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Information on EC 2.3.1.43 - phosphatidylcholine-sterol O-acyltransferase and Organism(s) Homo sapiens and UniProt Accession P04180

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EC Tree
IUBMB Comments
Palmitoyl, oleoyl and linoleoyl residues can be transferred; a number of sterols, including cholesterol, can act as acceptors. The bacterial enzyme also catalyses the reactions of EC 3.1.1.4 phospholipase A2 and EC 3.1.1.5 lysophospholipase.
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Homo sapiens
UNIPROT: P04180
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The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
lecithin:cholesterol acyltransferase, lecithin-cholesterol acyltransferase, lecithin cholesterol acyltransferase, lecithin cholesterol acyl transferase, lecithin-cholesterol acyl transferase, plasma lecithin-cholesterol acyltransferase, lecithin/cholesterol acyltransferase, lecithin:cholesterol acyl-transferase, tglcat, phospholipid-cholesterol acyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
lecithin cholesterol acyltransferase
-
lecithin-cholesterol acyl transferase
-
lecithin-cholesterol acyltransferase
-
lecithin:cholesterol acyl-transferase
-
lecithin:cholesterol acyltransferase
-
acyltransferase, lecithin-cholesterol
-
-
-
-
lecithin cholesterol acyltransferase
-
-
lecithin-cholesterol acyltransferase
lecithin/cholesterol acyltransferase
-
-
lecithin: cholesterol acyltransferase
-
-
lecithin:cholesterol acyltransferase
lysolecithin acyltransferase
-
-
-
-
phospholipid-cholesterol acyltransferase
-
-
-
-
plasma lecithin-cholesterol acyltransferase
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
phosphatidylcholine + a sterol = 1-acylglycerophosphocholine + a sterol ester
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
-
-
-
-
transesterification
-
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
phosphatidylcholine:sterol O-acyltransferase
Palmitoyl, oleoyl and linoleoyl residues can be transferred; a number of sterols, including cholesterol, can act as acceptors. The bacterial enzyme also catalyses the reactions of EC 3.1.1.4 phospholipase A2 and EC 3.1.1.5 lysophospholipase.
CAS REGISTRY NUMBER
COMMENTARY hide
9031-14-5
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,2-bis[4-(1-pyreno)butanoyl]-sn-glycero-3-phosphocholine + cholesterol
?
show the reaction diagram
fluorescent substrate assay
-
-
?
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
show the reaction diagram
i.e. 16:0-6:0 NBD-PC + (24S)-hydroxycholesterol
-
-
?
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine + dehydroergosterol
1-palmitoyl-glycerophosphocholine + dehydroergosterol 3-O-oleoyl ester
show the reaction diagram
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
-
-
?
L-alpha-phosphatidylcholine type XVI-E + cholesterol
1-acylglycerophosphocholine + cholesteryl ester
show the reaction diagram
-
-
-
?
phosphatidylcholine + 24-hydroxycholesterol
1-acylglycerophosphocholine + a 24-hydroxycholesterol 3-O-acyl ester
show the reaction diagram
-
-
-
?
phosphatidylcholine + a sterol
1-acylglycerophosphocholine + a sterol ester
show the reaction diagram
phosphatidylcholine + cerebrosterol
1-acylglycerophosphocholine + cerebrosteryl ester
show the reaction diagram
phosphatidylcholine + cholesterol
1-acylglycerophosphocholine + cholesterol ester
show the reaction diagram
phosphatidylcholine + cholesterol
1-acylglycerophosphocholine + cholesteryl ester
show the reaction diagram
1,2-bis-(1-pyrenebutanoyl)-sn-glycero-3-phosphocholine + cholesterol
cholesteryl-1-pyrenebutyrate + lysophosphatidylcholine
show the reaction diagram
1-acylglyceryl phosphorylcholine + lecithin
lecithin + 1-acylglyceryl phosphorylcholine
show the reaction diagram
-
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
show the reaction diagram
-
-
-
?
1-O-alkyl-2-acetyl-sn-glycerol-3-phosphocholine + H2O
1-O-alkyl-2-lyso-sn-glycerol-3-phosphocholine + acetate
show the reaction diagram
1-palmitoyl-2-20:4-sn-glycero-3-phosphocholine + cholesterol
?
show the reaction diagram
-
-
-
-
?
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine + cholesterol
?
show the reaction diagram
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoserine + cholesterol
?
show the reaction diagram
-
-
-
-
?
2-sn-phosphorylcholinediacylglycerol + cholesterol
?
show the reaction diagram
-
lower activity than the natural substrate
-
?
cholesterol + 1-O-hexadecyl-2-oleylphosphatidylcholine
cholesteryl oleate + 1-O-hexadecylglycerophosphocholine
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
cholesterol + 1-palmitoyl-2-arachidonoylphosphatidylcholine
cholesteryl arachidonate + 1-palmitoylglycerophosphocholine
show the reaction diagram
-
-
-
?
cholesterol + 1-palmitoyl-2-docosahexaenoylphosphatidylcholine
cholesteryl docosahexaenoate + 1-palmitoylglycerophosphocholine
show the reaction diagram
-
-
-
?
cholesterol + 1-palmitoyl-2-linoleoylphosphatidylcholine
cholesteryl linoleate + 1-palmitoylglycerophosphocholine
show the reaction diagram
-
-
-
?
