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1,2-bis-(1-pyrenebutanoyl)-sn-glycero-3-phosphocholine + cholesterol
cholesteryl-1-pyrenebutyrate + lysophosphatidylcholine
1,2-bis[4-(1-pyreno)butanoyl]-sn-glycero-3-phosphocholine + cholesterol
?
fluorescent substrate assay
-
-
?
1-acylglyceryl phosphorylcholine + lecithin
lecithin + 1-acylglyceryl phosphorylcholine
-
transfer of an acyl group from a lecithin molecule to another on the low-density lipoprotein surface, lysolecithin acyltransferase activity
-
r
1-O-alkyl-2-acetyl-sn-glycerol-3-phosphocholine + 1-O-acyl-2-lyso-sn-glycerol-3-phosphocholine
1-O-alkyl-2-lyso-sn-glycerol-3-phosphocholine + 1-O-acyl-2-acetyl-sn-glycerol-3-phosphocholine
-
-
-
?
1-O-alkyl-2-acetyl-sn-glycerol-3-phosphocholine + H2O
1-O-alkyl-2-lyso-sn-glycerol-3-phosphocholine + acetate
1-palmitoyl-2-(6-[(7-nitro-2-1,3-benzoxadiazol-4-yl)amino]hexanoyl)-sn-glycero-3-phosphocholine + cerebrosterol
1-palmitoyl-sn-glycero-3-phosphocholine + cerebrosteryl-(6-[(7-nitro-2-1,3-benzoxadiazol-4-yl)amino]hexanoyl)-ester
i.e. 16:0-6:0 NBD-PC + (24S)-hydroxycholesterol
-
-
?
1-palmitoyl-2-20:4-sn-glycero-3-phosphocholine + cholesterol
?
-
-
-
-
?
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine + cholesterol
1-palmitoyl-sn-glycero-3-phosphocholine + cholesteryl oleate
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine + cholesterol
?
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine + dehydroergosterol
1-palmitoyl-glycerophosphocholine + dehydroergosterol 3-O-oleoyl ester
dehydroergosterol is a naturally occurring fluorescent sterol, that is esterified by enzyme LCAT, although at a slower rate than esterification of cholesterol, assay method development, overview
-
-
?
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoserine + cholesterol
?
-
-
-
-
?
2-sn-phosphorylcholinediacylglycerol + cholesterol
?
-
lower activity than the natural substrate
-
?
cholesterol + 1-O-hexadecyl-2-oleylphosphatidylcholine
cholesteryl oleate + 1-O-hexadecylglycerophosphocholine
-
-
-
?
cholesterol + 1-palmitoyl-2-(5Z,8Z,11Z,14Z,17Z)-eicosapenta-5,8,11,14,17-enoylphosphatidylcholine
(3beta)-cholest-5-en-3-yl (5Z,8Z,11Z,14Z,17Z)-icosa-5,8,11,14,17-pentaenoate + 1-palmitoylglycerophosphocholine
-
-
-
?
cholesterol + 1-palmitoyl-2-arachidonoylphosphatidylcholine
cholesteryl arachidonate + 1-palmitoylglycerophosphocholine
-
-
-
?
cholesterol + 1-palmitoyl-2-docosahexaenoylphosphatidylcholine
cholesteryl docosahexaenoate + 1-palmitoylglycerophosphocholine
-
-
-
?
cholesterol + 1-palmitoyl-2-linoleoylphosphatidylcholine
cholesteryl linoleate + 1-palmitoylglycerophosphocholine
-
-
-
?
cholesterol + 1-palmitoyl-2-oleoylphosphatidylcholine
cholesteryl oleate + 1-palmitoylglycerophosphocholine
cholesterol + 1-palmitoyl-2-phytanoylphosphatidylcholine
cholesteryl phytanoate + 1-palmitoylglycerophosphocholine
-
-
-
?
cholesterol + 1-phytanoyl-2-palmitoylphosphatidylcholine
cholesteryl palmitate + 1-phytanylglyerophosphocholine
-
-
-
?
cholesterol + egg lecithin
cholesteryl ester + ?
-
-
-
-
?
dioleoyl-phosphatidyl choline + cholesterol
1-oleoyl-phosphatidyl choline + cholesteryl oleate
-
-
-
-
?
HDL + cholesterol
?
-
-
-
-
?
L-alpha-phosphatidylcholine type XVI-E + cholesterol
1-acylglycerophosphocholine + cholesteryl ester
p-nitrophenol butyrate + H2O
p-nitrophenol + butyric acid
-
esterase activity
-
?
phosphatidylcholine + 24-hydroxycholesterol
1-acylglycerophosphocholine + a 24-hydroxycholesterol 3-O-acyl ester
-
-
-
?
phosphatidylcholine + a sterol
1-acylglycerophosphocholine + a sterol ester
phosphatidylcholine + cerebrosterol
1-acylglycerophosphocholine + cerebrosteryl ester
phosphatidylcholine + cholesterol
1-acylglycerophosphocholine + cholesterol ester
phosphatidylcholine + cholesterol
1-acylglycerophosphocholine + cholesteryl ester
phosphatidylcholine + cholesterol
3-acylglycerophosphocholine + ?
-
isozyme abnormality cause hepatosplenic schistosomiasis mansoni, important in lipoprotein metabolism and cholesterol transport, cholesterol is trapped in the HDL particles, enzyme transfers a long-chain fatty acyl residue from the sn-2 position of phosphatidylcholine, i.e. lecithin, to the 3-beta-hydroxyl group of cholesterol producing lysophosphatidylcholine or lysolecithin and cholesteryl ester, predominantly on HDL containing the activator apolipoprotein A-I
-
-
?
phosphatidylcholine + cholesterol
cholesteryl ester + lysophosphatidylcholine
phosphatidylcholine + cholesterol
lysolecithin + cholesteryl ester
-
enzyme transfers a long-chain fatty acyl residue from the sn-2 position of phosphatidylcholine, i.e. lecithin, to the 3-beta-hydroxyl group of cholesterol producing lysophosphatidylcholine or lysolecithin and cholesteryl ester, predominantly on HDL containing the activator apolipoprotein A-I
-
-
?
phosphatidylcholine + cholesterol
lysophosphatidylcholine + cholesteryl ester
-
enzyme transfers a long-chain fatty acyl residue from the sn-2 position of phosphatidylcholine, i.e. lecithin, to the 3-beta-hydroxyl group of cholesterol producing lysophosphatidylcholine or lysolecithin and cholesteryl ester, predominantly on HDL containing the activator apolipoprotein A-I
-
-
?
phosphatidylcholine + sitosterol
1-acylglycerophosphocholine + sitosteryl ester
-
purified recombinant enzyme
-
-
?
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
phosphatidylethanolamine + cholesterol
cholesteryl ester + lysophosphatidylethanolamine
additional information
?
-
1,2-bis-(1-pyrenebutanoyl)-sn-glycero-3-phosphocholine + cholesterol
cholesteryl-1-pyrenebutyrate + lysophosphatidylcholine
-
-
-
?
1,2-bis-(1-pyrenebutanoyl)-sn-glycero-3-phosphocholine + cholesterol
cholesteryl-1-pyrenebutyrate + lysophosphatidylcholine
-
activity assay method based on this reaction
-
?
1-O-alkyl-2-acetyl-sn-glycerol-3-phosphocholine + H2O
1-O-alkyl-2-lyso-sn-glycerol-3-phosphocholine + acetate
-
-
-
?
1-O-alkyl-2-acetyl-sn-glycerol-3-phosphocholine + H2O
1-O-alkyl-2-lyso-sn-glycerol-3-phosphocholine + acetate
-
hydrolysis of human platelet-activating factor PAF to lyso-PAF
-
?
