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Information on EC 2.3.1.23 - 1-acylglycerophosphocholine O-acyltransferase and Organism(s) Homo sapiens and UniProt Accession Q6P1A2
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2.3.1.23 1-acylglycerophosphocholine O-acyltransferaseIUBMB Comments
Acts preferentially with unsaturated acyl-CoA derivatives. 1-Acyl-sn-glycero-3-phosphoinositol can also act as acceptor.
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Word Map
- 2.3.1.23
- acyl-coas
- lysophospholipids
- phospholipase
-
arachidonic
-
polyunsaturated
-
lysophosphatidic
-
reacylation
- lncrnas
-
platelet-activating
- glycerophospholipids
- palmitoyl-coa
- oleoyl-coa
- arachidonoyl-coa
-
lysopcs
-
cholinephosphotransferase
-
kennedy
- lysophospholipase
-
deacylation-reacylation
- lysophosphatidylinositol
-
mboats
-
oleoyl
-
lecithin-cholesterol
-
transacylation
-
arachidonoyl
- linoleoyl-coa
-
acyl-coa-dependent
- lysophosphatidylserine
- thimerosal
-
disaturated
- glycerolphosphate
-
coa-independent
-
cholinephosphate
- lysophosphatidylglycerol
- pharmacology
- medicine
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
pcat1, lpcat3, lpcat, lysophosphatidylcholine acyltransferase, alcat1, lpcat2, lysolecithin acyltransferase, lycat, lyso-paf acetyltransferase, lysophosphatidylcholine acyltransferase 1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
lysophosphatidylcholine acyltransferase 3
-
1-acyl-sn-glycero-3-phosphocholine acyltransferase
-
-
-
-
acyl coenzyme A-monoacylphosphatidylcholine acyltransferase
-
-
-
-
acyl-CoA:1-acyl-glycero-3-phosphocholine transacylase
-
-
-
-
acyltransferase, lysolecithin
-
-
-
-
LPCAT
lysolecithin acyltransferase
-
-
-
-
lysophosphatide acyltransferase
-
-
-
-
lysophosphatidylcholine acyltransferase
lysophospholipid acyltransferase
lysophosphatidylcholine acyltransferase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
acyl-CoA:1-acyl-sn-glycero-3-phosphocholine O-acyltransferase
Acts preferentially with unsaturated acyl-CoA derivatives. 1-Acyl-sn-glycero-3-phosphoinositol can also act as acceptor.
CAS REGISTRY NUMBER
COMMENTARY
9027-64-9
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-palmitoyl-2-lysophosphatidylcholine + alpha-linolenoyl-CoA
1-palmitoyl-2-alpha-linolenoylphosphatidylcholine + CoA
-
-
-
?
1-palmitoyl-2-lysophosphatidylcholine + arachidonoyl-CoA
1-palmitoyl-2-arachidonoylphosphatidylcholine + CoA
1-palmitoyl-2-lysophosphatidylcholine + linoleoyl-CoA
1-palmitoyl-2-linoleoylphosphatidylcholine + CoA
-
-
-
?
1-palmitoyl-2-lysophosphatidylcholine + oleoyl-CoA
1-palmitoyl-2-oleoylphosphatidylcholine + CoA
-
-
-
?
1-palmitoyl-2-lysophosphatidylcholine + stearoyl-CoA
1-palmitoyl-2-stearoylphosphatidylcholine + CoA
-
-
-
?
1-palmitoyl-2-lysophosphatidylserine + arachidonoyl-CoA
1-palmitoyl-2-arachidonoylphosphatidylserine + CoA
-
-
-
?
1-palmitoyl-2-lysophosphatidylserine + linoleoyl-CoA
1-palmitoyl-2-linoleoylphosphatidylserine + CoA
-
-
-
?
acyl-CoA + 1-acyl-sn-glycero-3-phosphocholine
CoA + 1,2-diacyl-sn-glycero-3-phosphocholine
-
-
-
?
arachidonoyl-CoA + 1-acyl-sn-glycero-3-phosphocholine
CoA + 1-acyl-2-arachidonoyl-sn-glycero-3-phosphocholine
-
-
-
?
arachidonoyl-CoA + 1-arachidoyl-2-lysophosphatidylcholine
CoA + 2-arachidonoyl-1-arachidoylphosphatidylcholine
-
-
-
?
arachidonoyl-CoA + 1-O-hexadecyl-sn-glycero-3-phosphocholine
CoA + 2-arachidonoyl-1-O-hexadecyl-sn-glycero-3-phosphocholine
LPCAT3 acylates 1-O-alkyl-sn-glycero-3-phosphocholine with arachidonyl-CoA but not with acetyl-CoA
-
-
?
arachidonoyl-CoA + 1-palmitoyl-2-lysophosphatidylcholine
CoA + 2-arachidonoyl-1-palmitoylphosphatidylcholine
-
-
-
?
arachidonoyl-CoA + 1-palmitoyl-2-lysophosphatidylethanolamine
CoA + 2-arachidonoyl-1-palmitoylphosphatidylethanolamine
lysophosphatidylethanolamine acylation is evident. But no significant activity of acylation is detected when 16:0-lysophosphatidylglycerol is used as substrate
-
-
?
arachidonoyl-CoA + 1-stearoyl-2-lysophosphatidylcholine
CoA + 2-arachidonoyl-1-stearoylphosphatidylcholine
-
-
-
?
