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EC Tree
The taxonomic range for the selected organisms is: Rattus norvegicus The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
lyso-paf-at, acetyl-coa:lyso-paf acetyltransferase, lyso-paf at, lyso-paf:acetyl-coa acetyltransferase, lyso-paf-acetyltransferase, acetyl-coa lyso-paf acetyltransferase, lyso-paf-act, lyso-pafat, lysopafat, lysopaf-at,
more
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1-alkyl-2-lyso-sn-glycero-3-phosphocholine acetyltransferase
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acetyl-CoA:1-alkyl-2-lyso-sn-glycero-3-phosphocholine 2-O-acetyltransferase
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acetyl-CoA:lyso-PAF acetyltransferase
acetyltransferase, 1-alkyl-2-lysolecithin
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acetyltransferase, 1-alkylglycerophosphocholine
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acyl-CoA:1-alkyl-sn-glycero-3-phosphocholine acyltransferase
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blood platelet-activating factor acetyltransferase
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lyso-GPC:acetyl CoA acetyltransferase
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lyso-platelet activating factor:acetyl-CoA acetyltransferase
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lyso-platelet-activating factor:acetyl-CoA acetyltransferase
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lysoPAF:acetyl CoA acetyltransferase
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PAF acetyltransferase
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platelet-activating factor acylhydrolase
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platelet-activating factor-synthesizing enzyme
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acetyl-CoA:lyso-PAF acetyltransferase
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acetyl-CoA:lyso-PAF acetyltransferase
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Acyl group transfer
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acetyl-CoA:1-alkyl-sn-glycero-3-phosphocholine 2-O-acetyltransferase
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acetyl-CoA + 1-palmitoyl-2-lyso-sn-glycero-3-phosphocholine
CoA + 2-acetyl-1-palmitoyl-sn-glycero-3-phosphocholine
acetyl-CoA + acyl-lyso-glycero-3-phosphocholine
CoA + acetyl-acyl-glycero-3-phosphocholine
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worse substrate than alkyl-lyso-glycero-3-phosphocholine
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?
acetyl-CoA + alkyl-lyso-glycero-3-phosphoethanolamine
CoA + 2-acetyl-alkyl-glycero-3-phosphoethanolamine
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least enzyme activity
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?
acetyl-CoA + alkyl-lyso-monomethylethanamine
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?
acetyl-CoA + alkyl-lyso-N',N'-dimethylethanamine
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?
acetyl-CoA + alkyl-sn-glycero-3-phosphocholine
CoA + 2-acetyl-1-alkyl-sn-glycero-3-phosphocholine
acetyl-CoA + octadecyl-lyso-sn-glycero-3-phosphocholine
CoA + 2-acetyl-1-octadecyl-sn-glycero-3-phosphocholine
butyryl-CoA + 1-alkyl-2-lyso-sn-glycero-3-phosphocholine
2-butyryl-1-alkyl-sn-glycero-3-phosphocholine
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?
hexanoyl-CoA + 1-alkyl-2-lyso-sn-glycero-3-phosphocholine
2-hexanoyl-1-alkyl-sn-glycero-3-phosphocholine
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?
oleoyl-CoA + alkyl-lyso-glycero-3-phosphoethanolamine
CoA + 1-alkyl-2-oleoyl-glycero-3-phosphoethanolamine
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10% of the activity observed in presence of acetyl-CoA
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?
palmitoyl-CoA + alkyl-lyso-glycero-3-phosphoethanolamine
CoA + acetyl-2-palmitoyl-glycero-3-phosphoethanolamine
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5% of the activity observed in presence of acetyl-CoA
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?
propionyl-CoA + alkyl-lyso-glycero-phosphocholine
CoA + 2-propionyl-1-alkyl-sn-glycero-3-phosphocholine
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acetyl-CoA + 1-palmitoyl-2-lyso-sn-glycero-3-phosphocholine
CoA + 2-acetyl-1-palmitoyl-sn-glycero-3-phosphocholine
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rate reduced to 50%
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?