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine + cholesterol
1-palmitoyl-sn-glycero-3-phosphocholine + cholesteryl oleate
-
in presence of apoA-I lipoprotein
-
-
?
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine + cholesterol
1-palmitoyl-sn-glycero-3-phosphocholine + cholesteryl oleate
-
in presence of apoA-I lipoprotein
-
-
?
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine + cholesterol
?
-
-
-
-
?
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine + cholesterol
?
-
cholesterol in HDL of 80 and 93 A, the latter gives a 12fold higher activity with recombinant His-tagged enzyme
-
-
?
cholesterol + 1-palmitoyl-2-oleoylphosphatidylcholine
cholesteryl oleate + 1-palmitoylglycerophosphocholine
-
-
-
?
cholesterol + 1-palmitoyl-2-oleoylphosphatidylcholine
cholesteryl oleate + 1-palmitoylglycerophosphocholine
-
-
-
?
cholesterol + 1-palmitoyl-2-oleoylphosphatidylcholine
cholesteryl oleate + 1-palmitoylglycerophosphocholine
-
-
-
?
L-alpha-phosphatidylcholine type XVI-E + cholesterol
1-acylglycerophosphocholine + cholesteryl ester
-
-
-
?
L-alpha-phosphatidylcholine type XVI-E + cholesterol
1-acylglycerophosphocholine + cholesteryl ester
-
-
-
?
phosphatidylcholine + a sterol
1-acylglycerophosphocholine + a sterol ester
-
-
-
-
?
phosphatidylcholine + a sterol
1-acylglycerophosphocholine + a sterol ester
-
-
-
?
phosphatidylcholine + a sterol
1-acylglycerophosphocholine + a sterol ester
-
-
-
-
?
phosphatidylcholine + a sterol
1-acylglycerophosphocholine + a sterol ester
-
-
-
?
phosphatidylcholine + a sterol
1-acylglycerophosphocholine + a sterol ester
-
-
-
-
?
phosphatidylcholine + a sterol
1-acylglycerophosphocholine + a sterol ester
-
-
-
?
phosphatidylcholine + a sterol
1-acylglycerophosphocholine + a sterol ester
enzyme activities with apolipoprotein A-I and Apo AI-derived peptides DRV, KLL, and VLES, overview
-
-
?
phosphatidylcholine + a sterol
1-acylglycerophosphocholine + a sterol ester
-
-
-
?
phosphatidylcholine + a sterol
1-acylglycerophosphocholine + a sterol ester
-
-
-
?
phosphatidylcholine + cerebrosterol
1-acylglycerophosphocholine + cerebrosteryl ester
-
-
-
?
phosphatidylcholine + cerebrosterol
1-acylglycerophosphocholine + cerebrosteryl ester
i.e. (24S)-hydroxycholesterol
-
-
?
phosphatidylcholine + cholesterol
1-acylglycerophosphocholine + cholesterol ester
-
-
-
?
phosphatidylcholine + cholesterol
1-acylglycerophosphocholine + cholesterol ester
-
-
-
-
?
phosphatidylcholine + cholesterol
1-acylglycerophosphocholine + cholesteryl ester
-
proteoliposome substrates
-
-
?
phosphatidylcholine + cholesterol
1-acylglycerophosphocholine + cholesteryl ester
-
-
-
-
?
phosphatidylcholine + cholesterol
1-acylglycerophosphocholine + cholesteryl ester
-
-
-
?
phosphatidylcholine + cholesterol
1-acylglycerophosphocholine + cholesteryl ester
-
-
-
-
?
phosphatidylcholine + cholesterol
1-acylglycerophosphocholine + cholesteryl ester
-
-
-
?
phosphatidylcholine + cholesterol
1-acylglycerophosphocholine + cholesteryl ester
-
esterification of plasma cholesterol in HDL via alpha-enzyme activity, and of plasma cholesterol in LDL via beta-enzyme activity
-
-
?
phosphatidylcholine + cholesterol
1-acylglycerophosphocholine + cholesteryl ester
-
the enzyme is responsible for esterification of cholesterol in high density lipoprotein HDL to prevent diffusion of cholesterol back to the cell
-
-
?
phosphatidylcholine + cholesterol
1-acylglycerophosphocholine + cholesteryl ester
-
purified recombinant enzyme
-
-
?
phosphatidylcholine + cholesterol
1-acylglycerophosphocholine + cholesteryl ester
-
proteoliposome substrates
-
-
?
phosphatidylcholine + cholesterol
1-acylglycerophosphocholine + cholesteryl ester
-
proteoliposome substrates
-
-
?
phosphatidylcholine + cholesterol
1-acylglycerophosphocholine + cholesteryl ester
-
LCAT contributes significantly to the apoB lipoprotein cholesteryl ester pool, enzyme role in lipid and lipoprotein metabolism in plasma, detailed overview
-
-
?
phosphatidylcholine + cholesterol
1-acylglycerophosphocholine + cholesteryl ester
-
activity with apoB lipoprotein, overview
-
-
?
phosphatidylcholine + cholesterol
1-acylglycerophosphocholine + cholesteryl ester
-
proteoliposome substrates
-
-
?
phosphatidylcholine + cholesterol
1-acylglycerophosphocholine + cholesteryl ester
-
LCAT contributes significantly to the apoB lipoprotein cholesteryl ester pool, enzyme role in lipid and lipoprotein metabolism in plasma, detailed overview
-
-
?
phosphatidylcholine + cholesterol
1-acylglycerophosphocholine + cholesteryl ester
-
activity with apoB lipoprotein, overview
-
-
?
phosphatidylcholine + cholesterol
1-acylglycerophosphocholine + cholesteryl ester
-
-
-
?
phosphatidylcholine + cholesterol
cholesteryl ester + lysophosphatidylcholine
-
-
-
-
?
phosphatidylcholine + cholesterol
cholesteryl ester + lysophosphatidylcholine
-
LCAT is a serum enzyme that catalyses esterification of free cholesterol to produce cholesteryl ester. Cholesterol for this reaction comes from peripheral tissues and the donor of the acyl group is lecithin from the high density lipoprotein, HDL, particles
-
-
?
phosphatidylcholine + cholesterol
cholesteryl ester + lysophosphatidylcholine
-
-
-
-
?
phosphatidylcholine + cholesterol
cholesteryl ester + lysophosphatidylcholine
-
LCAT hydrolyzes the sn-2 acyl group of phosphatidylcholine and subsequently transfers and esterifies the fatty acid to free cholesterol with apolipoprotein A-I as cofactor
-
-
?
phosphatidylcholine + cholesterol
cholesteryl ester + lysophosphatidylcholine
-
LCAT is a plasma enzyme produced by the liver, that catalyzes the conversion of cholesterol to cholesteryl esters on lipoproteins by the transacylation of fatty acid from the sn-2 position of phosphatidylcholine to the 3-hydroxyl group on the A-ring of cholesterol
-
-
?
phosphatidylcholine + cholesterol
cholesteryl ester + lysophosphatidylcholine
-
LCAT is critical in the metabolism of HDL
-
-
?
phosphatidylcholine + cholesterol
cholesteryl ester + lysophosphatidylcholine
-
enzyme with bound activator apolipoprotein A-I, structure-function relationship and analysis, molecular dynamics and simulations, overview
-
-
?
phosphatidylcholine + cholesterol
cholesteryl ester + lysophosphatidylcholine
-
in a first step, LCAT hydrolyzes the sn-2 acyl group of phosphatidylcholine and binds it at Ser181. In a second step, the enzyme transfers and esterifies the fatty acid to the 3beta-hydroxyl group on the A-ring of free cholesterol to form cholesteryl ester using apolipoprotein A-I as cofactor
-
-
?