arachidonoyl-CoA + NBD-labelled lysophosphatidylcholine
CoA + NBD-2-arachidonoyl-phosphatidylcholine
-
-
-
-
arachidonoyl-CoA + palmitoyl-lysophosphatidylcholine
CoA + 2-arachidonoyl-1-palmitoylphosphatidylcholine
-
-
-
?
linoleoyl-CoA + 1-acyl-sn-glycero-3-phosphocholine
CoA + 1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine
-
-
-
?
linoleoyl-CoA + 1-palmitoyl-2-lysophosphatidylcholine
CoA + 2-linoleoyl-1-palmitoylphosphatidylcholine
-
-
-
?
oleoyl-CoA + 1-palmitoyl-2-lysophosphatidylcholine
CoA + 2-oleoyl-1-palmitoylphosphatidylcholine
-
-
-
?
oleoyl-CoA + palmitoyl-lysophosphatidylcholine
CoA + 2-oleoyl-1-palmitoylphosphatidylcholine
-
-
-
?
palmitoyl-CoA + 1-palmitoyl-2-lysophosphatidylcholine
CoA + 1,2-dipalmitoylphosphatidylcholine
-
-
-
?
stearoyl-CoA + 1-palmitoyl-2-lysophosphatidylcholine
CoA + 2-stearoyl-1-palmitoylphosphatidylcholine
-
-
-
?
1-acyl-2-lysophosphatidylethanolamine + oleoyl-CoA
1-acyl-2-oleoylphosphatidylethanolamine + CoA
-
-
-
?
1-myristoyl-lysophosphatidylcholine + palmitoyl-CoA
CoA + 1-myristoyl-2-palmitoylphosphatidylcholine
-
-
-
-
?
1-oleoyl-lysophosphatidylcholine + palmitoyl-CoA
CoA + 1-oleoyl-2-palmitoylphosphatidylcholine
-
-
-
-
?
1-palmitoyl-2-lysophosphatidylcholine + palmitoyl-CoA
1,2-dipalmitoylphosphatidylcholine + CoA
activity observed only in the presence of phosphatidylcholine (1 mg/ml)
-
-
?
1-palmitoyl-2-lysophosphatidylglycerol + palmitoyl-CoA
1,2-dipalmitoylphosphatidylglycerol + CoA
activity observed only in the presence of phosphatidylcholine (1 mg/ml)
-
-
?
1-palmitoyl-lysophosphatidylcholine + arachidonoyl-CoA
CoA + 1-palmitoyl-2-arachidonoylphosphatidylcholine
-
-
-
-
?
1-palmitoyl-lysophosphatidylcholine + lauroyl-CoA
CoA + 1-palmitoyl-2-lauroylphosphatidylcholine
-
-
-
-
?
1-palmitoyl-lysophosphatidylcholine + linoleoyl-CoA
CoA + 1-palmitoyl-2-linoleoylphosphatidylcholine
-
-
-
-
?
1-palmitoyl-lysophosphatidylcholine + n-octanoyl-CoA
CoA + 1-palmitoyl-2-octanoylphosphatidylcholine
-
-
-
-
?
1-palmitoyl-lysophosphatidylcholine + oleoyl-CoA
CoA + 2-oleoyl-1-palmitoylphosphatidylcholine
-
-
-
-
?
1-palmitoyl-lysophosphatidylcholine + palmitoyl-CoA
CoA + 1,2-dipalmitoylphosphatidylcholine
-
-
-
-
?
1-palmitoyl-lysophosphatidylcholine + stearoyl-CoA
CoA + 1-palmitoyl-2-stearoylphosphatidylcholine
-
-
-
-
?
1-stearoyl-lysophosphatidylcholine + palmitoyl-CoA
CoA + 1-stearoyl-2-palmitoylphosphatidylcholine
-
-
-
-
?
acyl-CoA + 1-acyl-2-lysophosphatidylethanolamine
1,2-diacylphosphatidylethanolamine + CoA
-
-
-
?
acyl-CoA + 1-acyl-sn-glycero-3-phosphocholine
CoA + 1,2-diacyl-sn-glycero-3-phosphocholine
acyl-CoA + 1-acyl-sn-lysophosphatidylcholine
CoA + 1,2-diacyl-sn-lysophosphatidylcholine
-
-
-
?
linoleoyl-CoA + 1-palmitoyl-2-lysophosphatidylcholine
CoA + 1-palmitoyl-2-linoleoylphosphatidylcholine
-
-
-
?
lyso-platelet-activating factor + acetyl-CoA
platelet-activating factor + CoA
activity observed only in the presence of phosphatidylcholine (1 mg/ml)
-
-
?
oleoyl-CoA + 1-palmitoyl-sn-glycero-3-phosphocholine
CoA + 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine
-
-
-
-
?
oleoyl-CoA + sn-1-myristoyl-lysophosphatidylcholine
CoA + 1-myristoyl-2-oleoylphosphatidylcholine
-
-
-
-
?
oleoyl-CoA + sn-1-oleoyl-lysophosphatidylcholine
CoA + 1,2-dioleoylphosphatidylcholine
-
-
-
-
?
oleoyl-CoA + sn-1-stearoyl-lysophosphatidylcholine
CoA + 2-oleoyl-1-stearoylphosphatidylcholine
-
-
-
-
?