cholesterol + 1-palmitoyl-2-oleoylphosphatidylcholine
cholesteryl oleate + 1-palmitoylglycerophosphocholine
show the reaction diagram
cholesterol + 1-palmitoyl-2-phytanoylphosphatidylcholine
cholesteryl phytanoate + 1-palmitoylglycerophosphocholine
show the reaction diagram
-
-
-
?
cholesterol + 1-phytanoyl-2-palmitoylphosphatidylcholine
cholesteryl palmitate + 1-phytanylglyerophosphocholine
show the reaction diagram
-
-
-
?
cholesterol + egg lecithin
cholesteryl ester + ?
show the reaction diagram
-
-
-
-
?
dioleoyl-phosphatidyl choline + cholesterol
1-oleoyl-phosphatidyl choline + cholesteryl oleate
show the reaction diagram
-
-
-
-
?
HDL + cholesterol
?
show the reaction diagram
-
-
-
-
?
p-nitrophenol butyrate + H2O
p-nitrophenol + butyric acid
show the reaction diagram
-
esterase activity
-
?
phosphatidylcholine + a sterol
1-acylglycerophosphocholine + a sterol ester
show the reaction diagram
-
-
-
-
?
phosphatidylcholine + cholesterol
1-acylglycerophosphocholine + cholesteryl ester
show the reaction diagram
phosphatidylcholine + cholesterol
3-acylglycerophosphocholine + ?
show the reaction diagram
-
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
show the reaction diagram
phosphatidylcholine + cholesterol
lysolecithin + cholesteryl ester
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
purified recombinant enzyme
-
-
?
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
show the reaction diagram
phosphatidylethanolamine + cholesterol
cholesteryl ester + lysophosphatidylethanolamine
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
phosphatidylcholine + a sterol
1-acylglycerophosphocholine + a sterol ester
show the reaction diagram
phosphatidylcholine + cerebrosterol
1-acylglycerophosphocholine + cerebrosteryl ester
show the reaction diagram
i.e. (24S)-hydroxycholesterol
-
-
?
phosphatidylcholine + cholesterol
1-acylglycerophosphocholine + cholesterol ester
show the reaction diagram
-
-
-
?
phosphatidylcholine + cholesterol
1-acylglycerophosphocholine + cholesteryl ester
show the reaction diagram
-
-
-
?
phosphatidylcholine + a sterol
1-acylglycerophosphocholine + a sterol ester
show the reaction diagram
-
-
-
-
?
phosphatidylcholine + cholesterol
1-acylglycerophosphocholine + cholesteryl ester
show the reaction diagram
phosphatidylcholine + cholesterol
3-acylglycerophosphocholine + ?
show the reaction diagram
-
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
show the reaction diagram
phosphatidylcholine + sterol
1-acylglycerophosphocholine + sterol ester
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
apolipoprotein A1
-
-
-
additional information
-
hydrolysis of platelet-activating factor by LCAT does not require apolipoprotein as cofactor
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
stimulates phospholipase reaction and cholesterol esterification, EDTA suppresses stimulation
Cu2+
-
stimulates phospholipase reaction and cholesterol esterification, EDTA suppresses stimulation
Ni2+
-
stimulates phospholipase reaction and cholesterol esterification, EDTA suppresses stimulation
Zn2+
-
stimulates phospholipase reaction and cholesterol esterification, EDTA suppresses stimulation
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
antibody 25B7
-
-
1,2-diphytanoylphosphatidylcholine
-
competitive inhibitor
1-O-hexadecyl-2-O-oleoylphosphatidylcholine
-
competitive inhibitor
2-mercaptoethanol
-
at high concentration
4-(2-aminoethyl)benzenesulfonylfluoride
-
complete inhibition at 10 mM of the activity in plasma
5,5'-dithiobis(2-nitrobenzoic acid)
-
-
alpha2-Macroglobulin
-
association of this protein with LCAT inhibits the activity of LCAT, and may have a role in its catabolism
-
apolipoprotein A-II
-
-
-
carnitine
-
-
castanospermine
-
reduces the maximum reaction velocity but not the Km
ceramide phosphate
-
stronger physiologic inhibitory effect compared to sphingomyelin
chlorpromazine
-
-
cholesteryl ester transfer protein
-
56% inhibition of the activity in plasma
-
cysteine
-
-
deoxynojirimycin
-
reduces the maximum reaction velocity but not the Km
diisopropyl fluorophosphate
dithiothreitol
-
at high concentration
DTNB
-
83% inhibition at 1.4 mM of the activity in plasma
glycated discoidal (A-I)rHDL
-
after modification of lipid-free apoA-I arginine, lysine and tryptophan residues by glucose
-
Haptoglobin
-
binds apolipoprotein A-I and E, via its Hpt beta-subunit, and impairs its stimulation of LCAT, mechanism, overview. The affinity of Hpt for ApoE is higher than that for ApoA-I. Hpt also impairs human hepatoblastoma-derived cell uptake of cholesterol from proteoliposomes containing ApoE or ApoA-I
-
lysolecithin
-
inhibition of LCAT activity
lysophosphatidylcholine
-
both enantiomers, inhibition reversed by albumin
methyldeoxynojirimycin
-
reduces the maximum reaction velocity but not the Km
p-hydroxymercuribenzoate
-
-
Phenylarsenoxide derivatives
-
-
phenylmethylsulfonyl fluoride
-
-
reduced glutathione
-
-
Serum albumin
-
inhibits LAT activity
-
Sn-2-Difluoroketone phosphatidylcholine analogues
-
IC50 values between 0.5 and 0.028 mM
-
sphingomyelin
Triton X-100
-
inhibition reversed by albumin
tunicamycin