phosphatidylcholine + cholesterol
cholesteryl ester + lysophosphatidylcholine
-
LCAT hydrolyzes the sn-2 acyl group of phosphatidylcholine and subsequently transfers and esterifies the fatty acid to the 3beta-hydroxy group of free cholesterol
-
-
?
phosphatidylcholine + cholesterol
cholesteryl ester + lysophosphatidylcholine
-
LCAT hydrolyzes the sn-2 acyl group of phosphatidylcholine and subsequently transfers and esterifies the fatty acid to the beta3-hydroxyl group of free cholesterol using apolipoprotein A-I as cofactor
-
-
?
phosphatidylcholine + cholesterol
cholesteryl ester + lysophosphatidylcholine
-
-
-
-
?
phosphatidylcholine + cholesterol
cholesteryl ester + lysophosphatidylcholine
-
in a first step, LCAT hydrolyzes the sn-2 acyl group of phosphatidylcholine and binds it at Ser181. In a second step, the enzyme transfers and esterifies the fatty acid to the 3beta-hydroxyl group on the A-ring of free cholesterol to form cholesteryl ester using apolipoprotein A-I as cofactor
-
-
?
phosphatidylcholine + cholesterol
cholesteryl ester + lysophosphatidylcholine
-
LCAT hydrolyzes the sn-2 acyl group of phosphatidylcholine and subsequently transfers and esterifies the fatty acid to the 3beta-hydroxy group of free cholesterol
-
-
?
phosphatidylcholine + cholesterol
cholesteryl ester + lysophosphatidylcholine
-
-
-
-
?
phosphatidylcholine + cholesterol
cholesteryl ester + lysophosphatidylcholine
-
in a first step, LCAT hydrolyzes the sn-2 acyl group of phosphatidylcholine and binds it at Ser181. In a second step, the enzyme transfers and esterifies the fatty acid to the 3beta-hydroxyl group on the A-ring of free cholesterol to form cholesteryl ester using apolipoprotein A-I as cofactor
-
-
?
phosphatidylcholine + cholesterol
cholesteryl ester + lysophosphatidylcholine
-
-
-
?
phosphatidylcholine + cholesterol
cholesteryl ester + lysophosphatidylcholine
-
-
-
?
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
-
-
r
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
-
-
r
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
-
-
r
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
-
-
r
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
-
-
?
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
-
-
?
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
-
-
?
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
-
-
?
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
-
-
?
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
-
-
?
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
-
-
?
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
-
-
?
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
-
-
?
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
-
-
?
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
-
-
?
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
-
-
?
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
-
-
?
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
-
-
?
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
-
-
?
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
-
-
?
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
-
-
r
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
-
-
r
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
-
-
r
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
-
-
r
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
-
-
r
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
-
-
r
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
-
-
r
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
-
-
r
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
-
-
r
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
-
-
r
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
-
-
r
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
-
-
r
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
-
-
r
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
-
-
r
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
-
-
r
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
-
-
r
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
-
-
r
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
-
-
r
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
-
-
r
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
-
-
r
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
wide specificity for acyl acceptor: sterols with a beta-configuration at carbon-3 and trans fused A /B rings
-
r
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
wide specificity for acyl acceptor: sterols with a beta-configuration at carbon-3 and trans fused A /B rings
-
r
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
wide specificity for acyl acceptor: sterols with a beta-configuration at carbon-3 and trans fused A /B rings
-
r
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
cholesterol as substrate
-
r
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
cholesterol as substrate
-
r
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
cholesterol as substrate
-
r
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
cholesterol as substrate
-
r
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
cholesterol as substrate
-
r
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
water as acyl acceptor: phospholipase activity
-
r
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
water as acyl acceptor: phospholipase activity
-
r
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
phosphatidylethanolamine, dimethylphosphatidylethanolamine, lecithins containing different acyl chain lengths and degrees of saturation
-
r
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
phosphatidylethanolamine, dimethylphosphatidylethanolamine, lecithins containing different acyl chain lengths and degrees of saturation
-
r
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
acyl donor: high degree of specificity for phospholipids containing a basic nitrogen atom
-
r
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
predominant but incomplete specificity for reaction at position 2 of mixed lecithins
-
?
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
predominant but incomplete specificity for reaction at position 2 of mixed lecithins
-
r
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
enzyme is believed to act on the surface of high-density lipoproteins, catalyzes the hydrolysis of fatty acids of the sn-2-position of phosphatidylcholine and transfers the fatty acid to free cholesterol to form cholesteryl ester, transesterification is the major source of plasma cholesteryl ester in human, enzyme has the key role in the transport of cholesterol from peripheral tissues to the liver, in the interconversion of HDL subclasses and the maintenance of lipoprotein structure
-
?
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
important in metabolism and structure of plasma lipoproteins
-
?
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
-
-
r
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
-
-
r
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
-
-
?
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
-
-
r
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
-
-
r
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
-
-
r
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
-
-
r
phosphatidylethanolamine + cholesterol
cholesteryl ester + lysophosphatidylethanolamine
-
-
-
-
?
phosphatidylethanolamine + cholesterol
cholesteryl ester + lysophosphatidylethanolamine
-
-
-
-
?
phosphatidylethanolamine + cholesterol
cholesteryl ester + lysophosphatidylethanolamine
-
-
-
-
?
additional information
?
-
-
bacterial enzyme is not specific for phosphatidylcholine, it can use human erythrocyte membrane substrates, 2-positional specificity as acyltransferase
-
-
?
additional information
?
-
-
phospholipase A2 activity
-
-
?
additional information
?
-
-
symmetrical diacyl phosphatidylcholines are not substrates for human or rat enzymes
-
-
?
additional information
?
-
-
long-chain primary alcohols can act as acyl acceptors
-
-
?
additional information
?
-
-
long-chain primary alcohols can act as acyl acceptors
-
-
?
additional information
?
-
-
phospholipase activity
-
-
?
additional information
?
-
-
phospholipase activity
-
-
?
additional information
?
-
-
phospholipase activity
-
-
?
additional information
?
-
-
no significant activity with 1-sn-phosphorylcholinediacylglycerol
-
-
?
additional information
?
-
-
mechanism of LAT reaction is similar to that of LCAT, probably involving an acyl-enzyme intermediate, 2-acyl isomers of lysolecithin and lysophosphatidylethanolamine can act as substrates in the LAT reaction
-
-
?
additional information
?
-
-
enzyme hydrolyses ester linkage at carbon-2 position of phosphatidylcholine
-
-
?
additional information
?
-
-
lecithin-cholesterol single bilayer vesicles as substrate
-
-
?
additional information
?
-
-
lecithin-cholesterol single bilayer vesicles as substrate
-
-
?
additional information
?
-
-
lecithin-cholesterol single bilayer vesicles as substrate
-
-
?
additional information
?
-
enzyme deficiency can cause corneal opacity, proteinuria, anemia, and kidney failure
-
-
?
additional information
?
-
-
enzyme deficiency can cause corneal opacity, proteinuria, anemia, and kidney failure
-
-
?
additional information
?
-
-
enzyme forms higher aggregates with HDL and apolipoprotein A-I in plasma, esterification of cholesterol and binding to cholesteryl ester transfer protein are required for reverse cholesterol transport from peripheral cells to plasma
-
-
?
additional information
?
-
-
substrate binding study of wild-type and mutant enzymes
-
-
?
additional information
?
-
-
the enzyme accepts a variety of acceptor substrates including sterols and several other alcohols, at high lysophosphatidylcholine concentrations the enzyme catalyzes the reverse reaction producing lecithin on LDL, i.e. exhibiting lysolecithin acyltransferase activity, in absence of an appropriate sterol acceptor, the enzyme exhibits phospholipase A2 or esterase activity liberating free fatty acids
-
-
?
additional information
?