palmitoyl-CoA + 1-palmitoyl-2-lysophosphatidylcholine
CoA + 1,2-dipalmitoylphosphatidylcholine
-
-
-
?
palmitoyl-CoA + 1-palmitoyl-lysophosphatidylcholine
CoA + 1,2-dipalmitoyl-lysophosphatidylcholine
quantification of palmitic acid by gas chromatography
-
-
?
palmitoyl-CoA + 1-palmitoyl-sn-glycero-3-phosphocholine
CoA + 1,2-dipalmitoyl-sn-glycero-3-phosphocholine
palmitoyl-CoA + 1-palmitoyl-sn-glycero-3-phosphocholine
CoA + 1,2-dipalmitoylphosphatidylcholine
-
-
-
-
?
palmitoyl-CoA + 1-palmitoyl-sn-lysophosphatidylcholine
CoA + 1,2-dipalmitoyl-sn-lysophosphatidylcholine
-
-
-
?
palmitoyl-CoA + 2-palmitoyl-lysophosphatidylcholine
CoA + 1,2-dipalmitoyl-sn-lysophosphatidylcholine
reaction of EC 2.3.1.62
-
-
?
palmitoyl-CoA + sn-1-myristoyl-lysophosphatidylcholine
CoA + 1-myristoyl-2-palmitoylphosphatidylcholine
-
-
-
-
?
palmitoyl-CoA + sn-1-oleoyl-lysophosphatidylcholine
CoA + 1-oleoyl-2-palmitoylphosphatidylcholine
-
-
-
-
?
palmitoyl-CoA + sn-1-stearoyl-lysophosphatidylcholine
CoA + 1-stearoyl-2-palmitoylphosphatidylcholine
-
-
-
-
?
stearoyl-CoA + 1-palmitoyl-sn-glycero-3-phosphocholine
CoA + 1-palmitoyl-2-stearoyl-sn-glycero-3-phosphocholine
-
-
-
-
?
1-palmitoyl-2-lysophosphatidylcholine + arachidonoyl-CoA
1-palmitoyl-2-arachidonoylphosphatidylcholine + CoA
-
-
-
?
1-palmitoyl-2-lysophosphatidylcholine + arachidonoyl-CoA
1-palmitoyl-2-arachidonoylphosphatidylcholine + CoA
-
-
-
-
?
acyl-CoA + 1-acyl-sn-glycero-3-phosphocholine
CoA + 1,2-diacyl-sn-glycero-3-phosphocholine
-
-
-
r
acyl-CoA + 1-acyl-sn-glycero-3-phosphocholine
CoA + 1,2-diacyl-sn-glycero-3-phosphocholine
-
-
-
r
palmitoyl-CoA + 1-palmitoyl-sn-glycero-3-phosphocholine
CoA + 1,2-dipalmitoyl-sn-glycero-3-phosphocholine
-
-
-
?
palmitoyl-CoA + 1-palmitoyl-sn-glycero-3-phosphocholine
CoA + 1,2-dipalmitoyl-sn-glycero-3-phosphocholine
quantification of palmitic acid by gas chromatography
-
-
?
additional information
?
-
reduced activity with lysophosphatidylethanolamine and lysophosphatidylserine
-
-
?
additional information
?
-
-
reduced activity with lysophosphatidylethanolamine and lysophosphatidylserine
-
-
?
additional information
?
-
-
priming of Mono-Mac 6 cells by IFNgamma appears to involve LPCAT
-
-
?
additional information
?
-
-
the enzyme may mediate the priming reactions of monocytes to the cytokine interferon-gamma. The enzyme might also effect the responses of monocytes to the bacterial agent lipopolysaccharide that may be important in the development of sepsis
-
-
?
additional information
?
-
-
low activity with lauroyl-CoA, linoleoyl-CoA and arachidonyl-CoA
-
-
?
additional information
?
-
-
inhibition of Golgi complex-associated LPAT activity by the drug CI-976 stimulates Golgi tubule formation and subsequent redistribution of resident Golgi proteins to the endoplasmic reticulum, affecting secretory and endocytic membrane trafficking pathways, overview
-
-
?
additional information
?
-
a linear incorporation of labeled fatty acyl CoA into dipalmitoyl phosphatidylcholine (PC) indicates that lysophosphatidylcholine generated by Prdx6 PLA2 activity remains bound to the enzyme for the reacylation reaction
-
-
-
additional information
?
-
development and evaluation of an accurate and versatile method for determining the acyl group-introducing position of lysophospholipid acyltransferases, overview. Positional specificity of the hydroxyl group of the glycerol backbone (sn-2 or sn-1) at which LPLATs introduce a fatty acid. LPCAT1 introduces palmitic acid both at the sn-1 and sn-2 positions of palmitoyl-lysophosphatidylcholine (LPC). sn-1-Palmitoyl LPC appears to have a slightly higher affinity for LPCAT1 than sn-2-palmitoyl LPC, while sn-2-palmitoyl LPC has a higher turnover rate
-
-
-
additional information
?
