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Information on EC 2.3.1.23 - 1-acylglycerophosphocholine O-acyltransferase and Organism(s) Rattus norvegicus and UniProt Accession O35244

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EC Tree
IUBMB Comments
Acts preferentially with unsaturated acyl-CoA derivatives. 1-Acyl-sn-glycero-3-phosphoinositol can also act as acceptor.
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This record set is specific for:
Rattus norvegicus
UNIPROT: O35244
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The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
pcat1, lpcat3, lpcat, lysophosphatidylcholine acyltransferase, alcat1, lpcat2, lysolecithin acyltransferase, lycat, lyso-paf acetyltransferase, lysophosphatidylcholine acyltransferase 1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
lysophosphatidylcholine acyl transferase
-
1-acyl-sn-glycero-3-phosphocholine acyltransferase
-
-
-
-
1-acylglycerophosphocholine acyltransferase
-
-
acetyl-CoA:1-O-alkyl-sn-glycero-3-phosphocholine acetyltransferase
-
-
acyl coenzyme A-monoacylphosphatidylcholine acyltransferase
-
-
-
-
acyl-CoA:1-acyl-glycero-3-phosphocholine transacylase
-
-
-
-
acyltransferase, lysolecithin
-
-
-
-
LPCAT
lung-type acyl-CoA:lysophosphatidylcholine acyltransferase 1
-
lyso-PAF acetyltransferase
-
-
lysolecithin acyltransferase
-
-
-
-
lysoPC acyltransferase
-
lysophosphatide acyltransferase
-
-
-
-
lysophosphatidylcholine acyltransferase
lysophospholipid acyltransferase
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -, -, -, -, -
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 hide
9027-64-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
palmitoyl-CoA + 1-palmitoyl-sn-glycero-3-phosphocholine
CoA + 1,2-dipalmitoyl-sn-glycero-3-phosphocholine
show the reaction diagram
acyl-CoA + 1-acyl-sn-glycero-3-phosphocholine
CoA + 1,2-diacyl-sn-glycero-3-phosphocholine
show the reaction diagram
acyl-CoA + 1-acyl-sn-glycero-3-phosphoryldimethylethanolamine
CoA + 1,2-diacyl-sn-glycero-3-phosphoryldimethylethanolamine
show the reaction diagram
-
preferred acyl acceptors in descending order: 1-acyl-sn-glycero-3-phosphocholine, 1-acyl-sn-glycero-3-phosphoryldimethylethanolamine, 1-acyl-sn-glycero-3-phosphorylmonomethylethanolamine, 1-acyl-sn-glycero-3-phosphorylethanolamine
-
?
acyl-CoA + 1-acyl-sn-glycero-3-phosphorylethanolamine
CoA + 1,2-diacyl-sn-glycero-3-phosphorylethanolamine
show the reaction diagram
-
-
-
?
acyl-CoA + 1-acyl-sn-glycero-3-phosphorylmonomethylethanolamine
CoA + 1,2-diacyl-sn-glycero-3-phosphorylmonomethylethanolamine
show the reaction diagram
-
-
-
?
acyl-CoA + 1-myristoyl-sn-glycero-3-phosphocholine
CoA + 1-myristoyl-2-acyl-sn-glycero-3-phosphocholine
show the reaction diagram
-
preferred acyl acceptors: 1-myristyl-sn-glycero-3-phosphocholine, 1-stearyl-sn-glycero-3-phosphocholine, 1-oleoyl-sn-glycero-3-phosphocholine and 1-linoleoyl-sn-glycero-3-phosphocholine, very little activity with 1-decanoyl-sn-glycero-3-phosphocholine
-
?