-
-
the enzyme activity is largely influenced by HDL particle size and negative net charge of the cofactor apolipoprotein A-I, overview
-
-
?
additional information
?
-
-
the fatty acid substrate specificity is determined by residues E149, Y292, and W294, enzyme also shows phospholipase A2 activity with the substrates
-
-
?
additional information
?
-
-
the substrates are present in a ratio of 100:10:1 for phosphatidylcholine, cholesterol, and apolipoprotein A-I in the assay mixture
-
-
?
additional information
?
-
-
a frameshift mutation of the LCAT gene is associated with renal failure with proteinuria, corneal opacity, and anemia in familial LCAT deficiency
-
-
?
additional information
?
-
-
key enzyme in reverse cholesterol transport
-
-
?
additional information
?
-
-
the activity and fatty acid specificity of LCAT may be altered during the inflammatory response
-
-
?
additional information
?
-
-
the enzyme is involved in development of atherosclerosis
-
-
?
additional information
?
-
-
the enzyme is responsible for the cholesterol transport, controlling the flow of cholesterol from peripheral tissues to the liver
-
-
?
additional information
?
-
-
the rare enzyme genetic disorder, familial LCAT deficiency, leads to altered plasma lipid and lipoprotein levels, corneal opacities and proteinuria with renal failure, phenotype analysis, overview
-
-
?
additional information
?
-
-
comparison of conformational changes upon substrate binding of wild-type enzyme and mutant T123I, a naturally occuring mutation involved in the fish eye disease, overview
-
-
?
additional information
?
-
-
fatty acid specificity of LCAT, overview
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-
?
additional information
?
-
-
about 75% of plasma LCAT is associated with HDL
-
-
?
additional information
?
-
-
HDL2 and HDL3-phospholipids, HDL2-cholesterol concentrations and LCAT activity are reduced in preganancy-induced hypertension and in chronic hypertensive mothers, as well as in their small for gestational age, SGA, newborns, overview
-
-
?
additional information
?
-
-
plasma high-sensitivity C-reactive protein, CRP, is correlated inversely with HDL-C and apo A-I, and positively with LCAT activity, interaction between apo A-I and LCAT activity on CRP, interaction analysis, overview
-
-
?
additional information
?
-
-
cholesteryl ester-rich HDL particles bind LCAT effectively and contain apolipoprotein A-I and ample phosphatidylcholine and unesterified cholesterol substrates but exhibit relatively low reactivity with LCAT since the cholesteryl ester products cannot be removed from the active site
-
-
?
additional information
?
-
-
study of enzyme interactions with macromolecules and conformational changes upon binding by labeling of tryptophan with 8-anilino-1-naphthalenesulfonate, ANS, steady-state and time-resolved fluorescence emission and anisotropies, Foerster resonance energy transfer, FRET, mechanism, method development and evaluation, overview
-
-
?
additional information
?
-
-
the human enzyme prefers phospholipids with 18:1 or 18:2 fatty acids
-
-
?
additional information
?
-
cholesterol and (24S)-hydroxycholesterol compete for enzyme activity
-
-
?
additional information
?
-
structure/function requirements for the apolipoprotein A-I and lecithin cholesterol acyltransferase interaction loop of HDL, binding studies with recombinant wild/type apoA-I and apoA-I mutants P165A, Y166A, Y166E, Y166F, Y166N, S167A, D168A, Y192F, and Y192L. Loss of LCAT activation caused by apoA-I Y166A or Y166F mutations is at least partially due to the weaker binding between LCAT and apoA-I within these rHDL. Both Vmax of Y166F and Y166A are 20% lower than that of wild-type apoA-I, and the apparent Km are about 2-6fold higher than wild-type. rHDL formed with either apoA-I Y192F or Y192L mutants show normal LCAT activity. Incubation of hLCAT with rHDL formed using the apoA-I mutants P165A, Y166A, Y166F, S167A and D168A all show significant decreases in LCAT activity of 40%-60% compared with the wild-type
-
-
?
additional information
?
-
-
structure/function requirements for the apolipoprotein A-I and lecithin cholesterol acyltransferase interaction loop of HDL, binding studies with recombinant wild/type apoA-I and apoA-I mutants P165A, Y166A, Y166E, Y166F, Y166N, S167A, D168A, Y192F, and Y192L. Loss of LCAT activation caused by apoA-I Y166A or Y166F mutations is at least partially due to the weaker binding between LCAT and apoA-I within these rHDL. Both Vmax of Y166F and Y166A are 20% lower than that of wild-type apoA-I, and the apparent Km are about 2-6fold higher than wild-type. rHDL formed with either apoA-I Y192F or Y192L mutants show normal LCAT activity. Incubation of hLCAT with rHDL formed using the apoA-I mutants P165A, Y166A, Y166F, S167A and D168A all show significant decreases in LCAT activity of 40%-60% compared with the wild-type
-
-
?
additional information
?
-
development and evaluation of a simple but sensitive fluorescence assay method to accurately detect the esterification activity of lecithin:cholesterol acyltransferase, with the potential of the activity assay to be used as a screening test and clinical study tool. An amphiphilic peptide in place of apolipoprotein A-I is used as the lipid emulsifier and enzyme LCAT activator
-
-
?
additional information
?
-
-
development and evaluation of a simple but sensitive fluorescence assay method to accurately detect the esterification activity of lecithin:cholesterol acyltransferase, with the potential of the activity assay to be used as a screening test and clinical study tool. An amphiphilic peptide in place of apolipoprotein A-I is used as the lipid emulsifier and enzyme LCAT activator
-
-
?
additional information
?
-
high-density lipoprotein subfraction 3 functions as highly effective substrate
-
-
-
additional information
?
-
-
LCAT adds cholesteryl ester to LDL in mice and is important in remodeling VLDL to LDL, LCAT deficiency significantly decreases the cholesteryl ester percentage and significantly increases the phospholipid percentage of LDL, overview
-
-
?
additional information
?
-
-
the mouse enzyme prefers phospholipids with 20:4 fatty acids
-
-
?
additional information
?
-
-
for the endogenous assay, the plasma sample is equilibrated with human serum albumin-3H cholesterol emulsion
-
-
?
additional information
?
-
-
for the exogenous substrate assay, proteoliposomes containing 14C-labeled cholesterol, egg PC, and apo AI at molar ratios of 15:300:1 are prepared. Plasma sample is incubated with proteoliposome substrate
-
-
?
additional information
?
-
-
increased HDL cholesterol after LCAT lecithin-cholesterol acyltransfer activity inhibits progression of atherosclerosis and induces cholesterol unloading in complex lesions in rabbits, overview
-
-
?
additional information
?
-
-
LCAT catalyzes the transacylation of a fatty acid at the sn-2 position of phosphatidylcholine preferentially to the free 3beta-hydroxyl group of cholesterol in HDL and to a lesser extent in LDL particles
-
-
?
additional information
?
-
-
symmetrical diacyl phosphatidylcholines are not substrates for human or rat enzymes
-
-
?
additional information
?
-
-
rat enzyme has similar substrate specificity for phosphatidylcholines than human enzyme
-
-
?
additional information
?
-
-
lecithin-cholesterol single bilayer vesicles as substrate
-
-
?
additional information
?
-
the enzyme from Toxoplasma gondii also shows phospholipase and hemolytic activity, recombinant TgLCAT has a dual enzymatic activity as a calcium-independent phospholipase A2 and a cholesterol transacyltransferase
-
-
?
additional information
?