-
the enzyme is highly specific for substrates palmitoyl-CoA and lysophosphatidylcholine. Lysophosphatidylethanolamine, lysophosphatidylglycerol, lysophosphatidylinositol, and lysophosphatidylserine are poor substrates, as well as stearoyl-CoA, acetyl-CoA, oleoyl-CA, and arachidonoyl-CoA
-
-
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acyl-CoA + 1-acyl-sn-glycero-3-phosphocholine
CoA + 1,2-diacyl-sn-glycero-3-phosphocholine
-
-
-
?
arachidonoyl-CoA + 1-acyl-sn-glycero-3-phosphocholine
CoA + 1-acyl-2-arachidonoyl-sn-glycero-3-phosphocholine
-
-
-
?
acyl-CoA + 1-acyl-sn-lysophosphatidylcholine
CoA + 1,2-diacyl-sn-lysophosphatidylcholine
-
-
-
?
palmitoyl-CoA + 1-palmitoyl-sn-glycero-3-phosphocholine
CoA + 1,2-dipalmitoyl-sn-glycero-3-phosphocholine
-
-
-
?
additional information
?
-
-
priming of Mono-Mac 6 cells by IFNgamma appears to involve LPCAT
-
-
?
additional information
?
-
-
the enzyme may mediate the priming reactions of monocytes to the cytokine interferon-gamma. The enzyme might also effect the responses of monocytes to the bacterial agent lipopolysaccharide that may be important in the development of sepsis
-
-
?
additional information
?
-
-
inhibition of Golgi complex-associated LPAT activity by the drug CI-976 stimulates Golgi tubule formation and subsequent redistribution of resident Golgi proteins to the endoplasmic reticulum, affecting secretory and endocytic membrane trafficking pathways, overview
-
-
?
additional information
?
-
a linear incorporation of labeled fatty acyl CoA into dipalmitoyl phosphatidylcholine (PC) indicates that lysophosphatidylcholine generated by Prdx6 PLA2 activity remains bound to the enzyme for the reacylation reaction
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
lipopolysaccharide
suppresses the enzyme activity of isozyme LPCAT3 toward linoleoyl-CoA and arachidonoyl-CoA in phorbol 12-myristate 13-acetate-treated U-937 cells
N-ethylmaleimide
15 min preincubation on ice with 40 mM: activity completely abolished
18-(4'-azido-2'-hydroxybenzoylamino)-oleic acid
-
73% inhibition, reversible inhibition in the dark, irreversible inactivation after photolysis, used as photoaffinity label
CI-976
-
inhibition of Golgi complex-associated LPAT activity by the drug CI-976 stimulates Golgi tubule formation and subsequent redistribution of resident Golgi proteins to the endoplasmic reticulum, it prevents recycling of transferrin receptors, but does not inhibit transferrin uptake, overview
additional information
enzyme activity can be inhibited by high levels of acyl acceptors
-
additional information
-
enzyme activity can be inhibited by high levels of acyl acceptors
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.2668
NBD-labelled lysophosphatidylcholine
pH 6.0, 30°C, recombinant enzyme
-
0.005
Arachidonoyl-CoA
Vmax: 12.4 pmol/min/microgram protein for arachidonoyl-CoA
additional information
additional information
Km of NBD-lyso-PC and arachidonoyl CoA by the model of Bi-Bi reaction under optimal conditions. The theoretical Km values calculated by Bi-Bi kinetic equations are more accurate than that calculated by the Michaelis-Menten equation because the apparent Km of one substrate calculated by the Michaelis-Menten equation may be influenced by the concentration of another, whereas Bi-Bi kinetic equations could overcome this disadvantage. From the Lineweaver-Burk plots, a sequential kinetic mechanism can be proposed, but only a sequential Bi-Bi kinetic mechanism can be infered
-
additional information
additional information
-
Km of NBD-lyso-PC and arachidonoyl CoA by the model of Bi-Bi reaction under optimal conditions. The theoretical Km values calculated by Bi-Bi kinetic equations are more accurate than that calculated by the Michaelis-Menten equation because the apparent Km of one substrate calculated by the Michaelis-Menten equation may be influenced by the concentration of another, whereas Bi-Bi kinetic equations could overcome this disadvantage. From the Lineweaver-Burk plots, a sequential kinetic mechanism can be proposed, but only a sequential Bi-Bi kinetic mechanism can be infered
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.268
substrate: alpha-linolenoyl-CoA, 28°C, no cooperativity: Hill number 1.0
0.0001
-
activity in freshly prepared erythrocyte membranes with palmitoyl-CoA as acyl donor
0.0006
-
activity in stored erythrocyte membranes with palmitoyl-CoA as acyl donor
0.0007
-
activity in freshly prepared erythrocyte membranes with oleoyl-CoA as acyl donor
0.024
purified unphosphorylated recombinant enzyme, pH 7.0, 30°C, substrates LPC and palmitoyl CoA
0.065
purified unphosphorylated recombinant enzyme, pH 4.0, 30°C, substrates LPC and palmitoyl CoA
0.652
purified phosphorylated recombinant enzyme, pH 4.0, 30°C, substrates LPC and palmitoyl CoA
0.662
purified phosphorylated recombinant enzyme, pH 7.0, 30°C, substrates LPC and palmitoyl CoA
additional information
additional information
LPCAT3 exhibits the highest activity with lysophosphatidylcholine. LPCAT3 exhibits substrate preferences in the order of 1-stearoyl-2-lysophosphatidylcholine > 1-arachidoyl-2-lysophosphatidylcholine > 1-O-hexadecyl-sn-glycero-3-phosphocholine > 1-palmitoyl-2-lysophosphatidylcholine
additional information