acyl-CoA + 1-palmitoyl-sn-glycero-3-phosphocholine
CoA + 1-palmitoyl-2-acyl-sn-glycero-3-phosphocholine
show the reaction diagram
-
at 0.16 mM 1-palmitoyl-sn-glycero-3-phosphocholine is preferred 3.5fold over 1-stearoyl-sn-glycero-3-phosphocholine
-
r
arachidonoyl-CoA + 1-acyl-sn-glycero-3-phosphocholine
CoA + 1-acyl-2-arachidonoyl-sn-glycero-3-phosphocholine
show the reaction diagram
arachidonoyl-CoA + 1-acyl-sn-glycero-3-phosphoethanolamine
CoA + 1-acyl-2-arachidonoyl-sn-glycero-3-phosphoethanolamine
show the reaction diagram
arachidonoyl-CoA + 1-acyl-sn-glycero-3-phosphoinositol
CoA + 1-acyl-2-arachidonoyl-sn-glycero-3-phosphoinositol
show the reaction diagram
arachidonoyl-CoA + 1-acyl-sn-glycero-3-phosphoserine
CoA + 1-acyl-2-arachidonoyl-sn-glycero-3-phosphoserine
show the reaction diagram
linoleoyl-CoA + 1-acyl-sn-glycero-3-phosphocholine
CoA + 1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine
show the reaction diagram
lysophosphatidylcholine + acyl-CoA
phosphatidylcholine + CoA
show the reaction diagram
-
-
-
-
?
myristoyl-CoA + 1-acyl-sn-glycero-3-phosphocholine
CoA + 1-acyl-2-myristoyl-sn-glycero-3-phosphocholine
show the reaction diagram
-
-
-
r
oleoyl-CoA + 1-acyl-sn-glycero-3-phosphocholine
CoA + 1-acyl-2-oleoyl-sn-glycero-3-phosphocholine
show the reaction diagram
palmitoyl-CoA + 1-acyl-sn-glycero-3-phosphocholine
CoA + 1-acyl-2-palmitoyl-sn-glycero-3-phosphocholine
show the reaction diagram
-
-
-
r
palmitoyl-CoA + lysophosphatidylcholine
CoA + ?
show the reaction diagram
-
-
-
-
?
stearoyl-CoA + 1-acyl-sn-glycero-3-phosphocholine
CoA + 1-acyl-2-stearoyl-sn-glycero-3-phosphocholine
show the reaction diagram
-
-
-
-
r
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
palmitoyl-CoA + 1-palmitoyl-sn-glycero-3-phosphocholine
CoA + 1,2-dipalmitoyl-sn-glycero-3-phosphocholine
show the reaction diagram
-
-
-
?
acyl-CoA + 1-acyl-sn-glycero-3-phosphocholine
CoA + 1,2-diacyl-sn-glycero-3-phosphocholine
show the reaction diagram
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CI-976
about 50% inhibition at 0.01 mM
1-acyl-sn-glycero-3-phosphocholine
-
high concentration, lung enzyme
2,2-dimethyl-N-(2,4,6-trimethoxyphenyl)-dodecanamide
-
-
2,2-dimethyl-N-(2,4,6-trimethoxyphenyl)dodecanamide
-
-
2-methoxy-5-methyl-3-tetradecanoyloxy-1,4-benzoquinone
-
potent inhibitor
3,4-dihydroxy-1,2-dimethoxy-5-methylbenzene
-
-
3-acetoxy-2-methoxy-5-methyl-1,4-benzoquinone
-
-
3-decanoyloxy-2-methoxy-5-methyl-1,4-benzoquinone
-
potent inhibitor
3-hexanoyloxy-2-methoxy-5-methyl-1,4-benzoquinone
-
-
acyl-CoA
-
-
Brij 35
-
0.1%
Brij 98
-
0.1%
CI-976
-
complete inhibition at 0.05 mM, IC50: 0.015 mM, 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, overview
Clofibric acid
-
inhibition of mitochondrial enzyme
Cyclic nucleotide phosphodiesterase inhibitors
-
liver and heart enzyme
-
dihydrofumigatin
-
i.e. 2-methoxy-1,3,4- trihydroxy-5-methylbenzene
fumigatin
-
i.e. 3-hydroxy-2-methoxy-5-methyl-1,4-benzoquinone
iodoacetate
-
liver enzyme
Lubrol WX
-
0.1%
-
methanol
-
oleoyl-CoA as substrate
N-ethylmaleimide
p-chloromercuribenzoate
-
partially restorable by dithiothreitol
p-chloromercuriphenyl sulfonic acid
Phosphorylhomocholine
-
-
photooxidized phospholipids
-
0.0001-0.01 mM photoxoidized phospholipids preincubated with 0.1 mg microsomal membranes, approx. 45% loss of initial activity
