: -
Products: -
?
1-dodecanoyl-sn-glycero-3-phosphocholine + H2O
?
Substrates: -
Products: -
Products: -
?
1-hexanoyl-2-lysophosphatidylcholine + H2O
glycerophosphocholine + hexanoate
Substrates: -
Products: -
Products: -
?
1-hexyl-glycerophosphocholine + H2O
hexanoate + glycerophosphocholine
-
Substrates: -
Products: -
Products: -
?
1-lauroyl-sn-glycero-3-phosphocholine + H2O
lauric acid + sn-glycero-3-phosphocholine
-
Substrates: -
Products: -
Products: -
?
1-lauryl-glycerophosphocholine + H2O
laurate + glycerophosphocholine
-
Substrates: -
Products: -
Products: -
?
1-linoleoyl-2-lysophosphatidylcholine + H2O
lysophosphatidylcholine + linoleic acid
-
Substrates: -
Products: -
Products: -
?
1-linoleoyl-sn-glycero-3-phosphocholine + H2O
linoleic acid + glycerophosphorylcholine
-
Substrates: -
Products: -
Products: -
?
1-monopalmitoylglycerol + H2O
glycerol + palmitic acid
-
Substrates: -
Products: lipase activity of LPLA
Products: lipase activity of LPLA
?
1-monopalmitoyllysophosphatidylglycerol + H2O
glycerophosphoglycerol + palmitic acid
Substrates: -
Products: -
Products: -
?
1-myristoyl-2-(4-nitrophenylsuccinyl) phosphatidylcholine + H2O
?
-
Substrates: substrate for Lp-PLA2
Products: -
Products: -
?
1-myristoyl-2-lysophosphatidylcholine + H2O
lysophosphatidylcholine + myristic acid
-
Substrates: -
Products: -
Products: -
?
1-myristoyl-sn-glycero-3-phosphocholine + H2O
myristic acid + sn-glycero-3-phosphocholine
-
Substrates: -
Products: -
Products: -
?
1-O-hexadecyl-2-acetyl-rac-glycero-3-phosphocholine + H2O
1-O-hexadecyl-2-hydroxy-sn-glycero-3-phosphocholine + ?
-
Substrates: substrate for Lp-PLA2
Products: -
Products: -
?
1-O-hexadecyl-2-hydroxy-sn-glycero-3-phosphocholine + H2O
1-(1-hexadecyl)-sn-glycero-3-phosphate + choline
-
Substrates: substrate for LysoPLD
Products: -
Products: -
?
1-octanoyl-sn-glycero-3-phosphocholine + H2O
octanoic acid + sn-glycero-3-phosphocholine
-
Substrates: -
Products: -
Products: -
?
1-oleoyl lysophosphatidylcholine + H2O
glycerophosphocholine + oleate
-
Substrates: 30% of the activity with 1-palmitoyl lysophosphatidylcholine, LPL1
Products: -
Products: -
?
1-oleoyl-2-acetyl-sn-glycero-3-phosphocholine + H2O
?
-
Substrates: -
Products: -
Products: -
?
1-oleoyl-2-lysophosphatidylcholine + H2O
glycerophosphocholine + oleate
Substrates: -
Products: -
Products: -
?
1-oleoyl-2-lysophosphatidylcholine + H2O
glycerophosphocholine + oleic acid
-
Substrates: -
Products: -
Products: -
?
1-oleoyl-2-lysophosphatidylcholine + H2O
glycerophosphorylcholine + oleic acid
-
Substrates: 30% of the activity with 1-palmitoyl lysophosphatidylcholine at pH 5.0, 667% of the activity with 1-palmitoyl lysophosphatidylcholine at pH 7.0
Products: -
Products: -
?
1-oleoyl-glycerophosphocholine + H2O
oleate + glycerophosphocholine
-
Substrates: -
Products: -
Products: -
?
1-oleoyl-lysophosphatidylcholine + H2O
glycerophosphorylcholine + oleic acid
-
Substrates: 194% of activity with 1-palmitoyl-lysophosphatidylcholine
Products: -
Products: -
?
1-oleoyl-sn-glycero-3-phosphoethanolamine + H2O
oleic acid + glycero-3-phosphoethanolamine
1-palmitoyl lysophosphatidylcholine + H2O
glycerophosphocholine + palmitic acid
-
Substrates: -
Products: -
Products: -
?
1-palmitoyl-2-lyso-sn-phosphatidylcholine + H2O
glycerophosphocholine + palmitic acid
-
Substrates: -
Products: -
Products: -
?
1-palmitoyl-2-lysophosphatidylcholine + H2O
glycerophosphocholine + palmitate
Substrates: -
Products: -
Products: -
?
1-palmitoyl-2-lysophosphatidylcholine + H2O
palmitate + glycerophosphocholine
-
Substrates: -
Products: -
Products: -
?
1-palmitoyl-2-oleoylphosphatidylcholine + H2O
lysophosphatidylcholine + ?
-
Substrates: 36% of activity with 1,2-dipalmitoylphosphatidylcholine
Products: -
Products: -
?
1-palmitoyl-glycerophosphocholine + H2O
palmitate + glycerophosphocholine
-
Substrates: -
Products: -
Products: -
?
1-palmitoyl-lysophosphatidylethanolamine + H2O
glycerophosphatidylethanolamine + palmitic acid
1-palmitoyl-lysophosphatidylethanolamine + H2O
glycerophosphoethanolamine + palmitate
-
Substrates: 20% of the activity with 1-palmitoyl lysophosphatidylcholine, LPL1
Products: -
Products: -
?
1-palmitoyl-sn-glycero-3-phosphocholine + H2O
?
Substrates: -
Products: -
Products: -
?
1-palmitoyl-sn-glycero-3-phosphocholine + H2O
glycerophosphocholine + palmitate
Substrates: -
Products: -
Products: -
?
1-palmitoyl-sn-glycero-3-phosphoethanolamine + H2O
palmitic acid + glycero-3-phosphoethanolamine
1-palmitoyl-sn-glycerol + H2O
palmitic acid + glycerol
-
Substrates: -
Products: -
Products: -
?
1-stearoyl-glycerophosphocholine + H2O
stearate + glycerophosphocholine
-
Substrates: -
Products: -
Products: -
?
1-stearoyl-lysophosphatidylcholine + H2O
glycerophosphocholine + stearoyl acid
Substrates: enzyme is specific for sn1-18:0 lysophosphatidylcholines
Products: -
Products: -
?
1-stearoyl-sn-glycero-3-phosphoethanolamine + H2O
stearic acid + glycero-3-phosphoethanolamine
2,3-dipalmitoyl-sn-glycero-1-phosphocholine + H2O
monopalmitoyl-sn-glycero-1-phosphocholine + palmitic acid
2-acylglycerophosphoethanolamine + H2O
fatty acid + glycerylphosphoethanolamine
-
Substrates: -
Products: -
Products: -
?
2-acylglycerophosphoglycerol + H2O
fatty acid + glcyerophosphoglycerol
-
Substrates: -
Products: -
Products: -
?
2-lysophosphatidylcholine + H2O
glycerophosphocholine + a fatty acid
Substrates: -
Products: -
Products: -
?
2-lysophosphatidylcholine + H2O
glycerophosphorylcholine + a carboxylate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl butanoate + H2O
4-nitrophenol + butanoate
-
Substrates: less than 20% of the activity with 4-nitrophenyl palmitate
Products: -
Products: -
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
Substrates: -
Products: -
Products: -
?
4-nitrophenyl dodecanoate + H2O
4-nitrophenol + dodecanoate
-
Substrates: less than 20% of the activity with 4-nitrophenyl palmitate
Products: -
Products: -
?
4-nitrophenyl formate + H2O
4-nitrophenol + formate
-
Substrates: worst substrate
Products: -
Products: -
?
4-nitrophenyl hexanoate + H2O
4-nitrophenol + hexanoate
-
Substrates: -
Products: -
Products: -
?
C10:0-glycero-3-phosphocholine + H2O
?
-
Substrates: 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
Products: -
Products: -
?
C12:0-glycero-3-phosphocholine + H2O
?
-
Substrates: 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
Products: -
Products: -
?
C14:0-glycero-3-phosphocholine + H2O
?
-
Substrates: 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
Products: -
Products: -
?
C18:0-glycero-3-phosphocholine + H2O
?
-
Substrates: 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
Products: -
Products: -
?
C18:1-glycero-3-phosphocholine + H2O
?
-
Substrates: 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
Products: -
Products: -
?
C18:2-glycero-3-phosphocholine + H2O
?
-
Substrates: 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
Products: -
Products: -
?
C8:0-glycero-3-phosphocholine + H2O
?
-
Substrates: 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
Products: -
Products: -
?
dioleoylphosphatidylcholine + H2O
?
-
Substrates: 2% of the activity with dipalmitoylphosphatidylcholine
Products: -
Products: -
?
dioleoylphosphatidylethanolamine + H2O
?
-
Substrates: 11% of the activity with dipalmitoylphosphatidylcholine
Products: -
Products: -
?
dipalmitoylphosphatidylcholine + H2O
?