-
reduces the maximum reaction velocity but not the Km
unesterified cholesterol-(apo lipoprotein A-I-)HDL
-
the unesterified cholesterol is deuterium-labeled
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
antibody 27C3
antibody 27C3 binds to and substantially enhances the activity of the enzyme. 24 h after dosing 27C3, a 2.3fold increase of the serum enzyme enzyme activity is observed, followed by a steady elevation of enzyme activity that is sustained for about 20 days before gradually returning to baseline levels
-
apolipoprotein A-I
-
apolipoprotein E
-
LCAT activating peptide LAP642
an amphiphilic peptide in place of apolipoprotein A-I is used as the lipid emulsifier and enzyme LCAT activator. The peptide forms stable complexes with phosphatidylcholine and sterol that react suitably well with enzyme LCAT, Km is 0.006 mM
-
3-{[5-(ethylsulfanyl)-1,3,4-thiadiazol-2-yl]sulfanyl}pyrazine-2-carbonitrile
-
compound activates plasma LCAT from multiple species in vitro
albumin
-
phospholipase activity is dependent on
-
alpha-linolenic acid
-
a moderate dietary intake of myristic acid (1.8% total energy) and alpha-linolenic acid (0.9% total energy) increases LCAT activity
apolipoprotein A-I
-
apolipoprotein A-IV
-
-
-
Apolipoprotein C-1
-
apolipoprotein E
-
atorvastatin
-
significant increase in serum LCAT activity in patients with hyperlipoproteinemia during atorvastatin therapy for 3 months, overview
ceramide
-
30% activation, stimulation of synthesis of 20:4 cholesteryl ester and 18:2 cholesteryl ester, but not of 16:0 cholesteryl ester, a phosphocholine ether matrix abolishes the activation effect
low-density lipoprotein
-
required for acylation of lysolecithin
-
myristic acid
-
a moderate dietary intake of myristic acid (1.8% total energy) and alpha-linolenic acid (0.9% total energy) increases LCAT activity
Reducing agents
-
necessary for maximal activity
-
Serum albumin
-
activates LCAT activity
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00056
1,2-bis[4-(1-pyreno)butanoyl]-sn-glycero-3-phosphocholine
fluorescent assay, pH 7.4, 25°C, recombinant enzyme
0.027
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine
recombinant enzyme, pH 7.4, 37°C
0.003
dehydroergosterol
recombinant enzyme, pH 7.4, 37°C
0.0006
phosphatidylcholine
radioassay, pH 7.4, 37°C, recombinant enzyme
0.14 - 20.5
1,2-bis-(1-pyrenebutanoyl)-sn-glycero-3-phosphocholine
0.0006 - 0.001
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine
0.000091
apolipoprotein-A-I
-
-
-
0.57 - 21.4
cholesterol
additional information
additional information
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
inhibition kinetics
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.5 - 0.028
Sn-2-Difluoroketone phosphatidylcholine analogues
Homo sapiens
-
IC50 values between 0.5 and 0.028 mM
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.217
purified recombinant enzyme, pH 7.4, 37°C, substrates are 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine and dehydroergosterol
0.867
purified recombinant enzyme, pH 7.4, 37°C, substrates are 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine and cholesterol
0.001
-
recombinant enzyme
0.01
-
in cholesterol-lecithin vesicles activated with apolipoprotein A1, at 37°C and pH 7.1
0.06
-
-
0.08
-
-
0.27
-
in cholesterol-lecithin vesicles activated with apolipoprotein A1
0.34
-
at 37°C in cholesterol-lecithin vesicles
0.402
-
purified recombinant enzyme, substrate cholesterol
0.42
-
purified recombinant enzyme, substrate sitosterol
0.43
-
recombinant C-terminal histidine tagged enzyme, similar to plasma enzyme
0.54
-
at 37°C and pH: 7.4
0.57
-
in cholesterol-lecithin vesicles activated with apolipoprotein A1
2.7
-
in cholesterol-lecithin vesicles
3.47
-
in cholesterol-lecithin vesicles activated with apolipoprotein A1
53
-
in cholesterol-lecithin vesicles activated with apolipoprotein A1
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 8
-
lecithin-cholesterol acyltransferase activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.51 - 5.26
isolectric focusing of 9 isozymes, the intensity of spot e (pI 4.86) is 3fold higher in amyotrophic lateral sclerosis compared to control
3.9 - 4.8
-
plasma isozymes
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
secretion to plasma
Manually annotated by BRENDA team
additional information
-
most LCAT activity is found on high-density lipoprotein, HDL, but approximately 30% is also localized on apolipoprotein B-containing lipoproteins
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
LCAT is a member of the alpha/beta hydrolase family
malfunction
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
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
metabolism
physiological function
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
LCAT_HUMAN
440
2
49578
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
44000
x * 64000, recombinant glycosylated enzyme, SDS-PAGE, x * 44000, recombinant deglycosylated enzyme, SDS-PAGE
49000 - 62000
recombinant enzyme, gel filtration
64000
x * 64000, recombinant glycosylated enzyme, SDS-PAGE, x * 44000, recombinant deglycosylated enzyme, SDS-PAGE