-
LPCAT3 exhibits the highest activity with lysophosphatidylcholine. LPCAT3 exhibits substrate preferences in the order of 1-stearoyl-2-lysophosphatidylcholine > 1-arachidoyl-2-lysophosphatidylcholine > 1-O-hexadecyl-sn-glycero-3-phosphocholine > 1-palmitoyl-2-lysophosphatidylcholine
additional information
LPCAT3 is most active in utilizing linoleoyl-CoA as acyl donor. Order range: linoleoyl-CoA > palmitoyl-CoA > arachidonoyl-CoA > oleoyl-CoA > stearoyl-CoA
additional information
-
LPCAT3 is most active in utilizing linoleoyl-CoA as acyl donor. Order range: linoleoyl-CoA > palmitoyl-CoA > arachidonoyl-CoA > oleoyl-CoA > stearoyl-CoA
additional information
-
among all the different substrates examined, 1-myristoyl-LPC (14:0) and 1-palmitoyl-LPC (16:0) has the most robust activity, whereas no detectable activity is observed using 1-hexanoyl (6:0) and 1-arachidoyl (20:0) LPC as substrates
additional information
-
among the saturated fatty acyl-CoAs, only lauroyl-CoA has comparable activity compared with unsaturated fatty acyl-CoAs. Oleoyl-CoA (18:1), linoleoyl-CoA (18:2), and arachidonoyl-CoA (20:4) all demonstrate robust LPCAT activity
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
priming of Mono-Mac-6 cells by IFNgamma appears to involve LPCAT
-
determined by RT-PCR analysis. Furthermore, peroxisome proliferator-activated receptor alpha agonists dose-dependently regulate LPCAT3 in liver in a peroxisome proliferator-activated receptor alpha-dependent fashion
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Prdx6 is a unique LPCAT enzyme with demonstrated cytoplasmic localization
in addition to endoplasmic reticulum, both isoforms LCAT1 and LCAT2 localize to lipid droplets, which consist of a core of neutral lipids surrounded by a monolayer of phospholipid, mainly phosphatidylcholine. This dual localization is enabled by the monotopic topology of the enzymes with both termini facing the cytoplasm, irrespective of supplementation with oleic acid. Lipid droplets have the ability to locally synthesize phosphatidylcholine and this activity correlates with the LPCAT1 and -2 expression levels
additional information
the remodeling pathway for the repair of peroxidized cell membranes presumably occurs at the cytoplasmic face of the affected cell membrane
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
the liver X receptor-mediated induction of enzyme LPCAT3 specifically regulates the metabolism of arachidonic acid, the precursor of key inflammatory mediators, such as eicosanoids. Liver X receptor and lysophosphatidylcholine acyltransferase 3 modulate the fatty acid composition of human macrophages, overview
physiological function
malfunction
physiological function
malfunction
LPCAT3 knockdown induces a spindle-shaped morphology typical of M1-polarized macrophages, increases the secretion of CXCL10, and decreases the levels of CD206 in interleukin-4-activated U-937 cells. Knockdown of LPCAT3 shifts the differentiation of phorbol ester-treated U-937 cells to M1-polarized macrophages. Decrease in the content of phosphatidylcholine containing linoleic acid or arachidonic acid in biological membranes caused by the suppression of LPCAT3 may influencemembrane fluidity, curvature and function
malfunction
the liver X receptor-mediated effects on arachidonic acid distribution are abolished by LPCAT3 silencing, and a redistribution of arachidonic acid toward the neutral lipid fraction is observed
physiological function
lysophospholipid acyltransferases (LPLATs) regulate the diversification of fatty acid composition in biological membranes. Lysophosphatidylcholine acyltransferases (LPCATs) are members of the LPLATs that play a role in inflammatory responses. LPCAT3 is reported to be a major contributor to increase polyunsaturated fatty acids, including linoleic acid and arachidonic acid, and is associated with inflammatory responses in human primary macrophages, and the enzyme LPCAT3 plays an important role in M1/M2-macrophage polarization, analysis of the underlying mechanism
physiological function
the enzyme is involved in the Lands cycle, it controls the fatty acid composition at the sn-2 position of glycerophospholipids and the availability of fatty acids, such as arachidonic acid, used for eicosanoid synthesis. LPCAT3 gene expression is regulated by liver X receptor in human primary macrophages and monocytes. Liver X receptor stimulation significantly enhances the lysophospholipid acyltransferase activity of LPCAT3 increasing the arachidonic acid content in the polar lipid fraction, specifically in phosphatidylcholines. Preconditioning of human macrophages by LXR agonist treatment increases the release of arachidonate-derived eicosanoids, such as prostaglandin E2 and thromboxane after lipopolysaccharide stimulation, with a significant attenuation by LPCAT3 silencing
physiological function
hepatic lysophosphatidylcholine acyltransferase 3 (LPCAT3) has critical functions in triglycerides transport and endoplasmic reticulum stress response due to its unique ability to catalyze the incorporation of polyunsaturated fatty acids into phospholipids. Hepatic lysophosphatidylcholine acyltransferase 3 is encoded by a target gene regulated by peroxisome proliferator-activated receptor delta