-
Pronase
-
-
-
Triton X-100
Trypsin
-
-
-
Tween 20
-
0.1%
Tween 80
-
0.1%
WY-14643
-
inhibition of mitochondrial enzyme
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dioleoylphosphatidylcholine
-
incorporation in membrane elevates acyltransferase activity
egg yolk phosphatidylcholine
-
incorporation in membrane elevates acyltransferase activity
-
methanol
-
activation, arachidonoyl-CoA as substrate
phosphatidylethanolamine
-
incorporation in membrane elevates acyltransferase activity
phosphatidylinositol
-
incorporation in membrane elevates acyltransferase activity
phosphatidylserine
-
incorporation in membrane elevates acyltransferase activity
additional information
glucocorticoids and fibroblast growth factor induce the enzyme
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0032
Arachidonoyl-CoA
-
-
0.0035
linoleoyl-CoA
-
-
0.0028
oleoyl-CoA
-
-
0.0027
palmitoyl-CoA
-
-
additional information
additional information
-
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.02
2-methoxy-5-methyl-3-tetradecanoyloxy-1,4-benzoquinone
Rattus norvegicus
-
at pH 6.9 and 37°C
0.166
3,4-dihydroxy-1,2-dimethoxy-5-methylbenzene
Rattus norvegicus
-
at pH 6.9 and 37°C
0.391
3-acetoxy-2-methoxy-5-methyl-1,4-benzoquinone
Rattus norvegicus
-
at pH 6.9 and 37°C
0.003
3-decanoyloxy-2-methoxy-5-methyl-1,4-benzoquinone
Rattus norvegicus
-
at pH 6.9 and 37°C
0.139
3-hexanoyloxy-2-methoxy-5-methyl-1,4-benzoquinone
Rattus norvegicus
-
at pH 6.9 and 37°C
0.015
CI-976
Rattus norvegicus
-
complete inhibition at 0.05 mM, IC50: 0.015 mM, 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, overview
0.101
dihydrofumigatin
Rattus norvegicus
-
at pH 6.9 and 37°C
0.109
fumigatin
Rattus norvegicus
-
at pH 6.9 and 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.028
purified unphosphorylated recombinant enzyme, pH 7.0, 30°C, substrates LPC and palmitoyl CoA
0.068
purified unphosphorylated recombinant enzyme, pH 4.0, 30°C, substrates LPC and palmitoyl CoA
0.661
purified phosphorylated recombinant enzyme, pH 7.0, 30°C, substrates LPC and palmitoyl CoA
0.662
purified phosphorylated recombinant enzyme, pH 4.0, 30°C, substrates LPC and palmitoyl CoA
0.0028
-
crude extract, TLC assay
0.0029
-
crude extract, silic acid microcolumn assay
0.01
-
partially purified enzyme, 1-palmitoyl-glycero-3-phosphocholine as substrate
0.013
-
acyl donor oleoyl-CoA, heart enzyme
0.058
-
acyl donor oleoyl-CoA, liver enzyme
0.68
-
acyl donor arachidonoyl-CoA
2.3
-
acyl donor arachidonoyl-CoA
additional information
-
activity is different in either its microsomal environment or vesicles and is affected by the phospholipid molecular species environment
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 8
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 8.5
-
approx. half-maximal activity at pH 5.5 and 8.5
6 - 10
-
pH 6.0: about 55% of maximal activity, pH 10.0: about 80% of maximal activity, Golgi-associated enzyme
6 - 9
-
approx. half-maximal activity at pH 6.0 and 9.6
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
low activity
Manually annotated by BRENDA team
-
very low activity
Manually annotated by BRENDA team
additional information
expression tissue distribution, overview
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