46000
-
x * 46000, SDS-PAGE after cleavage of the N-linked carbohydrates
47000
-
x * 65000-68000, glycosylated protein, SDS-PAGE, x * 47000, deglycosylated enzyme, SDS-PAGE, x * 47089, sequence calculation
47089
-
x * 65000-68000, glycosylated protein, SDS-PAGE, x * 47000, deglycosylated enzyme, SDS-PAGE, x * 47089, sequence calculation
49000
-
x * 49000, denatured and deglycosylated enzyme
59000
-
sedimentation equilibrium ultracentrifugation
60000
-
sedimentation equilibrium ultracentrifugation
63000
-
sedimentation equilibrium
65000
-
x * 65000, SDS-PAGE
66000
-
x * 66000, SDS-PAGE
67000
68000
-
x * 68000, SDS-PAGE
70000
-
gel filtration
73000
-
x * 73000, recombinant enzyme, SDS-PAGE
83000
-
gradient gel electrophoresis
95000
additional information
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
Trp61 functions as a component of the interfacial recognition domain of the enzyme, comparison of conformational changes upon substrate binding of wild-type enzyme and mutant T123I, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
glycoprotein
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with antibody 27C3, hanging drop vapor diffusion method, using 0.1 M HEPES (pH 7.0) and 5% (w/v) PEG 20000
molecular dynamics simulation. LCAT anchors itself to lipoprotein surfaces by utilizing nonpolar amino acids located in the membrane-binding domain and the active site tunnel opening. The membrane-anchoring hydrophobic amino acids attract cholesterol molecules next to them. The apolipoprotein A-I-derived peptides from the LCAT-activating region bind to LCAT and promote its lipid surface interactions, although some of these peptides do not bind lipids individually. The transfer free-energy of phospholipid from the lipid bilayer into the active site is consistent with the activation energy of LCAT
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
P274S
the homozygous mutation causes familial lecithin-cholesterol acyltransferase deficiency with renal involvement
E149A
-
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
-
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
T123I
-
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
-
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
-
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
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.5 - 7
-
partially purified enzyme is stable down to pH 3.5
486997
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
0.4 mM phosphate buffer, pH 7.4, ionic strength 0.001: stable up to 6 h, 39 mM phosphate buffer, pH 7.4, ionic strength 0.1: 90% loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
apo-A-1, albumin and lecithin-cholesterol vesicles stabilize
-
complete loss of activity upon lyophilization
-
glycerol stabilizes during storage at -20°C
-
inactivation at the air-water interface is prevented by buffered media of low ionic strength
-
lability to freezing and thawing and to high ionic strength
-
lecithin-cholesterol vesicles stabilize against inactivation to a lesser extent than apo-A-1
-
remarkably stable in buffers of very low ionic strength
-
the purified enzyme is instable
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, purified recombinant enzyme, 1-2 mg/ml protein in phosphate buffer with 10% glycerol, the enzyme retains full activity for at least 6 months and is stable to repeated freeze-thaw cycles
-20°C, 90% of activity is retained, 4 weeks
-
4°C, 0.4 mM phosphate buffer, 4 mM 2-mercaptoethanol, under N2, 4 weeks
-
4°C, 100 h
-
4°C, 20% loss of activity, 24 h
-
4°C, 60 days
-
4°C, low ionic strength buffer, under nitrogen, 4 weeks
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
protein A affinity column chromatography, HisTrap column chromatography and Superdex S200 gel filtration
recombinant enzyme from HEK-293Fcells
recombinant enzyme from human lung cell line H1299 culture medium
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3)pLysS by nickel affinity chromatography
recombinant partially deglycosylated His-tagged enzyme from HEK-293 GnTI cells by nickel affinity chromatography to homogeneity
affinity chromatography using a p-aminophenylarsenoxide-linked phase
-
affinity chromatography using an anti-apolipoprotein D immunoglobulin-Sepharose column
-
antibody affinity chromatography
-
further purification of a recombinant enzyme using ACA-44 allows to remove a proteoglycan contaminant
-
HDL-Sepharose, agglutinin-Sepharose chromatography and polyacrylamide electrophoresis
-
native enzyme from plasma
-
native enzyme from plasma to homogeneity
-
precipitation from plasma and purification by phenyl-agarose, DEAE-cellulose and hydroxyapatite columns
-
precipitation from plasma and purification by phenyl-sepharose and concanavalin A-Sepharose columns
-
precipitation from plasma with dextran sulfate-Mg2+ followed by several chromatographic steps, including DEAE-Sepharose, phenyl-Sepharose and affinity chromatography
-
purification of a recombinant C-terminal histidine tagged enzyme using a cobalt affinity resin
-
purification of recombinant enzymes
-
recombinant LCAT from the conditioned medium of engineered human lung cells