-
Substrates: -
Products: -
Products: -
?
ghrelin + H2O
des-acyl ghrelin + n-octanoic acid
-
Substrates: -
Products: -
Products: -
?
lysophosphatidylcholine + H2O
glycerophosphorylcholine + a carboxylate
-
Substrates: lysophospholipase A activity
Products: -
Products: -
?
lysophosphatidylcholine + lysophosphatidylcholine
glycerophosphocholine + phosphatidylcholine
lysophosphatidylglycerol + H2O
fatty acid + glycerol
-
Substrates: -
Products: -
Products: -
?
lysophosphatidylinositol + H2O
glycerophosphatidylinositol + a carboxylate
-
Substrates: 78% of activity with 1-palmitoyl-lysophosphatidylcholine
Products: -
Products: -
?
monooleoylglycerol + H2O
oleic acid + glycerol
-
Substrates: -
Products: -
Products: -
?
monopalmitoylglycerol + H2O
palmitic acid + glycerol
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl butyrate
p-nitrophenol + butyrate
Substrates: substrate activity assay
Products: -
Products: -
?
p-nitrophenyl palmitate
p-nitrophenol + palmitate
Substrates: substrate activity assay
Products: -
Products: -
?
palmitoyl-Gialpha1 + H2O
palmitic acid + Gialpha1
-
Substrates: thioesterase activity
Products: -
Products: -
?
palmitoyl-glycero-3-phosphocholine + H2O
glycerophosphocholine + palmitic acid
-
Substrates: -
Products: -
Products: -
?
palmitoyl-peptide + H2O
palmitate + peptide
Substrates: residue 3 to 14 of RGS4 protein with palmitoyl group attached at Cys12 of RGS4 protein
Products: -
Products: -
?
palmitoyllysophosphatidylglycerol + H2O
glycerophosphoglycerol + palmitic acid
-
Substrates: -
Products: -
Products: -
?
phosphatidic acid + H2O
lysophosphatidic acid + ?
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
lysophosphatidylcholine + glycerophosphorylcholine + a carboxylate
phosphatidylcholine + H2O
lysophosphatidylcholine + glycerophosphorylcholine + a fatty acid
Substrates: -
Products: -
Products: -
?
phosphatidylethanolamine + H2O
lysophosphatidylethanolamine + glycerophosphorylethanolamine + a carboxylate
phosphatidylethanolamine + H2O
lysophosphatidylethanolamine + glycerophosphorylethanolamine + a fatty acid
Substrates: -
Products: -
Products: -
?
phosphatidylglycerol + H2O
lysophosphatidylglycerol + a carboxylate
-
Substrates: 94.2% of activity with 1,2-dipalmitoylphosphatidylcholine
Products: -
Products: -
?
phosphatidylinositol + H2O
lysophosphatidylinositol + glycerophosphorylinositol + a carboxylate
phosphatidylserine + H2O
lysophosphatidylserine + glycerophosphorylserine + a fatty acid
Substrates: -
Products: -
Products: -
?
platelet activating factor + H2O
platelet activating factor + a carboxylate
-
Substrates: 8.9% of activity with 1,2-dipalmitoylphosphatidylcholine
Products: -
Products: -
?
sphingomyelin + H2O
?
-
Substrates: 3% of the activity with dipalmitoylphosphatidylcholine
Products: -
Products: -
?
1,2-dioctanoyl-sn-glycero-3-phosphocholine + H2O
?
-
Substrates: -
Products: -
Products: -
?
1,2-dipalmitoyl-sn-glycero-3-phosphocholine + H2O
?
-
Substrates: -
Products: -
Products: -
?
1,2-dipalmitoyl-sn-glycero-3-phosphocholine + H2O
?
-
Substrates: -
Products: -
Products: -
?
1,2-dipalmitoyl-sn-glycero-3-phosphocholine + H2O
?
Substrates: -
Products: -
Products: -
?
1,2-dipalmitoylphosphatidylcholine + H2O
?
-
Substrates: -
Products: -
Products: -
?
1-acyl-sn-glycero-3-phospho-myo-inositol
fatty acid + glycero-3-phospho-myo-inositol
-
Substrates: weak
Products: -
Products: -
?
1-acyl-sn-glycero-3-phospho-myo-inositol
fatty acid + glycero-3-phospho-myo-inositol
-
Substrates: -
Products: -
Products: -
?
1-acyl-sn-glycero-3-phosphocholine + H2O
fatty acid + glycero-3-phosphocholine
-
Substrates: -
Products: -
Products: -
?
1-acyl-sn-glycero-3-phosphocholine + H2O
fatty acid + glycero-3-phosphocholine
-
Substrates: -
Products: -
Products: -
?
1-acyl-sn-glycero-3-phosphocholine + H2O
fatty acid + glycero-3-phosphocholine
-
Substrates: -
Products: -
Products: -
?
1-acyl-sn-glycero-3-phosphoserine + H2O
fatty acid + glycerophosphoserine
-
Substrates: -
Products: -
Products: -
?
1-acyl-sn-glycero-3-phosphoserine + H2O
fatty acid + glycerophosphoserine
-
Substrates: -
Products: -
Products: -
?
1-acyl-sn-glycero-3-phosphoserine + H2O
fatty acid + glycerophosphoserine
-
Substrates: -
Products: -
Products: -
?
1-acylglycerophosphoethanolamine + H2O
fatty acid + glycerylphosphoethanolamine
-
Substrates: -
Products: -
Products: -
?
1-acylglycerophosphoethanolamine + H2O
fatty acid + glycerylphosphoethanolamine
-
Substrates: -
Products: -
Products: -
?
1-oleoyl-sn-glycero-3-phosphocholine + H2O
oleic acid + glycerophosphorylcholine
-
Substrates: -
Products: -
Products: -
?
1-oleoyl-sn-glycero-3-phosphocholine + H2O
oleic acid + glycerophosphorylcholine
-
Substrates: -
Products: -
Products: -
?
1-oleoyl-sn-glycero-3-phosphocholine + H2O
oleic acid + glycerophosphorylcholine
-
Substrates: -
Products: -
Products: -
?
1-oleoyl-sn-glycero-3-phosphoethanolamine + H2O
oleic acid + glycero-3-phosphoethanolamine
-
Substrates: -
Products: -
Products: -
?
1-oleoyl-sn-glycero-3-phosphoethanolamine + H2O
oleic acid + glycero-3-phosphoethanolamine
-
Substrates: -
Products: -
Products: -
?
1-oleoyl-sn-glycero-3-phosphoethanolamine + H2O
oleic acid + glycero-3-phosphoethanolamine
-
Substrates: weak
Products: -
Products: -
?
1-oleoyl-sn-glycero-3-phosphoethanolamine + H2O
oleic acid + glycero-3-phosphoethanolamine
-
Substrates: -
Products: -
Products: -
?
1-palmitoyl lysophosphatidylcholine + H2O
glycerophosphocholine + palmitate
-
Substrates: preferred substrate, LPL1
Products: -
Products: -
?
1-palmitoyl lysophosphatidylcholine + H2O
glycerophosphocholine + palmitate
Substrates: -
Products: -
Products: -
?
1-palmitoyl-2-acetyl-sn-glycero-3-phosphocholine + H2O
?
-
Substrates: -
Products: -
Products: -
?
1-palmitoyl-2-acetyl-sn-glycero-3-phosphocholine + H2O
?
-
Substrates: -
Products: -
Products: -
?
1-palmitoyl-2-lysophosphatidylcholine + H2O
?
Substrates: -
Products: -
Products: -
?
1-palmitoyl-2-lysophosphatidylcholine + H2O
glycerophosphocholine + palmitic acid
-
Substrates: -
Products: -
Products: -
?
1-palmitoyl-2-lysophosphatidylcholine + H2O
glycerophosphocholine + palmitic acid
-
Substrates: -
Products: -
Products: -
?
1-palmitoyl-lysophosphatidylcholine + H2O
glycerophosphocholine + palmitic acid
-
Substrates: -
Products: -
Products: -
?
1-palmitoyl-lysophosphatidylcholine + H2O
glycerophosphocholine + palmitic acid
Substrates: -
Products: -
Products: -
?
1-palmitoyl-lysophosphatidylcholine + H2O
glycerophosphocholine + palmitic acid
-
Substrates: -
Products: -
Products: -
?
1-palmitoyl-lysophosphatidylcholine + H2O
glycerophosphocholine + palmitic acid
-
Substrates: -
Products: -
Products: -
?
1-palmitoyl-lysophosphatidylethanolamine + H2O
glycerophosphatidylethanolamine + palmitic acid
-
Substrates: as active as 1-palmitoyl lysophosphatidylcholine at pH 7.0
Products: -
Products: -
?
1-palmitoyl-lysophosphatidylethanolamine + H2O
glycerophosphatidylethanolamine + palmitic acid
-
Substrates: 29% of activity with 1-palmitoyl-lysophosphatidylcholine
Products: -
Products: -
?
1-palmitoyl-sn-glycero-3-phosphocholine + H2O
palmitic acid + glycero-3-phosphocholine
-
Substrates: -
Products: -
Products: -
?
1-palmitoyl-sn-glycero-3-phosphocholine + H2O
palmitic acid + glycero-3-phosphocholine
-
Substrates: -
Products: -
Products: -
?
1-palmitoyl-sn-glycero-3-phosphocholine + H2O
palmitic acid + glycero-3-phosphocholine
-
Substrates: -
Products: -
Products: -
?
1-palmitoyl-sn-glycero-3-phosphocholine + H2O
palmitic acid + glycero-3-phosphocholine
-
Substrates: -
Products: -
Products: -
?
1-palmitoyl-sn-glycero-3-phosphocholine + H2O
palmitic acid + glycero-3-phosphocholine
-
Substrates: -
Products: -
Products: -
?
1-palmitoyl-sn-glycero-3-phosphocholine + H2O
palmitic acid + glycero-3-phosphocholine
-
Substrates: -
Products: -
Products: -
?
1-palmitoyl-sn-glycero-3-phosphocholine + H2O
palmitic acid + glycero-3-phosphocholine
-
Substrates: -
Products: -
Products: -
?
1-palmitoyl-sn-glycero-3-phosphoethanolamine + H2O
palmitic acid + glycero-3-phosphoethanolamine
-
Substrates: -
Products: -
Products: -
?
1-palmitoyl-sn-glycero-3-phosphoethanolamine + H2O
palmitic acid + glycero-3-phosphoethanolamine
-
Substrates: -
Products: -
Products: -
?
1-palmitoyl-sn-glycero-3-phosphoethanolamine + H2O
palmitic acid + glycero-3-phosphoethanolamine
-
Substrates: -
Products: -
Products: -
?
1-palmitoyl-sn-glycero-3-phosphoethanolamine + H2O
palmitic acid + glycero-3-phosphoethanolamine
-
Substrates: weak
Products: -
Products: -
?