acetyl-CoA + 1-palmitoyl-2-lyso-sn-glycero-3-phosphocholine
CoA + 2-acetyl-1-palmitoyl-sn-glycero-3-phosphocholine
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12% of the activity observed in presence of alkyl-lyso-sn-glycero-phosphocholine
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?
acetyl-CoA + 1-palmitoyl-2-lyso-sn-glycero-3-phosphocholine
CoA + 2-acetyl-1-palmitoyl-sn-glycero-3-phosphocholine
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rate of synthesis is 55% of the rate observed with the ether linked substrate
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?
acetyl-CoA + alkyl-sn-glycero-3-phosphocholine
CoA + 2-acetyl-1-alkyl-sn-glycero-3-phosphocholine
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?
acetyl-CoA + alkyl-sn-glycero-3-phosphocholine
CoA + 2-acetyl-1-alkyl-sn-glycero-3-phosphocholine
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?
acetyl-CoA + alkyl-sn-glycero-3-phosphocholine
CoA + 2-acetyl-1-alkyl-sn-glycero-3-phosphocholine
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?
acetyl-CoA + alkyl-sn-glycero-3-phosphocholine
CoA + 2-acetyl-1-alkyl-sn-glycero-3-phosphocholine
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?
acetyl-CoA + alkyl-sn-glycero-3-phosphocholine
CoA + 2-acetyl-1-alkyl-sn-glycero-3-phosphocholine
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?
acetyl-CoA + alkyl-sn-glycero-3-phosphocholine
CoA + 2-acetyl-1-alkyl-sn-glycero-3-phosphocholine
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?
acetyl-CoA + alkyl-sn-glycero-3-phosphocholine
CoA + 2-acetyl-1-alkyl-sn-glycero-3-phosphocholine
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the higher the degree of methylation of the nitrogen base, the lower the enzyme activity
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?
acetyl-CoA + alkyl-sn-glycero-3-phosphocholine
CoA + 2-acetyl-1-alkyl-sn-glycero-3-phosphocholine
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the longer the acyl-CoA length, the smaller the values of apparent Km and Vmax
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?
acetyl-CoA + alkyl-sn-glycero-3-phosphocholine
CoA + 2-acetyl-1-alkyl-sn-glycero-3-phosphocholine
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alkyl-lyso-sn-glycero-3-phosphocholine is preferred to its saturated counterpart as substrate
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?
acetyl-CoA + octadecyl-lyso-sn-glycero-3-phosphocholine
CoA + 2-acetyl-1-octadecyl-sn-glycero-3-phosphocholine
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?
acetyl-CoA + octadecyl-lyso-sn-glycero-3-phosphocholine
CoA + 2-acetyl-1-octadecyl-sn-glycero-3-phosphocholine
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?
