2.3.1.23: 1-acylglycerophosphocholine O-acyltransferase
This is an abbreviated version!
For detailed information about 1-acylglycerophosphocholine O-acyltransferase, go to the full flat file.
Word Map on EC 2.3.1.23
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2.3.1.23
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acyl-coas
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lysophospholipids
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phospholipase
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arachidonic
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polyunsaturated
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lysophosphatidic
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reacylation
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lncrnas
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platelet-activating
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glycerophospholipids
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palmitoyl-coa
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oleoyl-coa
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arachidonoyl-coa
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lysopcs
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cholinephosphotransferase
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kennedy
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lysophospholipase
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deacylation-reacylation
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lysophosphatidylinositol
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mboats
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oleoyl
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lecithin-cholesterol
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transacylation
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arachidonoyl
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linoleoyl-coa
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acyl-coa-dependent
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lysophosphatidylserine
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thimerosal
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disaturated
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glycerolphosphate
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coa-independent
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cholinephosphate
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lysophosphatidylglycerol
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pharmacology
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medicine
- 2.3.1.23
- acyl-coas
- lysophospholipids
- phospholipase
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arachidonic
-
polyunsaturated
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lysophosphatidic
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reacylation
- lncrnas
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platelet-activating
- glycerophospholipids
- palmitoyl-coa
- oleoyl-coa
- arachidonoyl-coa
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lysopcs
-
cholinephosphotransferase
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kennedy
- lysophospholipase
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deacylation-reacylation
- lysophosphatidylinositol
-
mboats
-
oleoyl
-
lecithin-cholesterol
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transacylation
-
arachidonoyl
- linoleoyl-coa
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acyl-coa-dependent
- lysophosphatidylserine
- thimerosal
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disaturated
- glycerolphosphate
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coa-independent
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cholinephosphate
- lysophosphatidylglycerol
- pharmacology
- medicine
Reaction
Synonyms
1-acyl-sn-glycero-3-phosphocholine acyltransferase, 1-acylglycerol-3-phosphate O-acyltransferase 8, 1-acylglycerophosphocholine acyltransferase, 1-AGP acyltransferase 8, 1-AGPAT 8, 1-AGPAT7, acetyl-CoA:1-O-alkyl-sn-glycero-3-phosphocholine acetyltransferase, acyl coenzyme A-monoacylphosphatidylcholine acyltransferase, acyl-CoA:1-acyl-glycero-3-phosphocholine transacylase, acyl-CoA:glycerophosphocholine acyltransferase, acyl-CoA:lysocardiolipin acyltransferase 1, acyl-CoA:lysophosphatidylcholine acyltransferase, acyl-CoA:lysophosphatidylethanolamine acyltransferase 2, acyl-CoA:lysophospholipid acyltransferase, acyltransferase, lysolecithin, AGPAT7, AGPAT8, Alcat1, ALE1, At1g78690, AtLPLAT2, AYTL1, AYTL2, AYTL3, CF3, CG18445, CsLPCAT, GPCAT, hPrdx6, Lclat1, LPAT, LPC acyltransferase, LPCAT, LPCAT1, LPCAT2, LPCAT3, LPCAT4, LPEAT2, LPG acyltransferase, LPGAT, LPGAT1, LPLAT, LPLAT5, lung-type acyl-CoA:lysophosphatidylcholine acyltransferase 1, LYCAT, lyso-PAF acetyltransferase, lyso-PC acyltransferase, lyso-PC acyltransferase 1, lyso-phosphatidylcholine acyltransferase 1, lysolecithin acyltransferase, lysoPC acyltransferase, lysophosphatide acyltransferase, lysophosphatidylcholine acyl transferase, lysophosphatidylcholine acyltransferase, lysophosphatidylcholine acyltransferase 1, lysophosphatidylcholine acyltransferase 3, lysophosphatidylcholine acyltransferase 4, lysophosphatidylethanolamine acyltransferase 2, lysophosphocholine acyltransferase 1, lysophosphocholine acyltransferase 2, lysophosphocholine acyltransferase 3, lysophosphocholine acyltransferase 4, lysophospholipid acyltransferase, lysophospholipid:acyl-CoA acyltransferase, mboa-6, MBOAT protein Nes, MBOAT5, membrane-bound O-acyltransferase 5, mLPEAT2, More, mPrdx6, N-acylphosphatidylethanolamine synthase, NAPE synthase, PCAT1, PCAT2, PGAT, rPrdx6, YALI0E16797g, yeast tafazzin, Ypr140wp
ECTree
2.3.1.23 1-acylglycerophosphocholine O-acyltransferaseAdvanced search results
results (
results (KM Value
KM Value on EC 2.3.1.23 - 1-acylglycerophosphocholine O-acyltransferase
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KM VALUE [mM] 
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
0.2668
NBD-labelled lysophosphatidylcholine
pH 6.0, 30°C, recombinant enzyme
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0.0023
1-palmitoyl-lysophosphatidylcholine
pH 7.4, 30°C, recombinant enzyme
0.005
Arachidonoyl-CoA
Vmax: 12.4 pmol/min/microgram protein for arachidonoyl-CoA
0.00314
docosahexanoyl-CoA
with 1-octadecenyl-sn-glycero-3-phosphoethanolamine, pH and temperature not specified in the publication
0.0132
docosahexanoyl-CoA
with 1-palmitoyl-sn-glycero-3-phosphoethanolamine, pH and temperature not specified in the publication
additional information
additional information
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kinetic data of soluble and liposome-bound enzyme
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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
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additional information
additional information
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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
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