1-palmitoyl-sn-glycero-3-phosphoethanolamine + H2O
palmitic acid + glycero-3-phosphoethanolamine
-
Substrates: -
Products: -
Products: -
?
1-palmitoyl-sn-glycero-3-phosphoserine + H2O
glycerophosphoserine + palmitic acid
-
Substrates: as active as 1-palmitoyl lysophosphatidylcholine at pH 7.0, 70% of the activity with 1-palmitoyl lysophosphatidylcholine at pH 5.0
Products: -
Products: -
?
1-palmitoyl-sn-glycero-3-phosphoserine + H2O
glycerophosphoserine + palmitic acid
-
Substrates: 3.8% of activity with 1-palmitoyl-lysophosphatidylcholine
Products: -
Products: -
?
1-stearoyl-sn-glycero-3-phosphocholine + H2O
stearic acid + glycerophosphorylcholine
-
Substrates: -
Products: -
Products: -
?
1-stearoyl-sn-glycero-3-phosphocholine + H2O
stearic acid + glycerophosphorylcholine
-
Substrates: -
Products: -
Products: -
?
1-stearoyl-sn-glycero-3-phosphoethanolamine + H2O
stearic acid + glycero-3-phosphoethanolamine
-
Substrates: -
Products: -
Products: -
?
1-stearoyl-sn-glycero-3-phosphoethanolamine + H2O
stearic acid + glycero-3-phosphoethanolamine
-
Substrates: -
Products: -
Products: -
?
1-stearoyl-sn-glycero-3-phosphoethanolamine + H2O
stearic acid + glycero-3-phosphoethanolamine
-
Substrates: -
Products: -
Products: -
?
2,3-dipalmitoyl-sn-glycero-1-phosphocholine + H2O
monopalmitoyl-sn-glycero-1-phosphocholine + palmitic acid
-
Substrates: -
Products: -
Products: -
?
2,3-dipalmitoyl-sn-glycero-1-phosphocholine + H2O
monopalmitoyl-sn-glycero-1-phosphocholine + palmitic acid
-
Substrates: -
Products: -
Products: -
?
2-acylglycerophosphocholine + H2O
fatty acid + glycerylphosphocholine
-
Substrates: -
Products: -
Products: -
?
2-acylglycerophosphocholine + H2O
fatty acid + glycerylphosphocholine
-
Substrates: 2-acyl-sn-glycero-3-phosphocholine
Products: -
Products: -
?
2-lysophosphatidylcholine + H2O
glycerophosphocholine + a carboxylate
-
Substrates: -
Products: -
Products: -
?
2-lysophosphatidylcholine + H2O
glycerophosphocholine + a carboxylate
-
Substrates: -
Products: -
Products: -
?
2-lysophosphatidylcholine + H2O
glycerophosphocholine + a carboxylate
-
Substrates: -
Products: -
Products: -
?
2-lysophosphatidylcholine + H2O
glycerophosphocholine + a carboxylate
Substrates: enzyme has also lysophospholipase transcylase activity
Products: -
Products: -
?
2-lysophosphatidylcholine + H2O
glycerophosphocholine + a carboxylate
Substrates: -
Products: -
Products: -
?
2-lysophosphatidylcholine + H2O
glycerophosphocholine + a carboxylate
-
Substrates: -
Products: -
Products: -
?
2-lysophosphatidylcholine + H2O
glycerophosphocholine + a carboxylate
Substrates: -
Products: -
Products: -
?
2-lysophosphatidylcholine + H2O
glycerophosphocholine + a carboxylate
-
Substrates: -
Products: -
Products: -
?
2-lysophosphatidylcholine + H2O
glycerophosphocholine + a carboxylate
Substrates: -
Products: -
Products: -
?
2-lysophosphatidylcholine + H2O
glycerophosphocholine + a carboxylate
-
Substrates: -
Products: -
Products: -
?
2-lysophosphatidylcholine + H2O
glycerophosphocholine + a carboxylate
Substrates: -
Products: -
Products: -
?
2-lysophosphatidylcholine + H2O
glycerophosphocholine + a carboxylate
-
Substrates: -
Products: -
Products: -
?
2-lysophosphatidylcholine + H2O
glycerophosphocholine + a carboxylate
-
Substrates: -
Products: -
Products: -
?
2-lysophosphatidylcholine + H2O
glycerophosphocholine + a carboxylate
W8R447
Substrates: -
Products: -
Products: -
?
2-lysophosphatidylcholine + H2O
glycerophosphocholine + a carboxylate
-
Substrates: -
Products: -
Products: -
?
2-lysophosphatidylcholine + H2O
glycerophosphocholine + a carboxylate
-
Substrates: -
Products: -
Products: -
?
2-lysophosphatidylcholine + H2O
glycerophosphocholine + a carboxylate
-
Substrates: -
Products: -
Products: -
?
2-lysophosphatidylcholine + H2O
glycerophosphocholine + a carboxylate
-
Substrates: -
Products: -
Products: -
?
2-lysophosphatidylcholine + H2O
glycerophosphocholine + a carboxylate
-
Substrates: -
Products: -
Products: -
?
2-palmitoyl-sn-glycero-3-phosphocholine + H2O
palmitic acid + glycero-3-phosphocholine
-
Substrates: -
Products: -
Products: -
?
2-palmitoyl-sn-glycero-3-phosphocholine + H2O
palmitic acid + glycero-3-phosphocholine
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl benzoate + H2O
4-nitrophenol + benzoate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl benzoate + H2O
4-nitrophenol + benzoate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
Substrates: 6.84% activity compared to 4-nitrophenyl palmitate
Products: -
Products: -
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
Substrates: relative activity: 0.45%
Products: -
Products: -
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
Substrates: best substrate
Products: -
Products: -
?
4-nitrophenyl decanoate + H2O
4-nitrophenol + decanoate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl decanoate + H2O
4-nitrophenol + decanoate
-
Substrates: less than 20% of the activity with 4-nitrophenyl palmitate
Products: -
Products: -
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
Substrates: 23.21% activity compared to 4-nitrophenyl palmitate
Products: -
Products: -
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
Substrates: relative activity: 7.56%
Products: -
Products: -
?
4-nitrophenyl myristate + H2O
4-nitrophenol + myristate
-
Substrates: best substrate
Products: -
Products: -
?
4-nitrophenyl myristate + H2O
4-nitrophenol + myristate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl myristate + H2O
4-nitrophenol + myristate
-
Substrates: 58.61% activity compared to 4-nitrophenyl palmitate
Products: -
Products: -
?
4-nitrophenyl myristate + H2O
4-nitrophenol + myristate
Substrates: relative activity: 12.77%
Products: -
Products: -
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
Substrates: best substrate
Products: -
Products: -
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
Substrates: best substrate
Products: -
Products: -
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
Substrates: 100% activity
Products: -
Products: -
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
Substrates: relative activity: 100%
Products: -
Products: -
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
Substrates: worst substrate
Products: -
Products: -
?
4-nitrophenyl stearate + H2O
4-nitrophenol + stearate
-
Substrates: worst substrate
Products: -
Products: -
?
4-nitrophenyl stearate + H2O
4-nitrophenol + stearate
-
Substrates: second best substrate
Products: -
Products: -
?
4-nitrophenyl stearate + H2O
4-nitrophenol + stearate
-
Substrates: second best substrate
Products: -
Products: -
?
4-nitrophenyl stearate + H2O
4-nitrophenol + stearate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl stearate + H2O
4-nitrophenol + stearate
Substrates: relative activity: 56.69%
Products: -
Products: -
?
lysophosphatidylcholine + H2O
glycerophosphorylcholine + unesterified fatty acid
-
Substrates: -
Products: -
Products: -
?
lysophosphatidylcholine + H2O
glycerophosphorylcholine + unesterified fatty acid
-
Substrates: -
Products: -
Products: -
?
lysophosphatidylcholine + H2O
glycerophosphorylcholine + unesterified fatty acid
-
Substrates: -
Products: -
Products: -
?
lysophosphatidylcholine + H2O
glycerophosphorylcholine + unesterified fatty acid
-
Substrates: myristoyllysophosphatidylcholine is hydrolyzed 50% better than the longer chain palmitoyllysophosphatidylcholine
Products: -
Products: -
?
lysophosphatidylcholine + H2O
glycerophosphorylcholine + unesterified fatty acid
Substrates: -
Products: -
Products: -
?
lysophosphatidylcholine + H2O
glycerophosphorylcholine + unesterified fatty acid
-
Substrates: -
Products: -
Products: -
?
lysophosphatidylcholine + H2O
glycerophosphorylcholine + unesterified fatty acid
-
Substrates: -
Products: -
Products: -
?
lysophosphatidylcholine + H2O
glycerophosphorylcholine + unesterified fatty acid
Substrates: -
Products: -
Products: -
?
lysophosphatidylcholine + H2O
glycerophosphorylcholine + unesterified fatty acid
-
Substrates: -
Products: glycerophosphocholine + fatty acid
Products: glycerophosphocholine + fatty acid
?
lysophosphatidylcholine + H2O
glycerophosphorylcholine + unesterified fatty acid
-
Substrates: -
Products: -
Products: -
?
lysophosphatidylcholine + H2O
glycerophosphorylcholine + unesterified fatty acid
-
Substrates: 249% of the activity with phosphatidylcholine
Products: -
Products: -
?
lysophosphatidylcholine + lysophosphatidylcholine
glycerophosphocholine + phosphatidylcholine
-
Substrates: -
Products: -
Products: -
?
lysophosphatidylcholine + lysophosphatidylcholine
glycerophosphocholine + phosphatidylcholine
-
Substrates: slight preference for palmitate over stearate and laurate to be incorporated into phosphatidylcholine. No preference for palmitate over myristate
Products: -
Products: -
?
lysophosphatidylethanolamine + H2O
fatty acid + glycerylphosphoethanolamine
Substrates: -
Products: -
Products: -
?
lysophosphatidylethanolamine + H2O
fatty acid + glycerylphosphoethanolamine
-
Substrates: 27% of the activity with phosphatidylcholine
Products: -
Products: -
?
lysophosphatidylserine + H2O
glycerophosphorylserine + a carboxylate
-
Substrates: -
Products: -
Products: -
?
lysophosphatidylserine + H2O
glycerophosphorylserine + a carboxylate
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
Substrates: substrate activity assay
Products: -
Products: -
?