-
-
the enzyme from Toxoplasma gondii also shows phospholipase and hemolytic activity, recombinant TgLCAT has a dual enzymatic activity as a calcium-independent phospholipase A2 and a cholesterol transacyltransferase
-
-
?
additional information
?
-
the enzyme from Toxoplasma gondii also shows phospholipase and hemolytic activity, recombinant TgLCAT has a dual enzymatic activity as a calcium-independent phospholipase A2 and a cholesterol transacyltransferase
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
phosphatidylcholine + a sterol
1-acylglycerophosphocholine + a sterol ester
phosphatidylcholine + cerebrosterol
1-acylglycerophosphocholine + cerebrosteryl ester
i.e. (24S)-hydroxycholesterol
-
-
?
phosphatidylcholine + cholesterol
1-acylglycerophosphocholine + cholesterol ester
-
-
-
?
phosphatidylcholine + cholesterol
1-acylglycerophosphocholine + cholesteryl ester
phosphatidylcholine + cholesterol
3-acylglycerophosphocholine + ?
-
isozyme abnormality cause hepatosplenic schistosomiasis mansoni, important in lipoprotein metabolism and cholesterol transport, cholesterol is trapped in the HDL particles, enzyme transfers a long-chain fatty acyl residue from the sn-2 position of phosphatidylcholine, i.e. lecithin, to the 3-beta-hydroxyl group of cholesterol producing lysophosphatidylcholine or lysolecithin and cholesteryl ester, predominantly on HDL containing the activator apolipoprotein A-I
-
-
?
phosphatidylcholine + cholesterol
cholesteryl ester + lysophosphatidylcholine
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
additional information
?
-
phosphatidylcholine + a sterol
1-acylglycerophosphocholine + a sterol ester
-
-
-
-
?
phosphatidylcholine + a sterol
1-acylglycerophosphocholine + a sterol ester
-
-
-
?
phosphatidylcholine + a sterol
1-acylglycerophosphocholine + a sterol ester
-
-
-
-
?
phosphatidylcholine + a sterol
1-acylglycerophosphocholine + a sterol ester
-
-
-
?
phosphatidylcholine + a sterol
1-acylglycerophosphocholine + a sterol ester
-
-
-
-
?
phosphatidylcholine + a sterol
1-acylglycerophosphocholine + a sterol ester
-
-
-
?
phosphatidylcholine + a sterol
1-acylglycerophosphocholine + a sterol ester
-
-
-
?
phosphatidylcholine + a sterol
1-acylglycerophosphocholine + a sterol ester
-
-
-
?
phosphatidylcholine + cholesterol
1-acylglycerophosphocholine + cholesteryl ester
-
-
-
-
?
phosphatidylcholine + cholesterol
1-acylglycerophosphocholine + cholesteryl ester
-
-
-
?
phosphatidylcholine + cholesterol
1-acylglycerophosphocholine + cholesteryl ester
-
esterification of plasma cholesterol in HDL via alpha-enzyme activity, and of plasma cholesterol in LDL via beta-enzyme activity
-
-
?
phosphatidylcholine + cholesterol
1-acylglycerophosphocholine + cholesteryl ester
-
the enzyme is responsible for esterification of cholesterol in high density lipoprotein HDL to prevent diffusion of cholesterol back to the cell
-
-
?
phosphatidylcholine + cholesterol
1-acylglycerophosphocholine + cholesteryl ester
-
LCAT contributes significantly to the apoB lipoprotein cholesteryl ester pool, enzyme role in lipid and lipoprotein metabolism in plasma, detailed overview
-
-
?
phosphatidylcholine + cholesterol
1-acylglycerophosphocholine + cholesteryl ester
-
LCAT contributes significantly to the apoB lipoprotein cholesteryl ester pool, enzyme role in lipid and lipoprotein metabolism in plasma, detailed overview
-
-
?
phosphatidylcholine + cholesterol
cholesteryl ester + lysophosphatidylcholine
-
LCAT is a serum enzyme that catalyses esterification of free cholesterol to produce cholesteryl ester. Cholesterol for this reaction comes from peripheral tissues and the donor of the acyl group is lecithin from the high density lipoprotein, HDL, particles
-
-
?
phosphatidylcholine + cholesterol
cholesteryl ester + lysophosphatidylcholine
-
-
-
-
?
phosphatidylcholine + cholesterol
cholesteryl ester + lysophosphatidylcholine
-
LCAT hydrolyzes the sn-2 acyl group of phosphatidylcholine and subsequently transfers and esterifies the fatty acid to free cholesterol with apolipoprotein A-I as cofactor
-
-
?
phosphatidylcholine + cholesterol
cholesteryl ester + lysophosphatidylcholine
-
LCAT is a plasma enzyme produced by the liver, that catalyzes the conversion of cholesterol to cholesteryl esters on lipoproteins by the transacylation of fatty acid from the sn-2 position of phosphatidylcholine to the 3-hydroxyl group on the A-ring of cholesterol
-
-
?
phosphatidylcholine + cholesterol
cholesteryl ester + lysophosphatidylcholine
-
LCAT is critical in the metabolism of HDL
-
-
?
phosphatidylcholine + cholesterol
cholesteryl ester + lysophosphatidylcholine
-
-
-
-
?
phosphatidylcholine + cholesterol
cholesteryl ester + lysophosphatidylcholine
-
-
-
-
?
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
-
-
r
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
enzyme is believed to act on the surface of high-density lipoproteins, catalyzes the hydrolysis of fatty acids of the sn-2-position of phosphatidylcholine and transfers the fatty acid to free cholesterol to form cholesteryl ester, transesterification is the major source of plasma cholesteryl ester in human, enzyme has the key role in the transport of cholesterol from peripheral tissues to the liver, in the interconversion of HDL subclasses and the maintenance of lipoprotein structure
-
?
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
-
important in metabolism and structure of plasma lipoproteins
-
?
additional information
?
-
enzyme deficiency can cause corneal opacity, proteinuria, anemia, and kidney failure
-
-
?
additional information
?
-
-
enzyme deficiency can cause corneal opacity, proteinuria, anemia, and kidney failure
-
-
?
additional information
?
-
-
enzyme forms higher aggregates with HDL and apolipoprotein A-I in plasma, esterification of cholesterol and binding to cholesteryl ester transfer protein are required for reverse cholesterol transport from peripheral cells to plasma
-
-
?
additional information
?
-
-
a frameshift mutation of the LCAT gene is associated with renal failure with proteinuria, corneal opacity, and anemia in familial LCAT deficiency
-
-
?
additional information
?
-
-
key enzyme in reverse cholesterol transport
-
-
?
additional information
?
-
-
the activity and fatty acid specificity of LCAT may be altered during the inflammatory response
-
-
?
additional information
?
-
-
the enzyme is involved in development of atherosclerosis
-
-
?
additional information
?
-
-
the enzyme is responsible for the cholesterol transport, controlling the flow of cholesterol from peripheral tissues to the liver
-
-
?
additional information
?
-
-
the rare enzyme genetic disorder, familial LCAT deficiency, leads to altered plasma lipid and lipoprotein levels, corneal opacities and proteinuria with renal failure, phenotype analysis, overview
-
-
?
additional information
?
-
-
about 75% of plasma LCAT is associated with HDL
-
-
?
additional information
?
-
-
HDL2 and HDL3-phospholipids, HDL2-cholesterol concentrations and LCAT activity are reduced in preganancy-induced hypertension and in chronic hypertensive mothers, as well as in their small for gestational age, SGA, newborns, overview
-
-
?
additional information
?
-
-
plasma high-sensitivity C-reactive protein, CRP, is correlated inversely with HDL-C and apo A-I, and positively with LCAT activity, interaction between apo A-I and LCAT activity on CRP, interaction analysis, overview
-
-
?
additional information
?