-
recombinant wild-type and mutant enzymes from COS-1 cells
-
Sephadex G-100, hydroxyapatite and affinity column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in HEK-293S cells
expression in HEK-293-6E cell, HEK-293S GnTI cell
gene lcat, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)pLysS, recombinant expression of the enzyme in apoI-deficient mice, recombinant expression in CHO cells
gene lcat, stable recombinant expression in HEK-293Fcells
gene lcat, use of baculovirus as a transducing vector to express the C-or N-terminally His-tagged enzyme in insect cell line Sf9, and to transiently express tagged LCAT in human HEK-293 GnTI cells, deficient in N-acetylglucosaminyl transferase I and expression of the recombinant protein as a high-mannose glycoform (of the MAN9GlcNAc2 or MAN5GlcNAc2 types) suitable for deglycosylation by Endo H, which leaves a single N-acetyl glucosamine (GlcNAc) residue at the glycosylation sites, to avoid protein aggregation coccuring with fully deglycosylated protein. Or expression in HEK-293 6E cells. TEV or Factor Xa sites are introduced for tag cleavage. The enzyme is secreted. Method development and evaluation, overview
optimization of expression in human lung cell line H1299, enzyme is secreted to the culture medium
expression in baby hamster kidney cells
-
expression in Chinese hamster ovary cells, recombinant enzyme is structurally similar to plasma LCAT
-
expression in hepatic Mc-7777 cells
-
expression in mice and rabbit
-
expression of a C-terminal histidine tagged enzyme in Chinese hamster ovary cells
-
expression of mutant enzymes in baby hamster kidney cells
-
expression of mutant enzymes in COS-6 cells
-
expression of the naturally occurring mutants T123I and N228K in COS-1 and CHO cells
-
expression of truncated enzymes in COS-1 cells
-
expression of wild-type enzyme and N-terminally truncated enzymes in COS-7 cells, secretion to the cell culture
-
LCAT overexpression in transgenic mouse J774 macrophages
-
overexpression of LCAT in male nonhuman primate squirrel monkeys, Saimiri sciureus, using an adenoviral vector affects the lipoprotein metabolism, leading to an antiatherogenic lipoprotein profile by increasing HDL cholesterol and lowering ApoB, overview. Increased LCAT activity is also associated with a change in the size of HDL
-
stable expression in CHO cells, expression in insect cells via baculovirus infection, glycosylation pattern of the recombinant enzymes differs from the wild-type, overview
-
transient expression of wild-type and mutant enzymes in COS-1 cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
in blood plasma from sickle cell disease patients, the enzyme concentrations are lower than in normal blood
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
a therapeutic that increases enzyme LCAT activity may promote reverse cholesterol transport and prove beneficial for the treatment of dyslipidaemia and atherosclerosis
medicine
synthesis
baculovirus-mediated expression of LCAT in mammalian cells as a high-mannose glycoform suitable for deglycosylation by Endo H and its purification to homogeneity and characterization. Treatment of the protein with Endo H results in a recombinant protein product that retains its native form and is suitable for structural determination by X-ray crystallography
drug development
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Doi, Y.; Nishida, T.
Lecithin-cholesterol acyltransferase from human plasma
Methods Enzymol.
71
753-767
1981
Homo sapiens
Manually annotated by BRENDA team
Verdery III, R.B.; Gatt, S.
Assay for lecithin: cholesterol acyltransferase
Methods Enzymol.
72
375-384
1981
Homo sapiens
Manually annotated by BRENDA team
Ogawa, Y.; Fielding, C.J.
Assay of cholesteryl ester transfer activity and purification of a cholesteryl ester transfer protein
Methods Enzymol.
111
274-285
1985
Homo sapiens
Manually annotated by BRENDA team
Albers, J.J.; Chen, C.H.; Lacko, A.G.
Isolation, characterization, and assay of lecithin-cholesterol acyltransferase
Methods Enzymol.
129
763-783
1986
Homo sapiens
Manually annotated by BRENDA team
Fielding, C.J.
Mechanisms of action of lecithin-cholesterol acyltransferase
Methods Enzymol.
129
783-790
1986
Homo sapiens
Manually annotated by BRENDA team
Parks, J.S.; Thuren, T.Y.; Schmitt, J.D.
Inhibition of lecithin:cholesterol acyltransferase activity by synthetic phosphatidylcholine species containing eicosapentaenoic acid or docosahexaenoic acid in the sn-2 position
J. Lipid Res.
33
879-887
1992
Homo sapiens
Manually annotated by BRENDA team
Chong, K.S.; Mehrnoosh, J.; Hara, S.; Lacko, A.G.
Characterization of lecithin-cholesterol acyltransferase from human plasma. 3. Chemical properties of the enzyme
Can. J. Biochem. Cell Biol.
61
875-881
1983
Homo sapiens
Manually annotated by BRENDA team
Lacko, A.G.; Varma, K.G.; Rutenberg, H.L.; Soloff, L.A.
Studies on enzymatic and molecular properties of lecithin:cholesterol acyltransferase
Scand. J. Clin. Lab. Invest.
33
29-34
1974
Homo sapiens
-
Manually annotated by BRENDA team
Jauhiainen, M.; Yuan, W.; Gelb, M.H.; Dolphin, P.J.