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
-
Substrates: no activity detectable
Products: -
Products: -
?
phosphatidic acid + H2O
?
-
Substrates: 62% of the activity with phosphatidylcholine
Products: -
Products: -
?
phosphatidylcholine + H2O
lysophosphatidylcholine + a carboxylate
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
lysophosphatidylcholine + a carboxylate
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
lysophosphatidylcholine + glycerophosphorylcholine + a carboxylate
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
lysophosphatidylcholine + glycerophosphorylcholine + a carboxylate
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
lysophosphatidylcholine + glycerophosphorylcholine + a carboxylate
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
lysophosphatidylcholine + glycerophosphorylcholine + a carboxylate
-
Substrates: hydrolysis of the 1-acly ester bond and the 2-acyl ester bond, phospholipase B activity
Products: -
Products: -
?
phosphatidylcholine + H2O
lysophosphatidylcholine + glycerophosphorylcholine + a carboxylate
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
lysophosphatidylcholine + glycerophosphorylcholine + a carboxylate
-
Substrates: phospholipase B activity, hydrolyzes the acyl ester bonds sequentially, first the 2-acyl group and then the 1-acyl group
Products: -
Products: -
?
phosphatidylcholine + H2O
lysophosphatidylcholine + glycerophosphorylcholine + a carboxylate
-
Substrates: -
Products: -
Products: -
?
phosphatidylethanolamine + H2O
lysophosphatidylethanolamine + glycerophosphorylethanolamine + a carboxylate
-
Substrates: -
Products: -
Products: -
?
phosphatidylethanolamine + H2O
lysophosphatidylethanolamine + glycerophosphorylethanolamine + a carboxylate
-
Substrates: hydrolysis and acyl transfer
Products: -
Products: -
?
phosphatidylethanolamine + H2O
lysophosphatidylethanolamine + glycerophosphorylethanolamine + a carboxylate
-
Substrates: -
Products: -
Products: -
?
phosphatidylinositol + H2O
lysophophatidylinositol + a carboxylate
-
Substrates: 15.6% of activity with 1,2-dipalmitoylphosphatidylcholine
Products: -
Products: -
?
phosphatidylinositol + H2O
lysophophatidylinositol + a carboxylate
Substrates: -
Products: -
Products: -
?
phosphatidylinositol + H2O
lysophosphatidylinositol + glycerophosphorylinositol + a carboxylate
-
Substrates: -
Products: -
Products: -
?
phosphatidylinositol + H2O
lysophosphatidylinositol + glycerophosphorylinositol + a carboxylate
-
Substrates: -
Products: -
Products: -
?
phosphatidylinositol + H2O
lysophosphatidylinositol + glycerophosphorylinositol + a carboxylate
-
Substrates: 819% of the activity with phosphatidylcholine
Products: -
Products: -
?
phosphatidylserine + H2O
lysophosphatidylserine + glycerophosphorylserine + a carboxylate
-
Substrates: -
Products: -
Products: -
?
phosphatidylserine + H2O
lysophosphatidylserine + glycerophosphorylserine + a carboxylate
-
Substrates: -
Products: -
Products: -
?
phosphatidylserine + H2O
lysophosphatidylserine + glycerophosphorylserine + a carboxylate
-
Substrates: 22% of the activity with phosphatidylcholine
Products: -
Products: -
?
additional information
?
-
-
Substrates: acyl-CoA-binding protein 2 can bind both lysophosphatidylcholine and lysophospholipase 2 to promote the degradation of lysophosphatidylcholine in response to Cd2+-induced oxidative stress
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with tributyrin, tricaprilin or triolein
Products: -
Products: -
?
additional information
?
-
-
Substrates: LipC cleaves both ester linkages of the sn-1 and sn-2 positions of phospholipids (phospholipase B activity)
Products: -
Products: -
?
additional information
?
-
-
Substrates: the LPL1 protein only possesses lysophospholipase and transacylase activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: PLB1 shows phospholipase B activity, lysophospholipase activity and transacylase activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: the LPL1 protein only possesses lysophospholipase and transacylase activity
Products: -
Products: -
?
additional information
?
-
Substrates: phospholipase B is necessary for the initiation of pulmonary infection by Cryptpococcus neoformans and for dissemination from the lung via the lymphatics. PLB1 plays a role in the binding of Cryptpococcus neoformans to host lung epithelial cells, possibly due to production of fatty acids from plasma memrane and/or surfactant by PLB activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: phospholipase B is necessary for the initiation of pulmonary infection by Cryptpococcus neoformans and for dissemination from the lung via the lymphatics. PLB1 plays a role in the binding of Cryptpococcus neoformans to host lung epithelial cells, possibly due to production of fatty acids from plasma memrane and/or surfactant by PLB activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: phospholipase B1 is implicated in transcellular metabolism of macrophage-derived lipids. During both logarithmic and stationary phases of growth, the physiologically relevant phospholipids, dipalmitoyl phosphatidylcholine (DPPC) and dioleoyl phosphatidylcholine, are taken up and metabolized via PLB1
Products: -
Products: -
?
additional information
?
-
Substrates: substrate specificities of Escherichia coli thioesterase I/protease I/lysophospholipase L1 are governed by its switch loop movement
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificities of Escherichia coli thioesterase I/protease I/lysophospholipase L1 are governed by its switch loop movement
Products: -
Products: -
?
additional information
?
-
Substrates: combined activities of secretory phospholipases and eosinophil lysophospholipases induce pulmonary surfactant dysfunction by phospholipid hydrolysis
Products: -
Products: -
?
additional information
?
-
-
Substrates: human 60-kDa lysophospholipase contains an N-terminal L-asparaginase domain that is allosterically regulated by L-asparagine
Products: -
Products: -
?
additional information
?
-
Substrates: the iPLA2gamma activity has the ability to cleave phospholipid acyl chains from both sn-1 and sn-2 positions of phospholipids (but not in dilyso-cardiolipin). Thus iPLA2gamma also cleaves off the sn-1 saturated side-chain. A fatty acid (FA) cleavage pattern can be indicative of the given PLA2 isoform
Products: -
Products: -
-
additional information
?
-
Substrates: the iPLA2gamma activity has the ability to cleave phospholipid acyl chains from both sn-1 and sn-2 positions of phospholipids (but not in dilyso-cardiolipin). Thus iPLA2gamma also cleaves off the sn-1 saturated side-chain. A fatty acid (FA) cleavage pattern can be indicative of the given PLA2 isoform
Products: -
Products: -
-
additional information
?
-
Substrates: the iPLA2gamma activity has the ability to cleave phospholipid acyl chains from both sn-1 and sn-2 positions of phospholipids (but not in dilyso-cardiolipin). Thus iPLA2gamma also cleaves off the sn-1 saturated side-chain. A fatty acid (FA) cleavage pattern can be indicative of the given PLA2 isoform
Products: -
Products: -
-
additional information
?
-
Substrates: the iPLA2delta activity cleaves phospholipid acyl chains from both sn-1 and sn-2 positions of and fatty acids. A fatty acid (FA) cleavage pattern can be indicative of the given PLA2 isoform
Products: -
Products: -
-
additional information
?
-
Substrates: the iPLA2delta activity cleaves phospholipid acyl chains from both sn-1 and sn-2 positions of and fatty acids. A fatty acid (FA) cleavage pattern can be indicative of the given PLA2 isoform
Products: -
Products: -
-
additional information
?
-
Substrates: the iPLA2delta activity cleaves phospholipid acyl chains from both sn-1 and sn-2 positions of and fatty acids. A fatty acid (FA) cleavage pattern can be indicative of the given PLA2 isoform
Products: -
Products: -
-
additional information
?
-
Substrates: the iPLA2theta activity cleaves phospholipid acyl chains from both sn-1 and sn-2 positions of and fatty acids. A fatty acid (FA) cleavage pattern can be indicative of the given PLA2 isoform
Products: -
Products: -
-
additional information
?
-
Substrates: the iPLA2theta activity cleaves phospholipid acyl chains from both sn-1 and sn-2 positions of and fatty acids. A fatty acid (FA) cleavage pattern can be indicative of the given PLA2 isoform
Products: -
Products: -
-
additional information
?
-
Substrates: the iPLA2theta activity cleaves phospholipid acyl chains from both sn-1 and sn-2 positions of and fatty acids. A fatty acid (FA) cleavage pattern can be indicative of the given PLA2 isoform
Products: -
Products: -
-
additional information
?
-
-
Substrates: the function of the enzyme is directed to the disposal of the starch inclusion lipids during their release from the starch matrix during germination
Products: -
Products: -
?
additional information
?
-
-
Substrates: lysophospholipase activity of lysophosphatidylcholine/transacylase is smaller than the transacylase activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: global regulatory proteins LetA and RpoS control lysophospholipase A
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme encoded by the gene plaB is a phospholipase A and a lysophospholipase A
Products: -
Products: -
?
additional information
?
-
-
Substrates: global regulatory proteins LetA and RpoS control lysophospholipase A
Products: -
Products: -
?
additional information
?
-
-
Substrates: loss of lysophospholipase 3 increases atherosclerosis in apolipoprotein E-deficient mice. Even in a severe model of atherosclerosis, LCAT-like lysophospholipase exhibits a protective effect on atheroma formation at all stages and throughout the aortic tree in mice fed on normal diet
Products: -
Products: -
?
additional information
?
-
-
Substrates: combined activities of secretory phospholipases and eosinophil lysophospholipases induce pulmonary surfactant dysfunction by phospholipid hydrolysis
Products: -
Products: -
?
additional information
?