Prdx6 is a unique LPCAT enzyme with demonstrated cytoplasmic localization
Manually annotated by BRENDA team
additional information
the remodeling pathway for the repair of peroxidized cell membranes presumably occurs at the cytoplasmic face of the affected cell membrane
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
metabolism
-
key enzyme in platelet-activating factor biosynthesis
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PRDX6_RAT
224
0
24819
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
225000
-
gel filtration
63000
x * 63000, recombinant enzyme, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
one major protein of 21000 Da after purification of the enzyme from vesicles
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
oleoyl-CoA specific activity loses 50% of activity after 90 min, arachidonoyl-CoA specific activity loses 45% of activity after 90 min
43
-
half-life: 12 min
45
-
10% loss of activity after 1 min
48
-
half-life: 1 min, oleoyl-CoA specific activity
50
-
50% loss of activity after 1 min
52
-
half-life: 1 min, arachidonoyl-CoA specific activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
glycerol, 50%, stabilizes
-
low ionic strength stabilizes during purification
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, multiple freeze-thawing cycles, 6 weeks, 20% loss of activity
-
-20°C, partially purified enzyme, several months
-
-20°C, purified enzyme, at least 3 weeks
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme rPrdx6 by anion exchange chromatography
partially purified
-
partially purified from vesicles
-
solubilized by detergent effect of substrates lysolecithin and oleoyl-CoA, ratio 1:1
-
solubilized with Triton X-100
-
Ultrogel AcA 34
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene prdx6, recombinant enzyme expression
LPCAT, DNA and amino acid sequence determination and analysis, functional expression in COS-7 cells and HEK-293 cells
LPCAT1, DNA and amino acid sequence determination and analysis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yamashita, S.; Hosaka, K.; Miki, Y.; Numa, S.
Glycerolipid acyltransferases from rat liver: 1-acylglycerophosphate acyltransferase, 1-acylglycerophosphorylcholine acyltransferase, and diacylglycerol acyltransferase
Methods Enzymol.
71
528-536
1981
Rattus norvegicus
Manually annotated by BRENDA team
Koshlukova, S.; Momchilova-Pankova, A.; Markovska, T.; Kumanov, K.
Phospholipid dependence of rat liver microsomal acyl:CoA synthetase and acyl-CoA:1-acyl-sn-glycero-3-phosphocholine O-acyltransferase
J. Membr. Biol.
127
113-119
1992
Rattus norvegicus
Manually annotated by BRENDA team
Gavino, V.C.; Deamer, D.W.
Purification of acyl CoA:1-acyl-sn-glycero-3-phosphorylcholine acyltransferase
J. Bioenerg. Biomembr.
14
513-526
1982
Rattus norvegicus
Manually annotated by BRENDA team
Lands, W.E.M.; Hart, P.
Metabolism of glycerolipids. VI. Specificities of acyl-CoA: phospholipid acyltransferases
J. Biol. Chem.
240
1905-1911
1965
Bos taurus, Cavia porcellus, Mesocricetus auratus, Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Choy, P.C.; Tardi, P.G.; Mukherjee, J.J.
Lysophosphatidylcholine acyltransferase
Methods Enzymol.
209
80-86
1992
Bos taurus, Cavia porcellus, Oryctolagus cuniculus, Mammalia, Rattus norvegicus
Manually annotated by BRENDA team
Hill, E.E.; Lands, W.E.M.