Human plasma lecithin-cholesterol acyltransferase. Inhibition of the phospholipase A2-like activity by sn-2-difluoroketone phosphatidylcholine analogues
J. Biol. Chem.
264
1963-1967
1989
Homo sapiens
Manually annotated by BRENDA team
Collet, X.; Fielding, C.J.
Effects of inhibitors of N-linked oligosaccharide processing on the secretion, stability, and activity of lecithin:cholesterol acyltransferase
Biochemistry
30
3228-3234
1991
Homo sapiens
Manually annotated by BRENDA team
Aron, L.; Jones, S.; Fielding, C.J.
Human plasma lecithin-cholesterol acyltransferase. Characterization of cofactor-dependent phospholipase activity
J. Biol. Chem.
253
7220-7226
1978
Homo sapiens
Manually annotated by BRENDA team
Zhou, G.; Jauhiainen, M.; Stevenson, K.; Dolphin, P.J.
Human plasma lecithin:cholesterol acyltransferase. Preparation and use of immobilized p-aminophenylarsenoxide as a catalytic site-directed covalent ligand in enzyme purification
J. Chromatogr.
568
69-83
1991
Homo sapiens
Manually annotated by BRENDA team
Subbaiah, P.V.
Lysolecithin acyltransferase of human plasma: assay and characterization of enzyme activity
Methods Enzymol.
129
790-797
1986
Homo sapiens
Manually annotated by BRENDA team
Pownall, H.J.; Pao, Q.; Brockman, H.L.; Massey, J.B.
Inhibition of lecithin-cholesterol acyltransferase by diphytanoyl phosphatidylcholine
J. Biol. Chem.
262
9033-9036
1987
Homo sapiens
Manually annotated by BRENDA team
Chen, C.H.; Albers, J.J.
A rapid large-scale procedure for purification of lecithin-cholesterol acyltransferase from human and animal plasma
Biochim. Biophys. Acta
834
188-195
1985
Canis lupus familiaris, Capra hircus, Oryctolagus cuniculus, Homo sapiens, Sus scrofa
Manually annotated by BRENDA team
Mahadevan, V.; Soloff, L.A.
A method for isolating human plasma lecithin:cholesterol acyltransferase without using anti-apolipoprotein D, and its characterization
Biochim. Biophys. Acta
752
89-97
1983
Homo sapiens
Manually annotated by BRENDA team
Varma, K.G.; Soloff, L.A.
A method for the purification of milligram quantities of stable human phosphatidylcholine-cholesterol acyltransferase
Biochem. J.
155
583-588
1976
Homo sapiens
Manually annotated by BRENDA team
Kitabatake, K.; Piran, U.; Kamio, Y.; Doi, Y.; Nishida, T.
Purification of human plasma lecithin:cholesterol acyltransferase and its specificity towards the acyl acceptor
Biochim. Biophys. Acta
573
145-154
1979
Homo sapiens
Manually annotated by BRENDA team
Doi, Y.; Nishida, T.
Microheterogeneity and physical properties of human lecithin-cholesterol acyltransferase
J. Biol. Chem.
258
5840-5846
1983
Homo sapiens
Manually annotated by BRENDA team
Chaves, M.E.C.; Harry, D.S.; Owen, J.; McIntyre, N.
Purification of lecithin-cholesterol acyltransferase from human plasma
Biochem. Soc. Trans.
13
145-146
1985
Homo sapiens
-
Manually annotated by BRENDA team
Chong, K.S.; Hara, S.; Thompson, R.E.; Lacko, A.G.
Characterization of lecithin:cholesterol acyltransferase from human plasma: II. Physical properties of the enzyme
Arch. Biochem. Biophys.
222
553-560
1983
Homo sapiens
Manually annotated by BRENDA team
Chong, K.S.; Davidson, L.; Huttash, R.G.; Lacko, A.G.
Characterization of lecithin: cholesterol acyltransferase from human plasma: purification of the enzyme
Arch. Biochem. Biophys.
211
119-124
1981
Homo sapiens
Manually annotated by BRENDA team
Suzue, G.; Vezina, C.; Marcel, Y.L.
Purification of human plasma lecithin:cholesterol acyltransferase and its activation by metal ions
Can. J. Biochem.
58
539-541
1980
Homo sapiens
Manually annotated by BRENDA team
Smith, N.B.; Kuksis, A.
Stereochemical substrate requirements of lecithin:cholesterol acyltransferase and its inhibition by enantiomeric lysolecithins
Can. J. Biochem.
58
1286-1291
1980
Homo sapiens
Manually annotated by BRENDA team
Furukawa, Y.; Nishida, T.
Stability and properties of lecithin-cholesterol acyltransferase
J. Biol. Chem.
254
7213-7219
1979
Homo sapiens
Manually annotated by BRENDA team
Chung, J.; Abano, D.A.; Fless, G.M.; Scanu, A.M.
Isolation, properties, and mechanism of in vitro action of lecithin: cholesterol acyltransferase from human plasma
J. Biol. Chem.
254
7456-7464
1979
Homo sapiens
Manually annotated by BRENDA team
Albers, J.J.; Cabana, V.G.; De Barden Stahl, Y.