-
cholesterol and (24S)-hydroxycholesterol compete for enzyme activity
-
-
?
additional information
?
-
structure/function requirements for the apolipoprotein A-I and lecithin cholesterol acyltransferase interaction loop of HDL, binding studies with recombinant wild/type apoA-I and apoA-I mutants P165A, Y166A, Y166E, Y166F, Y166N, S167A, D168A, Y192F, and Y192L. Loss of LCAT activation caused by apoA-I Y166A or Y166F mutations is at least partially due to the weaker binding between LCAT and apoA-I within these rHDL. Both Vmax of Y166F and Y166A are 20% lower than that of wild-type apoA-I, and the apparent Km are about 2-6fold higher than wild-type. rHDL formed with either apoA-I Y192F or Y192L mutants show normal LCAT activity. Incubation of hLCAT with rHDL formed using the apoA-I mutants P165A, Y166A, Y166F, S167A and D168A all show significant decreases in LCAT activity of 40%-60% compared with the wild-type
-
-
?
additional information
?
-
-
structure/function requirements for the apolipoprotein A-I and lecithin cholesterol acyltransferase interaction loop of HDL, binding studies with recombinant wild/type apoA-I and apoA-I mutants P165A, Y166A, Y166E, Y166F, Y166N, S167A, D168A, Y192F, and Y192L. Loss of LCAT activation caused by apoA-I Y166A or Y166F mutations is at least partially due to the weaker binding between LCAT and apoA-I within these rHDL. Both Vmax of Y166F and Y166A are 20% lower than that of wild-type apoA-I, and the apparent Km are about 2-6fold higher than wild-type. rHDL formed with either apoA-I Y192F or Y192L mutants show normal LCAT activity. Incubation of hLCAT with rHDL formed using the apoA-I mutants P165A, Y166A, Y166F, S167A and D168A all show significant decreases in LCAT activity of 40%-60% compared with the wild-type
-
-
?
additional information
?
-
-
LCAT adds cholesteryl ester to LDL in mice and is important in remodeling VLDL to LDL, LCAT deficiency significantly decreases the cholesteryl ester percentage and significantly increases the phospholipid percentage of LDL, overview
-
-
?
additional information
?
-
-
increased HDL cholesterol after LCAT lecithin-cholesterol acyltransfer activity inhibits progression of atherosclerosis and induces cholesterol unloading in complex lesions in rabbits, overview
-
-
?
additional information
?
-
the enzyme from Toxoplasma gondii also shows phospholipase and hemolytic activity, recombinant TgLCAT has a dual enzymatic activity as a calcium-independent phospholipase A2 and a cholesterol transacyltransferase
-
-
?
additional information
?
-
-
the enzyme from Toxoplasma gondii also shows phospholipase and hemolytic activity, recombinant TgLCAT has a dual enzymatic activity as a calcium-independent phospholipase A2 and a cholesterol transacyltransferase
-
-
?
additional information
?
-
the enzyme from Toxoplasma gondii also shows phospholipase and hemolytic activity, recombinant TgLCAT has a dual enzymatic activity as a calcium-independent phospholipase A2 and a cholesterol transacyltransferase
-
-
?
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additional information
-
high plasma lecithin:cholesterol acyltransferase activity does not predict low incidence of cardiovascular events, a possible attenuation of cardioprotection is associated with high HDL cholesterol
evolution
LCAT is a member of the alpha/beta hydrolase family
evolution
-
lysosomal phospholipase A2 (LPLA2) and lecithin:cholesterol acyltransferase (LCAT) belong to a structurally uncharacterized family of key lipid-metabolizing enzymes responsible for lung surfactant catabolism and for reverse cholesterol transport, respectively. LCAT has a close structural relationship to LPLA2, construction of an LPLA2-based homology model corresponding to the catalytic, membrane binding and cap domains of LCAT, structure comparisons, overview. Lys202 in the alpha3 helix and Thr329 in the catalytic domain are invariant in LPLA2 and LCAT, but are conserved as hydrophobic residues in bacterial lipases. Although LPLA2 exhibits structural homology with bacterial lipases, their substrates are fundamentally different in that LPLA2 and LCAT hydrolyse glycerophospholipids, which contain polar, charged head groups, instead of triacylglycerol
malfunction
-
a high LCAT level is associated with an increased coronary artery disease risk in women
malfunction
-
inborn enzyme deficiency leads to the fish-eye disease, as well as anemia, proteinuria, renal failure, hepatosplenomegaly, and lymphadenopathy
malfunction
-
LCAT deficiency is involved in the end-stage renal insufficiency with elevated plasma triglyceride concentration, reduced and plasma HDL cholesterol, apolipoprotein A-1 and LCAT concentrations, whereas plasma phospholipid transfer protein and cholesteryl ester transfer protein concentrations and activities are unchanged in the patients
malfunction
-
LCAT inhibition leads to the Balkan endemic nephropathy, BEN, chronic, slowly progressive renal disease, overview. Familial renal disease can develop secondary LCAT deficiency and associated lipid abnormalities
malfunction
-
LCAT is synthesized in the liver and its synthesis and/or excretion is impaired in hepatocellular diseases as indicated by decreased activity of LCAT, e.g. parturient-haemoglobinuria and ketosis, detection of ketonuria, induced phenotypes, overview
malfunction
-
native mutants show the fish-eye disease
malfunction
-
deficiency in LCAT sensitizes mice to diet-induced hepatic deposition of triglycerides and alterations in hepatic histology and architecture. Mechanistic analysis indicate that this is due to enhanced intestinal absorption of dietary triglycerides, accelerated clearance of postprandial triglycerides from the circulation and reduced rate of hepatic triglyceride secretion. Ectopic expression of human LCAT by gene transfer in LCAT-/- mice fed a Western-type diet for 12 weeks result in a significant reduction in their hepatic triglyceride content and a great improvement of hepatic histology and architecture
malfunction
-
serine palmitoyltransferase deficient mice, and sphingomyelin synthase deficient mice, both of which have below normal sphingomyelin (SM)/phosphatidylcholine (PC) ratios, show significantly elevated LCAT activities when assayed with the endogenous substrates. LDL receptor knockout mice, and apo E knockout mice, both of which have high SM/PC ratios, have reduced LCAT activities
malfunction
-
enzyme mutations and loss of enzyme activity are involved in several diseases, e.g. atherosclerosis and acute coronary syndrome
malfunction
reduced enzyme activity occurs in the sickle cell disease. Deleterious mutations in both alleles of the LCAT gene result in fish eye disease when partial LCAT activity remains and familial LCAT deficiency when LCAT activity is essentially absent. Persons with fish eye disease have low levels of HDL cholesterol and develop lipid-rich, corneal opacities. Those with familial LCAT deficiency are hypocholesterolemic with very low HDL cholesterol levels, exhibit corneal opacities and, in addition, develop anemia and kidney disease typified by fatty deposits in the glomeruli. Persons with normal LCAT alleles are also reported to experience reductions in LCAT activity in conjunction with certain diseases including coronary artery disease, diabetes, kidney disease, rheumatoid arthritis, and anemia
malfunction
the level of 24-hydroxycholesterol esters is lower in cerebrospinal fluid of patients with amyotrophic lateral sclerosis compared to healthy subjects. Oxidative stress reduced LCAT activity in vitro
malfunction
Toxoplasma gondii lacking LCAT shows delayed egress whereas parasites overexpressing LCAT exit faster from host cells than parental parasites
malfunction
homozygosity for loss-of-function mutations causes familial lecithin-cholesterol acyltransferase deficiency, characterized by corneal opacities, anemia, and renal involvement
malfunction
the enzyme activity is reduced in sickle cell disease
malfunction
-
Toxoplasma gondii lacking LCAT shows delayed egress whereas parasites overexpressing LCAT exit faster from host cells than parental parasites
-
metabolism
-
LCAT catalyzes esterification of free cholesterol on the surface of HDL and is involved in HDL metabolism regulation
metabolism
-
LCAT is a key enzyme in high-density lipoprotein, HDL, metabolism
metabolism
the enzyme circulates in plasma, predominantly in association with high-density lipoproteins (HDL) where its principal mechanism of action is the transacylation of a fatty acid from phosphatidylcholine within HDL to cholesterol within the same HDL to form cholesteryl ester. The cholesteryl ester product accumulates in the HDL interior until it is cleared by hepatic lipoprotein receptors, either directly through selective cholesteryl ester uptake from HDL particles captured by HDL-specific receptors or by an indirect route comprised of cholesteryl ester transfer to the apolipoprotein B lipoproteins via cholesteryl ester transfer protein followed by clearance of the recipient lipoproteins through the hepatic apolipoprotein B/E-receptors. Intracellular lipases subsequently de-esterify the cholesteryl ester to liberate cholesterol for further processing