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Ca2+
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activation reversed by addition of EGTA in excess of Ca2+, Ca2+ reduces the apparent Km for acetyl-CoA, maximum effect between 0.0001 and 0.01 mM, the action of Ca2+ seems to be independent of the presence of calmodulin or phosphorylation
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1-methoxyphaseolidin
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IC50: 0.048 mM
1-methoxyphaseolin
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IC50: 0.057 mM
2-methoxy-5-methyl-3-tetradecanoyloxy-1,4-benzoquinone
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derivative of a metabolite from Penicillium sp. F33 , strong inhibition. Compound also significantly suppresses the gene expression of lyso-PAF acetyltransferase/LPCAT2 in mouse bone marrow-derived macrophages stimulated by lipopolysaccharide
3-decanoyloxy-2-methoxy-5-methyl-1,4-benzoquinone
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derivative of a metabolite from Penicillium sp. F33 , strong inhibition. Compound also significantly suppresses the gene expression of lyso-PAF acetyltransferase/LPCAT2 in mouse bone marrow-derived macrophages stimulated by lipopolysaccharide
4-(1-Naphthylvinyl)pyridine
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IC50: 0.043 mM
6,8-diprenylgenistein
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IC50: 0.019 mM
acetyl-salicylic acid
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weak inhibition
baicalein
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IC50: 0.148 mM
chiyusaponin
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IC50: 0.2 mM
dexamethasone
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2 mg/kg for 3 days in liver and spleen
diisopropylfluorophosphate
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98% inhibition at 10 mM
indomethacin
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weak inhibition at 1 mM
licoricidin
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IC50: 0.0077 mM
luteolin
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IC50: 0.045 mM
medroxyprogesterone
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50 mg/kg in liver
nordihydroguaiaretic acid
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IC50: 0.29 mM
p-bromophenacyl bromide
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90% inhibition at 0.1 mM
palmitoyl-CoA
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85% inhibition at 10 uM due to detergent effect
palmitoyllyso-glycero-3-phosphocholine
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competitive inhibitor for alkyl-sn-glycero-3-phosphocholine
quercetin
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IC50: 0.08 mM
sodium dodecylsulfate
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inactivation at 0.1%
Triton X-100
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75 and 95% inhibition at 0.2 and 0.6 mM respectively due to detergent
Urea
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inactivation at 8 mM
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AMP-dependent protein kinase
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activity increases 2-3fold in presence of MgATP2-, activation is reversible, stimulation is optimal with 30 U/ml protein kinase
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0.067
acetyl-CoA
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0.274
acetyl-CoA
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Km is induced to 0.118 mM in presence of Ca2+
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0.048
1-methoxyphaseolidin
Rattus norvegicus
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IC50: 0.048 mM
0.057
1-methoxyphaseolin
Rattus norvegicus
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IC50: 0.057 mM
0.02
2-methoxy-5-methyl-3-tetradecanoyloxy-1,4-benzoquinone
Rattus norvegicus
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pH 6.9, 37°C
0.003
3-decanoyloxy-2-methoxy-5-methyl-1,4-benzoquinone
Rattus norvegicus
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pH 6.9, 37°C
0.043
4-(1-Naphthylvinyl)pyridine
Rattus norvegicus
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IC50: 0.043 mM
0.019
6,8-diprenylgenistein
Rattus norvegicus
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IC50: 0.019 mM
0.148
baicalein
Rattus norvegicus
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IC50: 0.148 mM
0.2
chiyusaponin
Rattus norvegicus
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IC50: 0.2 mM
0.15
honokiol
Rattus norvegicus
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IC50: 0.15 mM
0.0077
licoricidin
Rattus norvegicus
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IC50: 0.0077 mM
0.045
luteolin
Rattus norvegicus
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IC50: 0.045 mM
0.15
magnolol
Rattus norvegicus
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IC50: 0.15 mM
0.29
nordihydroguaiaretic acid
Rattus norvegicus
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IC50: 0.29 mM
0.08
quercetin
Rattus norvegicus
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IC50: 0.08 mM
0.183
tetradecanoic acid
Rattus norvegicus
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pH 6.9, 37°C
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0.0004
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liver specific activity is reduced in presence of dexamethasone and medroxyprogesterone
0.001
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spleen specific activity is reduced in presence of dexamethasone
0.0021
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A23187 stimulated cell
additional information
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0.0002
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liver
0.004
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lung
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486103 , 487376 , 487377 , 487379 , 487380 , 487382 , 487385 , 487388 , 487389 , 487392 , 735644 -
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brenda
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brenda
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brenda
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brenda
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brenda
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mastocytoma cell, mucosal-type
brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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PCAT1_RAT
534
1
59762
Swiss-Prot
Mitochondrion (Reliability: 2 )
PCAT2_RAT
544
1
59829
Swiss-Prot
other Location (Reliability: 3 )
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29000
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x * 29000, SDS-PAGE and affinity labelling experiments
800000
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MW after gel filtration, aggregate of several proteins or protein aggregates coated with lipids
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?