-
-
Substrates: hydrolyzes sn-1 esters in lysophosphatidylcholine and lysophosphatidic acid
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-acyl-2-lysophosphatidylcholine + H2O
fatty acid + glycerophosphocholine
Substrates: -
Products: -
Products: -
?
1-monopalmitoyllysophosphatidylglycerol + H2O
glycerophosphoglycerol + palmitic acid
Substrates: -
Products: -
Products: -
?
1-palmitoyl-2-lysophosphatidylcholine + H2O
glycerophosphocholine + palmitic acid
-
Substrates: -
Products: -
Products: -
?
1-palmitoyl-sn-glycero-3-phosphocholine + H2O
glycerophosphocholine + palmitate
Substrates: -
Products: -
Products: -
?
lysophosphatidylcholine + H2O
glycerophosphorylcholine + a carboxylate
-
Substrates: lysophospholipase A activity
Products: -
Products: -
?
2-lysophosphatidylcholine + H2O
glycerophosphocholine + a carboxylate
-
Substrates: -
Products: -
Products: -
?
2-lysophosphatidylcholine + H2O
glycerophosphocholine + a carboxylate
-
Substrates: -
Products: -
Products: -
?
2-lysophosphatidylcholine + H2O
glycerophosphocholine + a carboxylate
Substrates: -
Products: -
Products: -
?
2-lysophosphatidylcholine + H2O
glycerophosphocholine + a carboxylate
-
Substrates: -
Products: -
Products: -
?
2-lysophosphatidylcholine + H2O
glycerophosphocholine + a carboxylate
Substrates: -
Products: -
Products: -
?
2-lysophosphatidylcholine + H2O
glycerophosphocholine + a carboxylate
Substrates: -
Products: -
Products: -
?
2-lysophosphatidylcholine + H2O
glycerophosphocholine + a carboxylate
-
Substrates: -
Products: -
Products: -
?
2-lysophosphatidylcholine + H2O
glycerophosphocholine + a carboxylate
Substrates: -
Products: -
Products: -
?
2-lysophosphatidylcholine + H2O
glycerophosphocholine + a carboxylate
-
Substrates: -
Products: -
Products: -
?
2-lysophosphatidylcholine + H2O
glycerophosphocholine + a carboxylate
-
Substrates: -
Products: -
Products: -
?
2-lysophosphatidylcholine + H2O
glycerophosphocholine + a carboxylate
W8R447
Substrates: -
Products: -
Products: -
?
2-lysophosphatidylcholine + H2O
glycerophosphocholine + a carboxylate
-
Substrates: -
Products: -
Products: -
?
2-lysophosphatidylcholine + H2O
glycerophosphocholine + a carboxylate
-
Substrates: -
Products: -
Products: -
?
2-lysophosphatidylcholine + H2O
glycerophosphocholine + a carboxylate
-
Substrates: -
Products: -
Products: -
?
2-lysophosphatidylcholine + H2O
glycerophosphocholine + a carboxylate
-
Substrates: -
Products: -
Products: -
?
2-lysophosphatidylcholine + H2O
glycerophosphocholine + a carboxylate
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
lysophosphatidylcholine + a carboxylate
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
lysophosphatidylcholine + a carboxylate
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: acyl-CoA-binding protein 2 can bind both lysophosphatidylcholine and lysophospholipase 2 to promote the degradation of lysophosphatidylcholine in response to Cd2+-induced oxidative stress
Products: -
Products: -
?
additional information
?
-
Substrates: phospholipase B is necessary for the initiation of pulmonary infection by Cryptpococcus neoformans and for dissemination from the lung via the lymphatics. PLB1 plays a role in the binding of Cryptpococcus neoformans to host lung epithelial cells, possibly due to production of fatty acids from plasma memrane and/or surfactant by PLB activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: phospholipase B is necessary for the initiation of pulmonary infection by Cryptpococcus neoformans and for dissemination from the lung via the lymphatics. PLB1 plays a role in the binding of Cryptpococcus neoformans to host lung epithelial cells, possibly due to production of fatty acids from plasma memrane and/or surfactant by PLB activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: phospholipase B1 is implicated in transcellular metabolism of macrophage-derived lipids. During both logarithmic and stationary phases of growth, the physiologically relevant phospholipids, dipalmitoyl phosphatidylcholine (DPPC) and dioleoyl phosphatidylcholine, are taken up and metabolized via PLB1
Products: -
Products: -
?
additional information
?
-
Substrates: combined activities of secretory phospholipases and eosinophil lysophospholipases induce pulmonary surfactant dysfunction by phospholipid hydrolysis
Products: -
Products: -
?
additional information
?
-
Substrates: the iPLA2gamma activity has the ability to cleave phospholipid acyl chains from both sn-1 and sn-2 positions of phospholipids (but not in dilyso-cardiolipin). Thus iPLA2gamma also cleaves off the sn-1 saturated side-chain. A fatty acid (FA) cleavage pattern can be indicative of the given PLA2 isoform
Products: -
Products: -
-
additional information
?
-
Substrates: the iPLA2gamma activity has the ability to cleave phospholipid acyl chains from both sn-1 and sn-2 positions of phospholipids (but not in dilyso-cardiolipin). Thus iPLA2gamma also cleaves off the sn-1 saturated side-chain. A fatty acid (FA) cleavage pattern can be indicative of the given PLA2 isoform
Products: -
Products: -
-
additional information
?
-
Substrates: the iPLA2gamma activity has the ability to cleave phospholipid acyl chains from both sn-1 and sn-2 positions of phospholipids (but not in dilyso-cardiolipin). Thus iPLA2gamma also cleaves off the sn-1 saturated side-chain. A fatty acid (FA) cleavage pattern can be indicative of the given PLA2 isoform
Products: -
Products: -
-
additional information
?
-
Substrates: the iPLA2delta activity cleaves phospholipid acyl chains from both sn-1 and sn-2 positions of and fatty acids. A fatty acid (FA) cleavage pattern can be indicative of the given PLA2 isoform
Products: -
Products: -
-
additional information
?
-
Substrates: the iPLA2delta activity cleaves phospholipid acyl chains from both sn-1 and sn-2 positions of and fatty acids. A fatty acid (FA) cleavage pattern can be indicative of the given PLA2 isoform
Products: -
Products: -
-
additional information
?
-
Substrates: the iPLA2delta activity cleaves phospholipid acyl chains from both sn-1 and sn-2 positions of and fatty acids. A fatty acid (FA) cleavage pattern can be indicative of the given PLA2 isoform
Products: -
Products: -
-
additional information
?
-
Substrates: the iPLA2theta activity cleaves phospholipid acyl chains from both sn-1 and sn-2 positions of and fatty acids. A fatty acid (FA) cleavage pattern can be indicative of the given PLA2 isoform
Products: -
Products: -
-
additional information
?
-
Substrates: the iPLA2theta activity cleaves phospholipid acyl chains from both sn-1 and sn-2 positions of and fatty acids. A fatty acid (FA) cleavage pattern can be indicative of the given PLA2 isoform
Products: -
Products: -
-
additional information
?
-
Substrates: the iPLA2theta activity cleaves phospholipid acyl chains from both sn-1 and sn-2 positions of and fatty acids. A fatty acid (FA) cleavage pattern can be indicative of the given PLA2 isoform
Products: -
Products: -
-
additional information
?
-
-
Substrates: the function of the enzyme is directed to the disposal of the starch inclusion lipids during their release from the starch matrix during germination
Products: -
Products: -
?
additional information
?
-
-
Substrates: global regulatory proteins LetA and RpoS control lysophospholipase A
Products: -
Products: -
?
additional information
?
-
-
Substrates: global regulatory proteins LetA and RpoS control lysophospholipase A
Products: -
Products: -
?
additional information
?
-
-
Substrates: loss of lysophospholipase 3 increases atherosclerosis in apolipoprotein E-deficient mice. Even in a severe model of atherosclerosis, LCAT-like lysophospholipase exhibits a protective effect on atheroma formation at all stages and throughout the aortic tree in mice fed on normal diet
Products: -
Products: -
?
additional information
?
-
-
Substrates: combined activities of secretory phospholipases and eosinophil lysophospholipases induce pulmonary surfactant dysfunction by phospholipid hydrolysis
Products: -
Products: -
?
additional information
?