Incorporation of long-chain and polyunsaturated acids into phosphatidate and phosphatidylcholine
Biochim. Biophys. Acta
152
645-648
1968
Cavia porcellus, Rattus norvegicus
Manually annotated by BRENDA team
Bouroudian, M.; Chautan, M.; Termine, E.; Lafont, H.; Nalbone, G.
Use of a silicic acid microcolumn to assay acyl-CoA: lysophosphatidylcholine acyltransferase
Biochim. Biophys. Acta
960
253-256
1988
Rattus norvegicus
Manually annotated by BRENDA team
Holub, B.J.; Piekarski, J.; Possmayer, F.
Relative suitability of 1-palmitoyl and 1-stearoyl homologues of 1-acyl-sn-glycerylphosphorylcholine and different acyl donors for phosphatidylcholine synthesis via acyl-CoA:1-acyl-sn-glycero-3-phosphorylcholine acyltransferase in rat lung microsomes
Can. J. Biochem.
58
434-439
1980
Rattus norvegicus
Manually annotated by BRENDA team
Van den Bosch, H.; Van Golde, L.M.G.; Eibl, H.; Van Deenen, L.L.M.
The acylation of 1-acylglycero-3-phosphorylcholines by rat-liver microsomes
Biochim. Biophys. Acta
144
613-623
1967
Rattus norvegicus
Manually annotated by BRENDA team
Yamashita, S.; Nakaya, N.; Miki, Y.; Numa, S.
Separation of 1-acylglycerolphosphate acyltransferase and 1-acylglycerolphosphorylcholine acyltransferase of rat liver microsomes
Proc. Natl. Acad. Sci. USA
72
600-603
1975
Rattus norvegicus
Manually annotated by BRENDA team
Miki, Y.; Hosaka, K.; Yamashita, S.; Handa, H.; Numa, S.
Acyl-acceptor specificities of 1-acylglycerolphosphate acyltransferase and 1-acylglycerophosphorylcholine acyltransferase resolved from rat liver microsomes
Eur. J. Biochem.
81
433-441
1977
Rattus norvegicus
Manually annotated by BRENDA team
Holub, B.J.; Macnaughton, J.A.; Piekarski, J.
Synthesis of 1-palmitoyl and 1-stearoyl phosphatidylcholines from mixtures of acyl acceptors via acyl-CoA:1-acyl-sn-glycero-3-phosphorylcholine acyltransferase in liver microsomes
Biochim. Biophys. Acta
572
413-422
1979
Rattus norvegicus
Manually annotated by BRENDA team
Hasegawa-Sasaki, H.; Ohno, K.
Extraction and partial purification of acyl-CoA:1-acyl-sn-glycero-3-phosphocholine acyltransferase from rat liver microsomes
Biochim. Biophys. Acta
617
205-217
1980
Rattus norvegicus
Manually annotated by BRENDA team
Renooij, W.; Snyder, F.
Transmembrane orientation of palmitoyl-CoA: lysophosphatidylcholine acyltransferase in microsomes isolated from an alveolar type II cell adenoma and rat liver
Biochim. Biophys. Acta
666
468-474
1981
Mus musculus, Mus musculus BALB/c, Rattus norvegicus
Manually annotated by BRENDA team
Iritani, N.; Ikeda, Y.; Kajitani, H.
Selectivities of 1-acylglycerophosphorylcholine acyltransferase and acyl-CoA synthetase for n-3 polyunsaturated fatty acids in platelets and liver microsomes
Biochim. Biophys. Acta
793
416-422
1984
Rattus norvegicus
Manually annotated by BRENDA team
Momchilova, A.B.; Markovska, T.T.; Koshlukova, S.E.; Koumanov, K.S.; Pankov, R.G.
Phospholipid modifications influence acyl-CoA:1-acyl-glycero-3-phosphocholine O-acyltransferase in rat liver plasma membranes
Biochem. Cell Biol.