physiological function
lysophosphatidylcholine acyltransferase 3 (LPCAT3) is an important enzyme in phospholipid remodeling, a process that influences the biophysical properties of cell membranes and thus cell function. LPCAT3 is involved in several diseases, including atherosclerosis, non-alcoholic steatohepatitis, and carcinoma
malfunction
LPCAT1 knockdown enhances polyunsaturated fatty acids (PUFAs)-induced cytotoxicity. Transfection of an siRNA against LPCAT1 efficiently reduces protein expression of LPCAT1 in HeLa cells. LPCAT1 knockdown cells show a significant reduction in the amount of DPPC upon eicosapentaenoic acid (EPA; 20:5) treatment compared with siControl-transfected cells, whereas the amounts of EPA-containing species are not affected by LPCAT1 knockdown. Oleic acid treatment has no effect
malfunction
upon hepatitis C virus (HCV) infection, both Huh-7.5.1 cells and primary human hepatocytes (PHH) show decreased levels of LPCAT1 transcript and protein, consistent with transcriptional downregulation. LPCAT1 depletion in either naive or infected Huh-7.5.1 cells results in altered lipid metabolism characterised by lipid droplet remodelling, increased triacylglycerol storage, and increased secretion of VLDL. In infected Huh-7.5.1 cells or PHH, LPCAT1 depletion increases production of the viral particles of lowest density and highest infectivity
physiological function
double knockdown of both isoforms LPCAT1 and LPCAT2 in A-431 cells leads to strong reduction of lipid-droplet-associated enzymic activity
physiological function
double knockdown of both isoforms LPCAT1 and LPCAT2 in A-431 cells or single knockdown of isoform LPCAT1 in Hu-H7 cells leads to strong reduction of lipid-droplet-associated enzymic activity. Reduction of LPCAT1 activity in Hu-H7 cells is associated with a morphological alteration in the lipid droplet pool, the mean lipid droplet size increases, although the amount of stored triacylglycerols remains constant
physiological function
fatty acyl chains of membrane phospholipids are regulated by various lysophospholipid acyltransferases (LPLATs). Cells respond to loading with excess polyunsaturated fatty acids (PUFAs), such as arachidonic acid, eicosapentaenoic acid, and docosahexaenoic acid. Dipalmitoylphosphatidylcholine (DPPC) is increased after the production of PUFA-containing phospholipids in cells loaded with PUFAs. An RNA interference screen of lipid-metabolizing enzymes reveals that lysophosphatidylcholine acyltransferase 1 (LPCAT1) is involved in the DPPC production, overview. Dipalmitoylphosphatidylcholine (DPPC) is produced via LPCAT1 to protect against excess PUFA-induced cytotoxicity
physiological function
lysophosphatidylcholine acyl transferase activity is expressed by peroxiredoxin 6, Prdx6, that shows a strong preference for lysophosphatidylcholine (LPC) as the head group and for palmitoyl CoA in the acylation reaction. The enzyme is a peroxiredoxin-6 (EC 1.11.1.27). Prdx6 also has a phospholipase A 2 (PLA2, EC 3.1.1.4) activity that plays important physiological roles in the synthesis of lung surfactant and in the repair of peroxidized cell membranes. These functions require the activity of a lysophospholipid acyl transferase as a critical component of the phospholipid remodeling pathway. A linear incorporation of labeled fatty acyl CoA into dipalmitoyl phosphatidylcholine (PC) indicated that lysophosphatidylcholine generated by Prdx6 PLA2 activity remains bound to the enzyme for the reacylation reaction. Prdx6 is a complete enzyme comprising both PLA2 and LPCAT activities for the remodeling pathway of PC synthesis or for repair of membrane lipid peroxidation. The remodeling pathway for the repair of peroxidized cell membranes presumably occurs at the cytoplasmic face of the affected cell membrane
physiological function
lysophosphatidylcholine acyltransferase 1 (LPCAT1), as an LD phospholipid-remodelling enzyme, plays a role in liver lipid metabolism and HCV infectious cycle
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MBOA5_HUMAN
487
7
56035
Swiss-Prot
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
Prdx6 is phosphorylated at amino acid T177 by incubation with the MAPK, Erk 2, in the presence of Mg2+-ATP
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D31A
site-directed mutagenesis, construction of mutant endothelial cells via lentivirus transfection
H26A
site-directed mutagenesis, construction of mutant endothelial cells via lentivirus transfection
M427T
naturally occuring mutation, does not significantly affect the activity or function
additional information
additional information
LPCAT3 isozyme knockdown to about 25% activity in U-937 cells by siRNA. LPCAT3 siRNA-transfected cells show a spindle-shaped. morphology similar to that of M1-polarized macrophages, whereas control siRNAtransfected cells show a rounded morphology typical ofM2-polarized macrophages. Knockdown of LPCAT3 in phorbol ester-treated U-937 cells decreases LPCAT activity toward linoleoyl-CoA and arachidonoyl-CoA
additional information
-
in a human hepatoma Huh7 cells, RNA interference-mediated knockdown of LPCAT3 results in virtually complete loss of membrane LPCAT activity, suggesting that LPCAT3 is primarily responsible for hepatic LPCAT activity