-
-
Substrates: hydrolyzes sn-1 esters in lysophosphatidylcholine and lysophosphatidic acid
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Al3+
Ca2+
CaCl2
-
10 mM, 22% inhibition of phospholipase B activity, slight activation of lysophospholipase activity, to 8% at pH 5.0 and 4% at pH 7.0
Cu2+
Fe2+
Fe3+
Ni2+
Zn2+
additional information
Al3+
strong activation at pH 8.0, optimal concentration is 20 mM
Ca2+
-
10 mM, stimulates to 260% of control at pH 7.0, but not at pH 5.0, LPL1
additional information
activity at pH 3.0 is independent on metal ions
additional information
-
activity at pH 3.0 is independent on metal ions
additional information
-
the enzyme activity is independent of the presence of metal ions
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(E)-6-(bromomethylene)-3-(1-naphthalenyl)-2H-tetrahydropyran-2-one
also termed R-bromoenol lactone (R-BEL), a highly selective inhibitor of iPLA2gamma, whereas the S-enantiomer (S-BEL) is ineffective, but is highly selective for iPLA2beta
1-palmitoyl lysophosphatidylcholine
competitive inhibitor for acylprotein thioesterase activity
1-[2-[2-hydroxy-3-(piperidin-1-yl)propoxy]phenyl]-2-phenylethan-1-one
-
AACOCF3
-
a trifluoromethyl ketone analog of arachidonic acid, uncompetitive
bis(p-nitrophenyl)phosphate
-
0.01 mM, 8% inhibition of lysophospholipase I and 61% inhibition of lysophospholipase II
CaCl2
-
10 mM, 22% inhibition of phospholipase B activity, slight activation of lysophospholipase activity
carnitine
-
10 mM, 38% inhibition of phospholipase B activity; 10 mM, 9% inhibition at pH 7.0, LPL1
chlorpromazine
-
at low concentrations significantly stimulates phospholipase B activity of native enzyme, strong stimulation at high concentrations
dipalmitoyl phosphatidylcholine
-
0.5 mM, 84% inhibition at pH 5.0, 50% inhibition at pH 7.0, LPL 1
dipalmitoylphosphatidylcholine
-
0.5 mM, 89% inhibition of lysophospholipase at pH 5.0, 82% inhibition of lysophospholipase at pH 7.0
FeCl3
-
10 mM, 39% inhibition at pH 5.0, 38% inhibition at pH 7.0, LPL1; 10 mM, 80% inhibiotion of phospholipase B activity, 17% inhibition of lysophospholipase activity at pH 5.0, 29% in inhibition of lysophospholipase activity at pH 7.0
glutathione
-
membrane-bound enzyme, no inhibition of the soluble enzyme
Insulin
-
insulin reduces NRE mRNA levels in a dose-dependent manner in 3T3-L1 adipocytes
-
palmitoyl carnitine
-
0.5 mM, 90% inhibition at pH 5.0, LPL1; 1 mM, 64% inhibition of phospholipase B activity, 65% inhibition of lysophospholipase activity at pH 5.0
sphingomyelin
-
0.5 MM, 21% inhibition at pH 5.0, 29% inhibition at pH 7.0, LPL1; 0.5 mM, 35% inhibition of phospholipase B activity, 45% inhibition of lysophospholipase at pH 5.0, 28% inhibition of lysophospholipase at pH 7.0
deoxycholate
-
0.1% sodium deoxycholate, complete inhibition of lysophospholipase activity
DNA containing thymine glycol
-
inhibits activity with ghrelin and with palmitoyllysophosphatidylglycerol
-
Fe3+
-
1 mM, 95% inhibition of phospholipase activity, 80% inhibition of lysophospholipase activity
Hg2+
-
5 mM, inhibits phospholipase B activity by 67%, no inhibition of lysophospholipase activity
phosphatidic acid
-
0.5 mM, 24% inhibition at pH 5.0, 66% inhibition at pH 7.0, LPL1; 0.5 mM, 58% inhibition of phospholipase B activity, 92% inhibition of lysophospholipase at pH 5.0, 87% inhibition of lysophospholipase at pH 7.0
Triton X-100
-
0.1 w/v, 48% inhibition at pH 5.0, LPL1; 0.1% w/v, 85% inhibition of phospholipase B activity, 91% inhibition of lysophospholipase B activity at pH 5.0, 95% inhibition of lysophospholipase B activity at pH 7.0
additional information
the enzyme cannot be inhibited by 5 mM EDTA
-
additional information
-
the addition of EDTA alone had no effect on the lipase activity
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
minimizes loss of activity in presence of sulfhydryl reagent
cardiolipin
the enzyme shows dependence on lipid bilayer structure and cardiolipin, overview
cardiolipin hydroperoxide
iPLA2gamma is alternatively activated by cardiolipin hydroperoxides and hypothetically by structural alterations of lipid bilayer due to lipid peroxidation
-
dithiothreitol
-
10 mM, activation to 122% of control at pH 5.0, LPL1
glycerol
-
50% increase of lysophospholipase activity in the presence of 30% glycerol
H2O2
iPLA2gamma is directly stimulated by H2O2 and, hence, is activated by redox signaling or oxidative stress
Isopropanol
isopropanol increases the enzyme activity to 133%
lysophosphatidylcholine
-
0.5 mM, activation of phospholipase B activity to 132% of control
pulmonary surfactant
-
enzyme activity significantly increases (28%) in the presence of 0.1 mg/ml pulmonary surfactant
-
EGTA
-
EGTA by itself or in combination with EDTA causes a slight increase in activity
palmitoyl carnitine
-
0.5 mM, stimulates to 157% of control at pH 7.0, LPL1
palmitoyl carnitine
-
1 mM, activation of lysophospholipase activity at pH 7.0 to 239% of control
sodium deoxycholate
-
0.1%, strongly stimulates phospholipase B activity
additional information
Ca2+ independence of the enzyme activity shows that the enzyme is active when it encounters specific structural alterations in the lipid bilayer. Such alterations can be caused by PUFAs, cardiolipin, and even hydroxy or peroxy groups existing in phospholipid FA side-chains and usually localized at the water/lipid interface. Identified mechanism (possible direct redox and indirect redox mechanisms) and hypothetical alternative pathways of iPLA2gamma activation, overview
-
additional information
Ca2+ independence of the enzyme activity shows that the enzyme is active when it encounters specific structural alterations in the lipid bilayer. Such alterations can be caused by PUFAs, cardiolipin, and even hydroxy or peroxy groups existing in phospholipid FA side-chains and usually localized at the water/lipid interface. Identified mechanism (possible direct redox and indirect redox mechanisms) and hypothetical alternative pathways of iPLA2gamma activation, overview
-
additional information
Ca2+ independence of the enzyme activity shows that the enzyme is active when it encounters specific structural alterations in the lipid bilayer. Such alterations can be caused by PUFAs, cardiolipin, and even hydroxy or peroxy groups existing in phospholipid FA side-chains and usually localized at the water/lipid interface. Identified mechanism (possible direct redox and indirect redox mechanisms) and hypothetical alternative pathways of iPLA2gamma activation, overview
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.04498
1-(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoyl-2-lysophosphatidylcholine
-
Vmax: 103.5 micromol/h/mg protein
0.0676
1-arachidonoyl-2-lysophosphatidylcholine
-
Vmax: 142.8 micromol/h/mg protein
0.04498
1-docosahexaenoyl lysophosphatidylcholine
-
Vmax: 103.5 micromol/h/mg protein
0.6071
4-nitrophenyl butyrate
in 50 mM HEPES (pH 8.0), at 85°C
0.0493
lysophosphatidylcholine
pH 8, temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0222
1-palmitoyl lysophosphatidylcholine
for acylprotein thioesterase activity
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00126
1-[2-[2-hydroxy-3-(piperidin-1-yl)propoxy]phenyl]-2-phenylethan-1-one
Plasmodium falciparum
pH 8.0, temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
specific activity is 4-5 times higher in oxidative muscle than in glycolytic muscle
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 5
-
phospholipase B activity, lysophospholipase activity and transacylase activity of PLB1
5
-
lysophospholipase activity and transacylase activity, short incubation time (30 s), LPL1
5.5 - 8
-
lysophospholipase activity, long incubation time (5 min), LPL1
7.4
7.5
8.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.2 - 3
-
pH 2.2: about 70% of maximal activity, pH 3.0: about 65% of maximal activity
2.5 - 6
-
approx. 50% of maximal phospholipase activity at pH 3.0 and pH 5.0, respectively
2.5 - 7
-
50-60% of maximal lysophospholipase activity at pH 3.0 and pH 5.5, respectively
4 - 11
-
41% of maximal activity at pH 5.0, 79% of maximal activity at pH 6, Semimembranosus proprius muscle, 33% of maximal acitivity at pH 5, 75% of maximal activity at pH 6, Longissimus lumborum muscle
4 - 7
4 - 8
-
pH 4.0: about 65% of maximal activity, pH 8.0: about 40% of maximal activity, production of phosphatidylcholine
4.2 - 6
-
pH 4.2: about 75% of maximal lysophospholipase activity, pH 6.0: about 75% of maximal lysophospholipase activity, short incubation time (30 s), LPL1
5 - 9
5 - 9.3
-
pH 5.0: about 30% of maximal activity, pH 9.3: about 35% of maximal activity
6 - 8
-
about 30% activity at pH 6.0, 100% activity at pH 7,0, about 40% activity at pH 8.0, no activity below pH 5.0 or above 9.0
7
-
no phospholipase B activity, no lysophospholipase activity and no transacylase activity of PLB1 is detected at short incubation time (30 s), at incubation time 5-10 min lysophospholipase activity and transacylase activity is detected (about 5% of the activity at pH 5.0), no phospholipase B activity is detected at incubation time 5-10 min
4 - 7
-
pH 4.0: about 45% of maximal activity, pH 7.0: about 85% of maximal activity, lysophosphatidylcholine transacylase activity, pH 4.0: about 50% of maximal activity, pH 7.0: about 80% of maximal activity, lysophosphatidyl hydrolase activity
4 - 7
-
pH 4.0: about 55% of maximal activity, pH 7.0: about 60% of maximal activity
5 - 9
-
pH 5.0: about 40% of maximal activity, pH 9.0: about 50% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
40
37
-
phospholipase B activity, lysophospholipase activity and transacylase activity of PLB1, no activity detectable at higher temperatures
40
-
lysophospholipase reaction proceeds even at 0°C and its rate increases with temperature up to roughly 50°C, the optimal temperature is near 40 °C
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 50
-
25°C: about 70% of maximal activity, 50°C: about 90% of maximal activity
30 - 80
conformational changes are negligible over the temperature range of 30-80°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.05
determined by isoelectric focusing, SDS-PAGE, extract of adult Schistosoma japonicum worm
6.3
6.4
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
var. grubii H99 wild-type strain and its PLB1 deletion mutant strain (the _plb1 strain)
-
-
brenda
acts as acyl-protein thioesterase/lysophospholipase, cf. EC 3.1.2.22
UniProt
brenda
acts as acyl-protein thioesterase/lysophospholipase, cf. EC 3.1.2.22
SwissProt
brenda
var. Advance, at least 3 enzymatic forms: PLP I, PLP II and PLP II'
-
-
brenda
acts as acyl-protein thioesterase/lysophospholipase, cf. EC 3.1.2.22
SwissProt
brenda
acts as acyl-protein thioesterase/lysophospholipase, cf. EC 3.1.2.22
SwissProt
brenda
native enzyme and modified enzyme that is generated by the introduction of some nicks into the native type of enzyme
-
-
brenda
enzyme exhibits the GXSXG consensus active site characteristic of serine proteases, esterases, and lipases, and includes the catalytic triad motif of SerAspHis residues characteristic of serine hydrolases. Three-dimensional structural predictions indicate that the putative catalytic triad formed by these three residues is located at the alpha/beta-hydrolase fold characteristic of the lipases and esterases
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