Purification and characterization of human plasma lecithin: cholesterol acyltransferase
Biochemistry
15
1084-1087
1976
Homo sapiens
Manually annotated by BRENDA team
Liu, M.; Subbaiah, P.V.
Hydrolysis and transesterification of platelet-activating factor by lecithin-cholesterol acyltransferase
Proc. Natl. Acad. Sci. USA
91
6035-6039
1994
Homo sapiens
Manually annotated by BRENDA team
Jonas, A.
Lecithin cholesterol acyltransferase
Biochim. Biophys. Acta
1529
245-256
2000
Homo sapiens
Manually annotated by BRENDA team
Liu, M.; Subbaiah, P.V.
Activation of plasma lysolecithin acyltransferase reaction by apolipoproteins A-I, C-I and E
Biochim. Biophys. Acta
1168
144-152
1993
Homo sapiens
Manually annotated by BRENDA team
O, K.; Hill, J.S.; Wang, X.; McLeod, R.; Pritchard, P.H.
Lecithin:cholesterol acyltransferase: Role of N-linked glycosylation in enzyme function
Biochem. J.
294
879-884
1993
Homo sapiens
Manually annotated by BRENDA team
Lee, Y.P.; Adimoolam, S.; Liu, M.; Subbaiah, P.V.; Glenn, K.; Jonas, A.
Analysis of human lecithin-cholesterol acyltransferase activity by carboxyl-terminal truncation
Biochim. Biophys. Acta
1344
250-261
1997
Homo sapiens
Manually annotated by BRENDA team
Ayyobi, A.F.; Lacko, A.G.; Murray, K.; Nair, M.; Li, M.; Molhuizen, H.O.F.; Pritchard, P.H.
Biochemical and compositional analyses of recombinant lecithin:cholesterol acyltransferase (LCAT) obtained from a hepatic source
Biochim. Biophys. Acta
1484
1-13
2000
Homo sapiens
Manually annotated by BRENDA team
Davit-Spraul, A.; Therond, P.; Leroy, A.; Palmade-Rieunier, F.; Rousset, C.; Moatti, N.; Legrand, A.
Inhibition of lecithin cholesterol acyltransferase by phosphatidylcholine hydroperoxides
FEBS Lett.
447
106-110
1999
Homo sapiens
Manually annotated by BRENDA team
Hida, Y.; Furukawa, Y.; Urano, T.; Kim, H.J.; Kimura, S.
Substrate specificity of rat plasma lecithin-cholesterol acyltransferase towards a molecular species of phosphatidylcholine
Biosci. Biotechnol. Biochem.
57
1111-1114
1993
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Calabresi, L.; Franceschini, G.; Burkybile, A.; Jonas, A.
Activation of lecithin cholesterol acyltransferase by a disulfide-linked apolipoprotein A-I dimer
Biochem. Biophys. Res. Commun.
232
345-349
1997
Homo sapiens
Manually annotated by BRENDA team
Demeester, N.; Castro, G.; Desrumaux, C.; De Geitere, C.; Fruchart, J.C.; Santens, P.; Mulleners, E.; Engelborghs, S.; De Deyn, P.P.; Vandekerckhove, J.; Rosseneu, M.; Labeur, C.
Characterization and functional studies of lipoproteins, lipid transfer proteins, and lecithin:cholesterol acyltransferase in CSF of normal individuals and patients with Alzheimer's disease
J. Lipid Res.
41
963-974
2000
Homo sapiens
Manually annotated by BRENDA team
Qu, S.J.; Fan, H.Z.; Blanco-Vaca, F.; Pownall, H.J.
Effects of site-directed mutagenesis on the N-glycosylation sites of human lecithin:cholesterol acyltransferase
Biochemistry
32
8732-8736
1993
Homo sapiens
Manually annotated by BRENDA team
Subbaiah, P.V.; Liu, M.; Paltauf, F.
Role of sn-2 acyl group of phosphatidyl choline in determining the positional specificity of lecithin-cholesterol acyltransferase
Biochemistry
33
13259-13266
1994
Homo sapiens
Manually annotated by BRENDA team
Parks, J.S.; Huggins, K.W.; Gebre, A.K.; Burleson, E.R.
Phosphatidylcholine fluidity and structure affect lecithin:cholesterol acyltransferase activity
J. Lipid Res.
41
546-553
2000
Homo sapiens
Manually annotated by BRENDA team
Lacko, A.G.; Reason, A.J.; Nuckolls, C.; Kudchodkar, B.J.; Nair, M.P.; Sundarrajan, G.; Pritchard, P.H.; Morris, H.R.; Dell, A.
Characterization of recombinant human plasma lecithin: cholesterol acyltransferase (LCAT): N-linked carbohydrate structures and catalytic properties
J. Lipid Res.
39
807-820
1998
Homo sapiens
Manually annotated by BRENDA team
Chisholm, J.W.; Gebre, A.K.; Parks, J.S.
Characterization of C-terminal histidine-tagged human recombinant lecithin:cholesterol acyltransferase
J. Lipid Res.
40
1512-1519
1999
Homo sapiens
Manually annotated by BRENDA team
Jin, L.; Lee, Y.P.; Jonas, A.
Biochemical and biophysical characterization of human recombinant lecithin: cholesterol acyltransferase
J. Lipid Res.
38
1085-1093
1997
Homo sapiens
Manually annotated by BRENDA team
Nair, M.P.; Kudchodkar, B.J.; Pritchard, P.H.; Lacko, A.G.