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x * 29000, SDS-PAGE and affinity labelling experiments
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stable to lyophilization
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solubilization in sodium deoxycholate, precipitation by ammonium sulfate, ultragel AcA-22 chromatography, DEAE-sepharose CL-6B chromatography, covalent chromatography with thiopropyl-sepharose 6B
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Lee, T.C.; Malone, B.; Snyder, F.
A new de novo pathway for the formation of 1-alkyl-2-acetyl-sn-glycerols, precursors of platelet activating factor. Biochemical characterization of 1-alkyl-2-lyso-sn-glycero-3-P:acetyl-CoA acetyltransferase in rat spleen
J. Biol. Chem.
261
5373-5377
1986
Rattus norvegicus
brenda
Gomez-Cambronero, J.; Velasco, S.; Sanchez-Crespo, M.; Vivanco, F.; Mato, J.M.
Partial purification and characterization of 1-O-alkyl-2-lyso-sn-glycero-3-phosphocholine: acetyl-CoA acetyltransferase from rat spleen
Biochem. J.
237
439-445
1986
Canis lupus familiaris, Rattus norvegicus
brenda
Lee, T.C.
Biosynthesis of platelet activating factor. Substrate specificity of 1-alkyl-2-lyso-sn-glycero-3-phosphocholine:acetyl-CoA acetyltransferase in rat spleen microsomes
J. Biol. Chem.
260
10952-10955
1985
Rattus norvegicus
brenda
Wykle, R.L.; Malone, B.; Snyder, F.
Enzymatic synthesis of 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine, a hypotensive and platelet-aggregating lipid
J. Biol. Chem.
255
10256-10260
1980
Rattus norvegicus
brenda
Gomez-Cambronero, J.; Velasco, S.; Mato, J.M.; Sanchez-Crespo, M.
Modulation of lyso-platelet activating factor: acetyl-CoA acetyltransferase from rat splenic microsomes. The role of cyclic AMP-dependent protein kinase
Biochim. Biophys. Acta
845
516-519
1985
Rattus norvegicus
brenda
Gomez-Cambronero, J.; Nieto, M.L.; Mato, J.M.; Sanchez-Crespo, M.
Modulation of lyso-platelet-activating factor: acetyl-CoA acetyltransferase from rat splenic microsomes. The role of calcium ions
Biochim. Biophys. Acta
845
511-515
1985
Rattus norvegicus
brenda
Yamazaki, R.; Sugatani, J.; Fujii, I.; Kuroyanagi, M.; Umehara, K.; Ueno, A.; Suzuki, Y.; Miwa, M.
Development of a novel method for determination of acetyl-CoA:1-alkyl-sn-glycero-3-phosphocholine acetyltransferase activity and its application to screening for acetyltransferase inhibitors. Inhibition by magnolol and honokiol from Magnoliae cortex
Biochem. Pharmacol.
47
995-1006
1994
Homo sapiens, Rattus norvegicus
brenda
Yanoshita, R.; Chang, H.W.; Son, K.H.; Kudo, I.; Samejina, Y.
Inhibition of lysoPAF acetyltransferase activity by flavonoids
Inflamm. Res.
45
546-549
1996
Rattus norvegicus
brenda
Nagumo, S.; Fukuju, A.; Takayama, M.; Nagai, M.; Yanoshita, R.; Samejima, Y.
Inhibition of lysoPAF acetyltransferase activity by components of licorice root
Biol. Pharm. Bull.
22
1144-1146
1999
Rattus norvegicus
brenda
Ihara, Y.; Frenkel, R.A.; Johnston, J.M.
Hormonal regulation of platelet-activating factor-acetyltransferase activity in rat tissues
Arch. Biochem. Biophys.
304
503-507
1993
Rattus norvegicus
brenda
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
Mus musculus, Mus musculus (Q8BYI6), Rattus norvegicus
brenda