additional information
-
membranes from HEK293 cells overexpressing LPCAT3 show significantly increased LPCAT activity as assessed by thin layer chromatography analysis with substrate preference toward unsaturated fatty acids
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant Twin-Strep-tagged enzyme from Sf9 insect cells by membrane preparation, affinity chromatography, and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene LPCAT3, hepatic lysophosphatidylcholine acyltransferase 3 is encoded by a target gene regulated by peroxisome proliferator-activated receptor delta
gene LPCAT3, recombinant expression of C-terminally Twin-Strep-tagged enzyme in Spodoptera frugiperda Sf9 cells
FLAG-tagged version expressed in HEK293T cell, expressed in Escherichia coli BL21 (DE3)
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme LPCAT3 is upregulated by liver X receptor LXR agonists, e.g. T0901317, in human macrophages
hepatic LPCAT3 gene is transcriptionally regulated by peroxisome proliferator-activated receptor delta (PPARdelta). Adenovirus-mediated knockdown of PPARdelta in cultured hepatic cells and liver tissue reduced LPCAT3 mRNA levels, and exogenous overexpression of PPARdelta increases LPCAT3 mRNA expression. Activation of PPARdelta in Hep-G2, Huh-7, and Hepa 1-6 cells with its specific agonists increases LPCAT3 mRNA levels in all three hepatic cell lines. The functional PPAR-responsive element to a proximal region from -135 to -123 of the LPCAT3 promoter plays an essential role in mediating PPARdelta-induced transactivation of the LPCAT3 gene. Upregulation of human LPCAT3 promoter activity in HepG2 cells by PPARdelta agonists, e.g. L165041 and GW0742, and LXR agonist, e.g. GW3965. Specific interaction of PPARdelta with PPRE1 motif of LPCAT3 promoter is enhanced by ligand treatment
lipopolysaccharide significantly downregulates the mRNA expression of isozyme LPCAT3
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
LPCAT3 may have potential as a therapeutic target for diseases, including atherosclerosis, non-alcoholic steatohepatitis, and carcinoma
pharmacology
the enzyme is a potential therapeutic targets for the regulation of immune and inflammatory disorders
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Gehring, L.; Haase, D.; Habben, K.; Kerkhoff, C.; Meyer, H.H.; Kaever, V.
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Homo sapiens
Neville, N.T.; Parton, J.; Harwood, J.L.; Jackson, S.K.
The activities of monocyte lysophosphatidylcholine acyltransferase and coenzyme A-independent transacylase are changed by the inflammatory cytokines tumor necrosis factor alpha and interferon gamma
Biochim. Biophys. Acta
1733
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2005
Homo sapiens
Jackson, S.K.; Parton, J.
Lysophospholipid acyltransferases in monocyte inflammatory responses and sepsis
Immunobiology
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Homo sapiens
Yang, Y.; Cao, J.; Shi, Y.
Identification and characterization of a gene encoding human LPGAT1, an endoplasmic reticulum-associated lysophosphatidylglycerol acyltransferase
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279
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Homo sapiens
Chambers, K.; Judson, B.; Brown, W.J.
A unique lysophospholipid acyltransferase (LPAT) antagonist, CI-976, affects secretory and endocytic membrane trafficking pathways
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Homo sapiens, Rattus norvegicus
Zhao, Y.; Chen, Y.Q.; Bonacci, T.M.; Bredt, D.S.; Li, S.; Bensch, W.R.; Moller, D.E.; Kowala, M.; Konrad, R.J.; Cao, G.
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283
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Homo sapiens
Kazachkov, M.; Chen, Q.; Wang, L.; Zou, J.
Substrate preferences of a lysophosphatidylcholine acyltransferase highlight its role in phospholipid remodeling
Lipids
43
895-902
2008
Homo sapiens (Q6P1A2), Homo sapiens
Matsuda, S.; Inoue, T.; Lee, H.C.; Kono, N.; Tanaka, F.; Gengyo-Ando, K.; Mitani, S.; Arai, H.
Member of the membrane-bound O-acyltransferase (MBOAT) family encodes a lysophospholipid acyltransferase with broad substrate specificity
Genes Cells
13
879-888
2008
Caenorhabditis elegans (O01925), Caenorhabditis elegans, Homo sapiens (Q6P1A2), Homo sapiens
Cao, J.; Shan, D.; Revett, T.; Li, D.; Wu, L.; Liu, W.; Tobin, J.F.; Gimeno, R.E.
Molecular identification of a novel mammalian brain isoform of acyl-CoA:lysophospholipid acyltransferase with prominent ethanolamine lysophospholipid acylating activity, LPEAT2
J. Biol. Chem.
283
19049-19057
2008
Homo sapiens (Q643R3)
Gijon, M.A.; Riekhof, W.R.; Zarini, S.; Murphy, R.C.; Voelker, D.R.
Lysophospholipid acyltransferases and arachidonate recycling in human neutrophils
J. Biol. Chem.
283
30235-30245
2008
Homo sapiens (Q6P1A2), Homo sapiens
Shindou, H.; Shimizu, T.
Acyl-CoA:lysophospholipid acyltransferases
J. Biol. Chem.
284
1-5
2009
Mus musculus (Q3TFD2), Mus musculus (Q8BYI6), Mus musculus (Q8R3I2), Mus musculus (Q91V01), Homo sapiens (Q6P1A2), Homo sapiens (Q6ZWT7), Homo sapiens (Q7L5N7), Homo sapiens (Q8NF37)
Perez-Chacon, G.; Astudillo, A.M.; Ruiperez, V.; Balboa, M.A.; Balsinde, J.