physiological function
-
LCAT expression is inversely related to atherosclerosis, the enzyme is not atheroprotective
physiological function
-
LCAT is a key enzyme in the metabolism of high-density lipoprotein, HDL
physiological function
-
LCAT is a key enzyme in the metabolism of high-density lipoprotein, HDL. It is responsible for the synthesis of cholesteryl esters in human plasma. In addition to its role in HDL metabolism, LCAT has been proposed to have a critical and central role in reverse cholesterol transport, RCT, the process by which excess peripheral cholesterol is effluxed to HDL-based acceptors and returned to the liver for biliary excretion
physiological function
-
LCAT is necessary for reverse cholesterol transport from peripheral tissues
physiological function
-
LCAT might have a beneficial role in reducing atherosclerosis
physiological function
-
LCAT might have a beneficial role in reducing atherosclerosis
physiological function
-
LCAT might have a beneficial role in reducing atherosclerosis
physiological function
-
LCAT plays a major role in reverse cholesterol transport, RCT
physiological function
-
LCAT plays a role in HDL maturation
physiological function
a key enzyme in the esterification of cholesterol and its subsequent incorporation into the core of high density lipoprotein (HDL) particles. The enzyme is also also involved in reverse cholesterol transport, the mechanism by which cholesterol is removed from peripheral cells and transported to the liver for excretion
physiological function
plasma enzyme lecithin:cholesterol acyltransferase is essential for the efficient transit of cholesterol through the plasma compartment. The enzyme facilitates the process of reverse-cholesterol transport by potentiating the migration of excess cholesterol from tissues throughout the body towards the liver hepatocytes. The hepatocytes guideexcess cholesterol and cholesterol-derived bile acids to the bile ducts for elimination
physiological function
since unesterified 24OH-C is neurotoxic in cell culture, the LCATactivity might be addressed to reduce the amount of this oxysterolfor neuron survival. Enhanced enzyme LCAT secretion from astrocytes might represent anadaptive response to the increase of non-esterified 24-hydroxycholesterol percentage, aimed to avoid the accumulation of this neurotoxic compound. The low degree of 24-hydroxycholesterol esterification in cerebrospinal fluid or plasma might reflect reduced activity of enzyme LCAT during neurodegeneration
physiological function
the enzyme lecithin-cholesterol acyltransferase esterifies cerebrosterol and limits the toxic effect of this oxysterol on SH-SY5Y cells. The enzyme, in the presence of the apolipoproteins, converts (24S)-hydroxycholesterol into esters restricted to the extracellular environment, thus preventing or limiting oxysterol-induced neurotoxic injuries to neurons in culture
physiological function
the interaction of lecithin-cholesterol acyl transferase with apolipoprotein A-I plays a critical role in high-density lipoprotein HDL maturation. A highly solvent-exposed apoA-I loop domain (L159-L170) in nascent HDL, the socalled solar flare region, and proposed it serves as an lecithin-cholesterol acyl transferase docking site
physiological function
the protozoan parasite Toxoplasma gondii develops within a parasitophorous vacuole in mammalian cells, where it scavenges cholesterol. When cholesterol is present in excess in its environment, the parasite expulses this lipid into the parasitophorous vacuole or esterifies it for storage in lipid bodies. The unique enzyme from Toxoplasma gondii is a homologue of mammalian lecithin:cholesterol acyltransferase (LCAT), a key enzyme that produces cholesteryl esters via transfer of acyl groups from phospholipids to the 3-OH of free cholesterol, leading to the removal of excess cholesterol from tissues
physiological function
enzyme esterifies cholesterol in high density lipoprotein particles. LCAT preferentially binds to the edge of discoidal high density lipoprotein near the boundary between helix 5 and 6 of apolipoprotein ApoA-I creating a path from the lipid bilayer to the active site of LCAT. Results support for the anti-parallel double belt model of high density lipoprotein, with LCAT binding preferentially to the helix 4/6 region
physiological function
increased enzyme activity is associated with increased formation of triglyceride-rich lipoproteins, leading to a reduction in the low-density lipoprotein-particle size in patients at a high risk for atherosclerotic cardiovascular disease
physiological function
LCAT-null parasites have impaired growth in vitro, reduced virulence in animals, and exhibit delays in egress from host cells. Parasites overexpressing LCAT show increased virulence and faster egress
physiological function
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LCAT-null parasites have impaired growth in vitro, reduced virulence in animals, and exhibit delays in egress from host cells. Parasites overexpressing LCAT show increased virulence and faster egress
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physiological function
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the protozoan parasite Toxoplasma gondii develops within a parasitophorous vacuole in mammalian cells, where it scavenges cholesterol. When cholesterol is present in excess in its environment, the parasite expulses this lipid into the parasitophorous vacuole or esterifies it for storage in lipid bodies. The unique enzyme from Toxoplasma gondii is a homologue of mammalian lecithin:cholesterol acyltransferase (LCAT), a key enzyme that produces cholesteryl esters via transfer of acyl groups from phospholipids to the 3-OH of free cholesterol, leading to the removal of excess cholesterol from tissues
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E149A
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site-directed mutagenesis, mutation alters the human enzyme residue to the corresponding residue of the rat sequence, 2.9fold increased cholesteryl ester formation activity, 5.5fold increased phospholipase A2 activity in the mutant compared to the wild-type enzyme
E149A/Y292H/W294F
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site-directed mutagenesis, mutation alters the human enzyme residues to the corresponding residues of the rat sequence, increased cholesteryl ester formation activity and phospholipase A2 activity with 1-palmitoyl-2-20:4-sn-glycero-3-phosphocholine, decreased activities with 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine compared to the wild-type enzyme
P274S
the homozygous mutation causes familial lecithin-cholesterol acyltransferase deficiency with renal involvement
T123I
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naturally occuring mutation involved in the fish eye disease, conformational changes upon substrate binding is altered in mutant T123I compared to the wild-type enzyme, overview
V309M
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naturally occuring mutation in exon 6, the rare enzyme genetic disorder, familial LCAT deficiency, leads to corneal opacities and proteinuria with renal failure, phenotype analysis of a Polish family, the patients show 10% of control enzyme activity and highly reduced enzyme concentrations, low total HDL-cholesterol and cholesteryl ester concentrations, decreased apo AI and apo AII serum levels, low LDL-cholesterol and apoB and Lp levels, and increased oleate/linoleate ratios, in cholestryl esters, phenotype, overview
Y292H/W294F
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site-directed mutagenesis, mutation alters the human enzyme residues to the corresponding residues of the rat sequence, 1.4fold increased cholesteryl ester formation activity, 2.8fold increased phospholipase A2 activity in the mutant compared to the wild-type enzyme
C31Y
site-directed mutagenesis, the mutation renders the enzyme more stable and active than the native form
C31Y
the mutant has an about 10fold higher cholesterol esterification activity compared with wild type
additional information
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deletion of the first residue of the enzyme's N-terminus lead to 95% reduced alpha-enzyme activity and slightly increased beta-enzyme activity, deletion of the first 2 residues lead to abolished alpha-enzyme activity and reduced beta-enzyme activity, respectively, but the mutant enzymes are still able to bind the substrates, mutants with deletion of 3-5 N-terminal residues show no alpha-enzyme activity and residual or no beta-enzyme activity, overview