primary cultures of mouse neural cells. PLB activity is present in a variety of cultured mouse neural cell types but that acute loss of this activity is not cytotoxic
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hLysoPLA I expression is induced by phorbol 12-myristate 13-acetate
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additional information
LYPLA1 contributes to Enterococcus faecalis-induced hypertension by accumulating glycerophosphocholine and activating epithelial sodium channel alpha subunit in the renal medulla
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additional information
the iPLA2gamma mRNA is found in multiple human parenchymal tissues
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additional information
the iPLA2gamma mRNA is found in multiple human parenchymal tissues
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additional information
the iPLA2gamma mRNA is found in multiple human parenchymal tissues
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additional information
PNPLA7 is significantly down-regulated in gastric and colorectal cancer tumor tissues compared to adjacent normal tissues
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additional information
LPL3 displays a dynamic localization throughout asexual stages, mainly localizing in the host-parasite interface
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
enzyme is also located in mitochondria even in the absence of prenylation
brenda
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two-third of the enzyme is particulate, one-third is cytoplasmic
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in late-trophozoite and schizonts stages, enzyme is observed at the parasite periphery, in the parasitophorous vacuole region. During the late-trophozoite stages, LPL3 is present in the parasitophorous vacuole extensions forming a host-parasite interface structure
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additional information
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two-third of the enzyme is particulate, one-third is cytoplasmic
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in early development stages, ring and midtrophozoite stages, protein is mainly observed in the cytosol
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the catalytic region of PNPLA7 localizes to mature lipid droplets ex vivo and also colocalizes with pre-existing lipid droplets. This induces lipid droplets clustering via non-enzymatic intermolecular associations. Residues 742-1016 contain four putative transmembrane domains which act as a targeting motif to the lipid droplets and are required for the localization of PNPLA7 to lipid droplets
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PNPLA7-C localizes to the mature lipid droplets ex vivo and also colocalizes with pre-existing lipid droplets
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protein contians a putative peroxisomal targeting sequence
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additional information
ithe enzyme acts on membrane and the outer mitochondrial membrane outer leaflet
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additional information
ithe enzyme acts on membrane and the outer mitochondrial membrane outer leaflet
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additional information
ithe enzyme acts on membrane and the outer mitochondrial membrane outer leaflet
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Highest Expressing Human Cell Lines
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
comparisons of selected intracellular calcium-independent phospholipases A2 (patatin-like phospholipase domain-containing proteins, PNPLA), calcium-dependent cytosolic phospholipases A2 (cPLA2s), and low-molecular-weight secreted phospholipases A2 (sPLA2s), detailed overview. iPLA2gamma belongs to the intracellular calcium-independent phospholipases A2 (patatin-like phospholipase domain-containing proteins, PNPLA)
evolution
comparisons of selected intracellular calcium-independent phospholipases A2 (patatin-like phospholipase domaincontaining proteins, PNPLA), calcium-dependent cytosolic phospholipases A2 (cPLA2s), and low-molecular-weight secreted phospholipases A2 (sPLA2s), detailed overview. iPLA2gamma belongs to the intracellular calcium-independent phospholipases A2 (patatin-like phospholipase domain-containing proteins, PNPLA)
malfunction
-
lysoPL2 knockout mutants show enhanced sensitivity to Zn2+ and H2O2 in comparison to wild type
malfunction
mitochondrial iPLA2gamma in brain physiology and pathology, overview
malfunction
PNPLA7 is significantly down-regulated in gastric and colorectal cancer tumor tissues compared to adjacent normal tissues. The overall survival of patients with high expression of PNPLA7 is significantly higher than that of patients with low expression in stomach and rectum adenocarcinoma
metabolism
-
the enzyme exerts important functions in the homeostasis of phospholipids or detoxification of lysophospholipids
metabolism
iPLA2gamma is directly stimulated by H2O2 and is activated by redox signaling or oxidative stress. This redox activation permits the antioxidant synergy with mitochondrial uncoupling proteins (UCPs) or other SLC25 mitochondrial carrier family members by FA-mediated protonophoretic activity, termed mild uncoupling, that leads to diminishing of mitochondrial superoxide formation. iPLA2gamma is alternatively activated by cardiolipin hydroperoxides and hypothetically by structural alterations of lipid bilayer due to lipid peroxidation. Fatty acid-mediated signaling by iPLA2gamma, overview
physiological function
-
lysophospholipase 2 can effectively remove lysophosphatidylcholine and detoxify the peroxidized membrane. Lysophospholipase 2-overexpressing Arabidopsis is more tolerant to H2O2 and Cd2+ than wild type, suggesting involvement lysophospholipase-2 in phospholipid repair following lipid peroxidation arising from metal-induced stress. The enzyme confers protection during oxidative stress
physiological function
-
LipC plays an important role in the degradation of the outer spore membrane during sporulation
physiological function
-
phospholipase B activity is involved in the process of adhesion and internalization of yeast cells at the MH-S cell surface and may enhance virulence and subsequent down-regulation of macrophage activation
physiological function
-
the serum activity of APT1 plays an important role in determination of the concentration of des-acyl ghrelin in circulation, especially under septic inflammation
physiological function
-
the lipase activity of surface-exposed VolA contributes to the success of Vibrio cholerae, improving the overall adaptation and survival of the organism in different environments
physiological function
-
treating RAW264.7 cells with the enzyme significantly induces interleukin-25 expression. The enzyme activates hepatic stellate cells by upregulating interleukin-25 in macrophages through the protein kinase A-dependent B-Raf/ERK1/2 pathway and potentially promotes hepatic fibrosis during Clonorchis sinensis infection
physiological function
-
the enzyme plays important roles in the pathogenicity of Spiroplasma eriocheiris
physiological function
-
the enzyme can attenuate the fibrogenic response by inhibiting activation of LX-2 cells, thereby balancing the pro-fibrotic and anti-fibrotic response during the Clonochis sinensis infection. The enzyme inhibits the phosphorylations of Smad3, JNK, and ERK in response to transforming growth factor-beta1 in LX-2 cells
physiological function
LPL3 displays a dynamic localization throughout asexual stages, mainly localizing in the host-parasite interface. Inducible knockdown of LPL3 disrupts parasite development from trophozoites to schizont, inducing a drastic reduction in merozoite progenies. LPL3 generates fatty acids from scavenged host lipids to generate neutral lipids. These are then timely mobilized to allow schizogony and merozoite formation
physiological function
-
upon Verticillium dahliae attack, LPL2 accumulates on the membrane and binds to V. dahliae secreted Necrosis-and ethylene-inducing peptide NLP1, to block its contribution to virulence. LPL2 silenced cotton plants also display high resistance to V. dahliae, but show severe dwarfing phenotype and developmental defects. GhLPL2 silencing results in lysophosphatidylinositol over-accumulation and decreased glycometabolism, leading to a lack of carbon sources required for plants and pathogens to survive
physiological function
the level of isoform LYPLA1 is unaffected by knock-out of LYPLA2. LYPLA2-/- cells display significantly lower acyl-protein thioesterase and lysophospholipase activities than wild-type. Double knock-out cells lacking both LYPLA1 and LYPLA2 retain 64% and 46% acyl-protein thioesterase and lysophospholipase activity, respectively, and display dramatically increased lysophosphatidylipid levels
physiological function
the level of isoform LYPLA1 is unaffected by knock-out of LYPLA2. LYPLA1-/- cells display similar acyl-protein thioesterase and lysophospholipase activities as wild-type. Double knock-out cells lacking both LYPLA1 and LYPLA2 retain 64% and 46% acyl-protein thioesterase and lysophospholipase activity, respectively, and display dramatically increased lysophosphatidylipid levels
physiological function
Acyl-CoA-binding protein2 may play a role in facilitating a direct interaction between LYSOPL2 and lysophosphatidylcholine. Acyl-CoA-binding protein2 binds lysophosphollipase 2 via its ankyrin repeats in vitro. The interactions of acyl-CoA-binding protein2 amino acids 70-354 with LYSOPL2 and lysophopshatidylcholine are both endothermic, favoured by solvation entropy and opposed by enthalpy, with dissociation constants in the micromolar range
physiological function
-
PNPLA7-C localizes to the mature lipid droplets ex vivo and also colocalizes with pre-existing lipid droplets. Localization of PNPLA7-C with lipid droplets induces lipid droplets clustering via non-enzymatic intermolecular associations, while PNPLA7 alone does not induce lipid droplet clustering. Residues 742-1016, four putative transmembrane domains, act as a lipid droplet targeting motif. The N-terminal flanking region of the targeting motif, residues 681-741, contributes to the targeting. The lipid droplet targeting motif does not exhibit lysophosphatidylcholine hydrolase activity
physiological function
-
overexpression of FSH1 leads to a significant reduction in the cellular phospholipid levels and an increase in the triacylglycerol levels and lipid droplet number
physiological function
patatin-like phospholipase domain-containing protein PNPLA8, also termed Ca2+-independent phospholipase A2gamma (iPLA2gamma), is addressed to the mitochondrial matrix (or peroxisomes), where it may manifest its unique activity to cleave phospholipid side-chains from both sn-1 and sn-2 positions, consequently releasing either saturated or unsaturated fatty acids (FAs), including oxidized FAs. Other iPLA2 roles include the remodeling of mitochondrial (or peroxisomal) membranes and the generation of specific lipid second messengers. Thus, for example, during FA beta-oxidation in pancreatic beta-cells, H2O2-activated iPLA2 supplies the GPR40 metabotropic FA receptor to amplify FA-stimulated insulin secretion. Antioxidant synergy of iPLA2gamma and mitochondrial uncoupling of proteins, mechanism. Cytoprotective roles of iPLA2 in the heart and brain are also observed. The iPLA2gamma plays an essential role in the hydrolysis of oxidized cardiolipin, from which specifically 9-hydroxy-octadecenoic acid is hydrolyzed