Signaling role for lysophosphatidylcholine acyltransferase 3 in receptor-regulated arachidonic acid reacylation reactions in human monocytes
J. Immunol.
184
1071-1078
2010
Homo sapiens
Jain, S.; Zhang, X.; Khandelwal, P.J.; Saunders, A.J.; Cummings, B.S.; Oelkers, P.
Characterization of human lysophospholipid acyltransferase 3
J. Lipid Res.
50
1563-1570
2009
Homo sapiens (Q6P1A2), Homo sapiens
Harayama, T.; Shindou, H.; Shimizu, T.
Biosynthesis of phosphatidylcholine by human lysophosphatidylcholine acyltransferase 1
J. Lipid Res.
50
1824-1831
2009
Homo sapiens (Q8NF37), Homo sapiens
Mansilla, F.; da Costa, K.A.; Wang, S.; Kruh?ffer, M.; Lewin, T.M.; Orntoft, T.F.; Coleman, R.A.; Birkenkamp-Demtroeder, K.
Lysophosphatidylcholine acyltransferase 1 (LPCAT1) overexpression in human colorectal cancer
J. Mol. Med.
87
85-97
2009
Homo sapiens (Q8NF37), Homo sapiens
Jackson, S.K.; Abate, W.; Tonks, A.J.
Lysophospholipid acyltransferases: novel potential regulators of the inflammatory response and target for new drug discovery
Pharmacol. Ther.
119
104-114
2008
Bos taurus, Rattus norvegicus, Mus musculus (Q3TFD2), Homo sapiens (Q8NF37)
Moessinger, C.; Kuerschner, L.; Spandl, J.; Shevchenko, A.; Thiele, C.
Human lysophosphatidylcholine acyltransferases 1 and 2 are located in lipid droplets where they catalyze the formation of phosphatidylcholine
J. Biol. Chem.
286
21330-21339
2011
Homo sapiens (Q7L5N7), Homo sapiens (Q8NF37), Homo sapiens
Ishibashi, M.; Varin, A.; Filomenko, R.; Lopez, T.; Athias, A.; Gambert, P.; Blache, D.; Thomas, C.; Gautier, T.; Lagrost, L.; Masson, D.
Liver X receptor regulates arachidonic acid distribution and eicosanoid release in human macrophages: a key role for lysophosphatidylcholine acyltransferase 3
Arterioscler. Thromb. Vasc. Biol.
33
1171-1179
2013
Homo sapiens (Q6P1A2), Homo sapiens
Taniguchi, K.; Hikiji, H.; Okinaga, T.; Hashidate-Yoshida, T.; Shindou, H.; Ariyoshi, W.; Shimizu, T.; Tominaga, K.; Nishihara, T.
Essential role of lysophosphatidylcholine acyltransferase 3 in the induction of macrophage polarization in PMA-treated U937 cells
J. Cell. Biochem.
116
2840-2848
2015
Homo sapiens (Q6P1A2)
Kawana, H.; Kano, K.; Shindou, H.; Inoue, A.; Shimizu, T.; Aoki, J.
An accurate and versatile method for determining the acyl group-introducing position of lysophospholipid acyltransferases
Biochim. Biophys. Acta
1864
1053-1060
2019
Mus musculus (Q3TFD2), Mus musculus (Q3UN02), Mus musculus (Q91V01), Homo sapiens (Q8NF37)
Akagi, S.; Kono, N.; Ariyama, H.; Shindou, H.; Shimizu, T.; Arai, H.
Lysophosphatidylcholine acyltransferase 1 protects against cytotoxicity induced by polyunsaturated fatty acids
FASEB J.
30
2027-2039
2016
Mus musculus (Q3TFD2), Mus musculus, Homo sapiens (Q8NF37)
Du, X.; Hu, J.; Zhang, Q.; Liu, Q.; Xiang, X.; Dong, J.; Lou, B.; He, S.; Gu, X.; Cao, Y.; Li, Y.; Ding, T.
A novel assay for measuring recombinant human lysophosphatidylcholine acyltransferase 3 activity
FEBS open bio
9
1734-1743
2019
Homo sapiens (Q6P1A2), Homo sapiens
Beilstein, F.; Lemasson, M.; Pene, V.; Rainteau, D.; Demignot, S.; Rosenberg, A.R.
Lysophosphatidylcholine acyltransferase 1 is downregulated by hepatitis C virus impact on production of lipo-viro-particles
Gut
66
2160-2169
2017
Homo sapiens (Q8NF37), Homo sapiens
Singh, A.B.; Liu, J.
Identification of hepatic lysophosphatidylcholine acyltransferase 3 as a novel target gene regulated by peroxisome proliferator-activated receptor delta
J. Biol. Chem.
292
884-897
2017
Homo sapiens (Q6P1A2), Mus musculus (Q91V01), Mus musculus
Fisher, A.B.; Dodia, C.; Sorokina, E.M.; Li, H.; Zhou, S.; Raabe, T.; Feinstein, S.I.
A novel lysophosphatidylcholine acyl transferase activity is expressed by peroxiredoxin 6
J. Lipid Res.
57
587-596
2016
Mus musculus (O08709), Mus musculus, Rattus norvegicus (O35244), Homo sapiens (P30041), Mus musculus C57BL/6J (O08709)
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