69
643-648
1991
Rattus norvegicus
Manually annotated by BRENDA team
Yamashita, S.; Hosaka, K.; Numa, S.
Acyl-donor specificities of partially purified 1-acylglycerophosphate acyltransferase, 2-acylglycerophosphate acyltransferase and 1-acylglycerophosphorylcholine acyltransferase from rat-liver microsomes
Eur. J. Biochem.
38
25-31
1973
Rattus norvegicus
Manually annotated by BRENDA team
Alberghina, M.; Lupo, G.; Anfuso, C.D.; el Ghonemy, S.H.
Lipid peroxidation inhibits acyl-CoA:-1-acyl-sn-glycero-3-phosphocholine O-acyltransferase but not CTP: phosphocholine cytidylyltransferase activity in rat brain membranes
Neurochem. Int.
26
477-487
1995
Rattus norvegicus
Manually annotated by BRENDA team
Fyrst, H.; Pham, D.V.; Lubin, B.H.; Kuypers, F.A.
Formation of vesicles by the action of acyl-CoA:1-acyllsophosphatidylcholine acyltransferase from rat liver microsomes: optimal solubilization conditions and analysis of lipid composition and enzyme activity
Biochemistry
35
2644-2650
1996
Rattus norvegicus
Manually annotated by BRENDA team
Chambers, K.; Brown, W.J.
Characterization of a novel CI-976-sensitive lysophospholipid acyltransferase that is associated with the Golgi complex
Biochem. Biophys. Res. Commun.
313
681-686
2004
Rattus norvegicus
Manually annotated by BRENDA team
Drecktrah, D.; Chambers, K.; Racoosin, E.L.; Cluett, E.B.; Gucwa, A.; Jackson, B.; Brown, W.J.
Inhibition of a Golgi complex lysophospholipid acyltransferase induces membrane tubule formation and retrograde trafficking
Mol. Biol. Cell
14
3459-3469
2003
Rattus norvegicus
Manually annotated by BRENDA team
Nakanishi, H.; Shindou, H.; Hishikawa, D.; Harayama, T.; Ogasawara, R.; Suwabe, A.; Taguchi, R.; Shimizu, T.
Cloning and characterization of mouse lung-type acyl-CoA:lysophosphatidylcholine acyltransferase 1 (LPCAT1). Expression in alveolar type II cells and possible involvement in surfactant production
J. Biol. Chem.
281
20140-20147
2006
Rattus norvegicus (Q1HAQ0), Mus musculus (Q3TFD2), Mus musculus
Manually annotated by BRENDA team
Chambers, K.; Judson, B.; Brown, W.J.
A unique lysophospholipid acyltransferase (LPAT) antagonist, CI-976, affects secretory and endocytic membrane trafficking pathways
J. Cell Sci.
118
3061-3071
2005
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Chen, X.; Hyatt, B.A.; Mucenski, M.L.; Mason, R.J.; Shannon, J.M.
Identification and characterization of a lysophosphatidylcholine acyltransferase in alveolar type II cells
Proc. Natl. Acad. Sci. USA
103
11724-11729
2006
Rattus norvegicus (Q1HAQ0), Mus musculus (Q3TFD2), Mus musculus
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
Yamazaki, Y.; Yasuda, K.; Matsuyama, T.; Ishihara, T.; Higa, R.; Sawairi, T.; Yamaguchi, M.; Egi, M.; Akai, S.; Miyase, T.; Ikari, A.; Miwa, M.; Sugatani, J.
A Penicillium sp. F33 metabolite and its synthetic derivatives inhibit acetyl-CoA:1-O-alkyl-sn-glycero-3-phosphocholine acetyltransferase (a key enzyme in platelet-activating factor biosynthesis) and carrageenan-induced paw edema in mice
Biochem. Pharmacol.
86
632-644
2013
Rattus norvegicus
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team