physiological function
patatin-like phospholipase domain-containing protein PNPLA6, also termed Ca2+-independent phospholipase A2delta (iPLA2delta), is addressed to the endoplasmic reticulum and Golgi, where it is involved in neuroprotection and intracellular membrane trafficking
physiological function
patatin-like phospholipase domain-containing protein PNPLA6, also termed Ca2+-independent phospholipase A2theta (iPLA2theta), is involved in neuroprotection and intracellular membrane trafficking
physiological function
patatin-like phospholipase domain containing protein 7 (PNPLA7) is a pyrophosphokinase localized to the endoplasmic reticulum membrane. Patatin-like phospholipase domain containing protein 7 (PNPLA7) is associated with tumorigenesis and the occurrence and development of hepatocellular carcinoma, online gene expression profiling interactive analysis and Kaplan Meier Plotter databases for the analysis of expression of PNPLA7 and survival curve, respectively. PNPLA7 is significantly down-regulated in gastric and colorectal cancer tumor tissues compared to adjacent normal tissues
physiological function
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overexpression of FSH1 leads to a significant reduction in the cellular phospholipid levels and an increase in the triacylglycerol levels and lipid droplet number
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additional information
Ser-Asp catalytic site. Molecular mechanism of antioxidant synergy involving iPLA2 and UCPs and selected cases of the SLC25 family proteins, overview
additional information
Ser-Asp catalytic site. Molecular mechanism of antioxidant synergy involving iPLA2 and UCPs and selected cases of the SLC25 family proteins, overview
additional information
Ser-Asp catalytic site. Molecular mechanism of antioxidant synergy involving iPLA2 and UCPs and selected cases of the SLC25 family proteins, overview
additional information
a Ser-Asp dyads contributes to the catalytic site. Molecular mechanism of antioxidant synergy involving iPLA2 and UCPs and selected cases of the SLC25 family proteins, overview
additional information
a Ser-Asp dyads contributes to the catalytic site. Molecular mechanism of antioxidant synergy involving iPLA2 and UCPs and selected cases of the SLC25 family proteins, overview
additional information
a Ser-Asp dyads contributes to the catalytic site. Molecular mechanism of antioxidant synergy involving iPLA2 and UCPs and selected cases of the SLC25 family proteins, overview
Show AA Sequence and Transmembrane Helices (15511 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
106000
-
x * 106000, modified enzyme that is generated by the introduction of some nicks into the native type of enzyme, SDS-PAGE
220000
23000
24840
25000
26000
28000
29000
37000
52000
a 52000 Da species and a 63000 Da species is detected by SDS-PAGE.The 52000 Da species is a truncated version of the 63000 Da protein
63000
66000
23000
determined by Western blot analysis, extract of adult Schistosoma japonicum worm
23000
immunoblot analysis, single band in both membrane-associated and soluble tissue fractions of adult schistosomes
26000
determined by SDS-PAGE, recombinant 6-His-tagged lysophospholipase
63000
a 52000 Da species and a 63000 Da species is detected by SDS-PAGE. The 52000 Da species is a truncated version of the 63000 Da protein
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
prediction, based on the determination of the hydrodynamic radius by dynamic light scattering measurements
homohexamer
monomer
?
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x * 106000, modified enzyme that is generated by the introduction of some nicks into the native type of enzyme, SDS-PAGE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
side-chain modification
side-chain modification
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phospholipase B2 contains 0.0104 mM carbohydrate per mg protein
side-chain modification
-
phospholipase B1 contains 0.0207 mM mannose per mg of protein
side-chain modification
-
phospholipase 2 contains 0.0097 mM mannose per mg of protein
side-chain modification
-
phospholipase B1 contains 0.0224 mM carbohydrate per mg protein
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of the multifunctional thioesterase I/protease I/lysophospholipase L1 in complex with octanoic acid and of the L109P mutant enzyme in complex with octanoic acid
structure of LYPLA2 modified by PMSF, at 2.7 A resolution. LYPLA2 lacks a cap domain, which is replaced by the beta4-alpha2 loops
sitting drop vapor diffusion method, using 20% (w/v) PEG 3350, 50 mM sodium-citrate buffer, pH 4.5
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structure of LYPLA2 modified by PMSF, at 2.7 A resolution. LYPLA2 lacks a cap domain, which is replaced by the beta4-alpha2 loops
structure of LYPLA2 modified by PMSF, at 2.7 A resolution. LYPLA2 lacks a cap domain, which is replaced by the beta4-alpha2 loops
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D268A
catalytic triad mutant, binds lysophosphatidylcholine only weakly
H298A
catalytic triad mutant, binds lysophosphatidylcholine only weakly
S147A
catalytic triad mutant, binds lysophosphatidylcholine only weakly
S11A
-
the amount of free fatty acids in the mutant spores is about 35fold less than in the wild type spores
D17S/L162R
-
the mutant shows 2.2fold increased thioesterase activity compared to the wild type
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
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 50
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after 10 min of incubation, the enzyme shows 100% activity at 30°C, about 65% activity at 40°C, almost no activity at 50°C
4 - 10
enzyme is a psychrophilic enzyme and retains about 50% of its maximal activity at 10°C and 40% at 4°C
50
55
60 - 70
-
less than 20% activity remains after 30 min incubation at above 60°C
85
50
-
45% loss of lysophospholipase and transacylase activity, complete loss of phospholipase activity
50
-
about 60% loss of activity of the Ca2+-depleted enzyme after 2 h, about 80% loss of activity of the Ca2+-containing enzyme after 2 h
55
-
the enzyme has a half-life of 10.5 h, 3.7 h and 0.5 h at 55°C, 65°C and 75°C, respectively
85
begins to unfold above 85°C, with unfolding remaining incomplete even at 95°C
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, in absence of glycerol, the enzyme loses all of its activity during the freezing and thawing process
-
60% loss of activity after 14 h dialysis in the absence of lysophosphatidylcholine, at 0-4°C
-
unstable upon purification, enzyme activity is lost during storage at 4°C or -70°C
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
acetonitrile
Ethanol
25%, substrate p-nitrophenyl palmitate, relative activiy 39%
Methanol
25%, substrate p-nitrophenyl palmitate, relative activiy 20%
acetonitrile
25%, substrate p-nitrophenyl palmitate, relative activiy 58%
acetonitrile
more than 90% of the enzyme activity retains after incubation with acetonitrile
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, enzyme concentration: 0.01-0.025 mg/ml, 60-70% glycerol, stable for several months
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation and DEAE anion exchange column chromatography
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ammonium sulfate, phenyl-Sepharose, Uno Q-1, Superose 12 HR, Superdex 200
-
by procedures employing acetic acid precipitation, 1-butanol solubilization and ammonium sulfate fractionation, and chromatographies
-
cytosolic fractions of COS7 cell extracts containing His-tagged NRE are loaded onto a Q-Sepharose column
-
Ni-NTA column chromatography
Ni-Sepharose 6 Fast Flow column chromatography and Superdex 200 gel filtration
-
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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
expression in Escherichia coli
expression in Escherichia coli as a secreted, soluble, non-tagged, mature construct
expression in Escherichia coli, enzyme encoded by the gene plaB is a phospholipase A and a lysophospholipase A
-
expression in Escherichia coli, overexpression in Legionella pneumophila completely protects from the toxic effects of lysophosphatidylcholine
gene PNPLA7, quantitative real-time PCR enzyme expression analysis and gene expression profiling interactive analysis (GEPIA)
GST-fusion protein expressed in Escherichia coli BL21, expressed in HEK-293 cell
into the vector pGEX-KG and subsequently into pET23a for expression in Escherichia coli BL21DE3 pLysS cells
mutant cDNAs (R108A, S146A, and D392A) are expressed in Saccharomyces cerevisiae
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
APT1 is released at high levels from RAW264.7 macrophage-like cells into the culture medium after stimulation with lipopolysaccharide, the mRNA level of lysophospholipase II in RAW264.7 cells is much less than APT1 and not changed by lipopolysaccharide treatment
lipopolysaccharide suppresses APT1 mRNA and protein expression
lysoPL2 mRNA expression in shoots is up-regulated by Zn2+, and H2O2 (but not by Pb2+, Cd2+ and Cu2+), while roots are only up-regulated by H2O2
-
protein is expressed throughout all stages of the asexual blood life cycle
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
degradation
-
GMGL accepts monoacylglycerol as substrate, as well as lysophosphatidylcholine, lysophosphatidylethanolamine and glycerolphosphatidylcholine. Lysophosphatidylethanolamine and glycerolphosphatidylcholine bind as stably as monoacylglycerol. The enzyme shows great potential in enzymatic degumming. The phosphorus content in crude soybean oil decreases from 680.50 to 2.01 mg/kg and the yield of oil reaches to 98.80 % after treatment with phospholipase A1 combined with lipase GMGL
diagnostics
PNPLA7 can be used as a diagnostic marker for gastric and colorectal tumors. The overall survival of patients with high expression of PNPLA7 is significantly higher than that of patients with low expression in stomach and rectum adenocarcinoma. Phospholipase PNPLA7 can be used as a positive diagnostic indicator for colorectal and gastric cancers
medicine
medicine
-
LLPL activity is anti-atherogenic and the regulation of this enzyme might be a novel drug target for the treatment of atherosclerosis
medicine
Schistosome lysophospholipase may represent a new target for anti-schistosomal chemotherapy
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
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
medicine
-
the cytotoxic potential and signalling properties enable Legionella pneumophila PLA, LPLA enzymes to act as bacterial virulence factors, involved in severe lung disease
medicine
schistosome lysophospholipase may represent a new target for anti-schistosomal-chemotherapy
medicine
Enterococcus faecalis treatment increases blood pressure, serum angiotensin II, sodium reabsorption, and expression of epithelial sodium channel alpha subunit and LYPLA1 in the renal medulla of mice. LYPLA1 promotes the accumulation of renal glycerophosphocholine, which directly elevates the expression of epithelial sodium channel alpha subunit and sodium reabsorption
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