additional information
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a frameshift mutation, insertion of an adenine identified at codon 178 generating a Tsp 509 I restriction site, s AATT, in exon 5 of the LCAT gene is associated with renal failure with proteinuria, corneal opacity, and anemia in familial LCAT deficiency
additional information
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using adenovirus-mediated gene transfer of the mutants apoA-I(R151C), apoA-I(R160L) and apoA-I(R149A) in apoA-I-/- mice, a common feature of the three mutations are observed: low HDL levels and the presence of discoidal particles in plasma. These defects can be corrected by coinfection of apoA-I-/- mice with adenoviruses expressing the mutant proteins along with human LCAT, indicating that the endogenous LCAT is rate limiting in the conversion of discoidal into spherical HDL
additional information
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deleterious LCAT mutants show low HDL-cholesterol levels
additional information
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enzyme deficiency phenotypes, overview. Generation of transgenic mice, monkeys, or rabbits overexpressing the human LCAT
additional information
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HDL2 and HDL3-phospholipids, HDL2-cholesterol concentrations and LCAT activity are reduced in preganancy-induced hypertension and in chronic hypertensive mothers, as well as in their small for gestational age, SGA, newborns. Maternal hypertension and foetal intrauterine growth retardation are associated with profound abnormalities in HDL metabolism, consistent with an atherogenic risk, phenotype, overview
additional information
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LCAT overexpression in transgenic wild-type and human-apolipoprotein A-I-transgenic mice does not promote macrophage reverse cholesterol transport, even in the setting of hepatic SR-BI overexpression or CETP expression, overview
additional information
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loss-of-function LCAT mutants show highly decreased HDL-cholesteryl ester plasma levels and inability to form mature HDL particles, leading to progressive renal insufficiency, up to end-stage renal disease A, and corneal opacification, as well as to hemolytic anemia, phenotype of heterozygotes and homozygotes
additional information
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reduced LCAT expression can cause reduction of plasma HDL cholesterol concentration, impaired HDL maturation, altered HDL composition and increased plasma concentration of lipid-poor pre-beta HDL particles, overview
additional information
construction of a recombinant human lecithin-cholesterol acyltransferase Fc fusion (huLCAT-Fc), a chimeric protein produced by fusing human Fc to the C-terminus of the human enzyme via a linker sequence. The huLCAT-Fc homodimer contains five N-linked glycosylation sites per monomer. The heterogeneity and site-specific distribution of the various glycans are examined using enzymatic digestion and LC-MS/MS, followed by automatic processing. Almost all of the N-linked glycans in human LCAT are fucosylated and sialylated. The predominant LCAT N-linked glycoforms are biantennary glycans, followed by triantennary sugars, whereas the level of tetraantennary glycans is much lower. Glycans at the Fc N-linked site exclusively contain typical asialobiantennary structures. HuLCAT-Fc is also confirmed to have mucin-type glycans attached at T407 and S409. When LCAT-Fc fusions are constructed using a G-S-G-G-G-G linker, an unexpected 1632 Da xylose-based glycosaminoglycan (GAG) tetrasaccharide core of Xyl-Gal-Gal-GlcA is attached to S418. Several minor intermediate species including Xyl, Xyl-Gal, Xyl-Gal-Gal, and a phosphorylated GAG core are also present. GAG incorporation can be eliminated through engineering by shifting the linker Ser residue downstream in the linker sequence
additional information
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construction of a recombinant human lecithin-cholesterol acyltransferase Fc fusion (huLCAT-Fc), a chimeric protein produced by fusing human Fc to the C-terminus of the human enzyme via a linker sequence. The huLCAT-Fc homodimer contains five N-linked glycosylation sites per monomer. The heterogeneity and site-specific distribution of the various glycans are examined using enzymatic digestion and LC-MS/MS, followed by automatic processing. Almost all of the N-linked glycans in human LCAT are fucosylated and sialylated. The predominant LCAT N-linked glycoforms are biantennary glycans, followed by triantennary sugars, whereas the level of tetraantennary glycans is much lower. Glycans at the Fc N-linked site exclusively contain typical asialobiantennary structures. HuLCAT-Fc is also confirmed to have mucin-type glycans attached at T407 and S409. When LCAT-Fc fusions are constructed using a G-S-G-G-G-G linker, an unexpected 1632 Da xylose-based glycosaminoglycan (GAG) tetrasaccharide core of Xyl-Gal-Gal-GlcA is attached to S418. Several minor intermediate species including Xyl, Xyl-Gal, Xyl-Gal-Gal, and a phosphorylated GAG core are also present. GAG incorporation can be eliminated through engineering by shifting the linker Ser residue downstream in the linker sequence
additional information
generation of human LCAT transgenic mice that are apoA-I deficient by breeding hLCATTg/Tg mice on C57Bl/6J background with apoA-I-/- mice on C57Bl/6J background, both over more than 10 generations
additional information
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generation of human LCAT transgenic mice that are apoA-I deficient by breeding hLCATTg/Tg mice on C57Bl/6J background with apoA-I-/- mice on C57Bl/6J background, both over more than 10 generations
additional information
removal of a proline rich region (residues 402 to 416) on the C-terminus
additional information
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LCAT deficiency significantly decreases the cholesteryl ester percentage and significantly increases the phospholipid percentage of LDL, overview
additional information
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mice deficient in apo A-I and especially in apoE lipoproteins show reduced plasma enzyme activity, overview
additional information
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overexpression of human LCAT in transgenic wild-type and human-apolipoprotein A-I-transgenic mice does not promote macrophage reverse cholesterol transport, even in the setting of hepatic SR-BI overexpression or CETP expression, overview. LCAT heterozygous and homozygous deficient mice mutants, phenotypes, detailed overview
additional information
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overexpression of LCAT does not protect against diet-induced atherosclerosis, but in contrary does increase the atherosclerosis risk. LCAT knockout mice show markedly reduced plasma total cholesterol, cholesteryl esters, HDL-C, apolipoprotein A-I, and an increase in plasma triglycerides, the amount of alpha-HDl is decreased compared to wild-type mice
additional information
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mice deficient in apo A-I and especially in apoE lipoproteins show reduced plasma enzyme activity, overview
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additional information
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hepatocyte-directed adenoviral gene transfer of LCAT or apolipoprotein A-I to LDLr+/- rabbits with 0.15% cholesterol-diet-induced hyperlipidemia increases the HDL cholesterol in these rabbits, intimal lesions in organs of the LDL+/- heterozygous rabbits, overview
additional information
construction of enzyme knockout and overexpressing strains, the loss of TgLCAT expression leads to an egress defect, and its overexpression confers an egress advantage, phenotype, overview
additional information
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construction of enzyme knockout and overexpressing strains, the loss of TgLCAT expression leads to an egress defect, and its overexpression confers an egress advantage, phenotype, overview
additional information
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construction of enzyme knockout and overexpressing strains, the loss of TgLCAT expression leads to an egress defect, and its overexpression confers an egress advantage, phenotype, overview
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