Purification of recombinant lecithin: cholesterol acyltransferase
Protein Expr. Purif.
10
38-41
1997
Homo sapiens
Manually annotated by BRENDA team
Krimbou, L.; Marcil, M.; Davignon, J.; Genest, J.Jr.
Interaction of lecithin:cholesterol acyltransferase (LCAT).a2-macroglobulin complex with low density lipoprotein receptor-related protein (LRP). Evidence for an a2-macroglobulin/LRP receptor-mediated system participating in LCAT clearance
J. Biol. Chem.
276
33241-33248
2001
Homo sapiens
Manually annotated by BRENDA team
Adimoolam, S.; Jin, L.; Grabbe, E.; Shieh, J.J.; Jonas, A.
Structural and functional properties of two mutants of lecithin-cholesterol acyltransferase (T123I and N228K)
J. Biol. Chem.
273
32561-32567
1998
Homo sapiens
Manually annotated by BRENDA team
Zhao, Y.; Wang, J.; Gebre, A.K.; Chisholm, J.W.; Parks, J.S.
Negative charge at amino acid 149 is the molecular determinant for substrate specificity of lecithin: cholesterol acyltransferase for phosphatidylcholine containing 20-carbon sn-2 fatty acyl chains
Biochemistry
42
13941-13949
2003
Homo sapiens
Manually annotated by BRENDA team
Nakamura, Y.; Kotite, L.; Gan, Y.; Spencer, T.A.; Fielding, C.J.; Fielding, P.E.
Molecular mechanism of reverse cholesterol transport: reaction of pre-beta-migrating high-density lipoprotein with plasma lecithin/cholesterol acyltransferase
Biochemistry
43
14811-14820
2004
Homo sapiens
Manually annotated by BRENDA team
Alexander, E.T.; Bhat, S.; Thomas, M.J.; Weinberg, R.B.; Cook, V.R.; Bharadwaj, M.S.; Sorci-Thomas, M.
Apolipoprotein A-I helix 6 negatively charged residues attenuate lecithin-cholesterol acyltransferase (LCAT) reactivity
Biochemistry
44
5409-5419
2005
Homo sapiens
Manually annotated by BRENDA team
Hoang, A.; Huang, W.; Sasaki, J.; Sviridov, D.
Natural mutations of apolipoprotein A-I impairing activation of lecithin:cholesterol acyltransferase
Biochim. Biophys. Acta
1631
72-76
2003
Homo sapiens
Manually annotated by BRENDA team
Vickaryous, N.K.; Teh, E.M.; Stewart, B.; Dolphin, P.J.; Too, C.K.; McLeod, R.S.
Deletion of N-terminal amino acids from human lecithin:cholesterol acyltransferase differentially affects enzyme activity toward alpha- and beta-substrate lipoproteins
Biochim. Biophys. Acta
1646
164-172
2003
Homo sapiens
Manually annotated by BRENDA team
Lima, V.L.M.; Coelho, L.C.B.B.; Kennedy, J.F.; Owen, J.S.; Dolphin, P.J.
Lecithin-cholesterol acyltransferase (LCAT) as a plasma glycoprotein: an overview
Carbohydr. Polym.
55
179-191
2004
Homo sapiens
-
Manually annotated by BRENDA team
Temel, R.E.; Gebre, A.K.; Parks, J.S.; Rudel, L.L.
Compared with acyl-CoA:cholesterol O-acyltransferase (ACAT) 1 and lecithin:cholesterol acyltransferase, ACAT2 displays the greatest capacity to differentiate cholesterol from sitosterol
J. Biol. Chem.
278
47594-47601
2003
Homo sapiens
Manually annotated by BRENDA team
Lane, S.B.; Tchedre, K.T.; Nair, M.P.; Thigpen, A.E.; Lacko, A.G.
Characterization of lecithin:cholesterol acyltransferase expressed in a human lung cell line
Protein Expr. Purif.
36
157-164
2004
Homo sapiens (P04180), Homo sapiens
Manually annotated by BRENDA team
Idzior-Walus, B.; Sieradzki, J.; Kostner, G.; Ma?ecki, M.T.; Klupa, T.; Weso?owska, T.; Rostworowski, W.; Hartwich, J.; Walu?, M.; Kie?, A.D.; Naruszewicz, M.
Familial lecithin-cholesterol acyltransferase deficiency: biochemical characteristics and molecular analysis of a new LCAT mutation in a Polish family
Atherosclerosis
185
413-420
2006
Homo sapiens
Manually annotated by BRENDA team
Subbaiah, P.V.; Horvath, P.; Achar, S.B.
Regulation of the activity and fatty acid specificity of lecithin-cholesterol acyltransferase by sphingomyelin and its metabolites, ceramide and ceramide phosphate
Biochemistry
45
5029-5038
2006
Homo sapiens
Manually annotated by BRENDA team
Kassai, A.; Illyes, L.; Mirdamadi, H.Z.; Seres, I.; Kalmar, T.; Audikovszky, M.; Paragh, G.
The effect of atorvastatin therapy on lecithin:cholesterol acyltransferase, cholesteryl ester transfer protein and the antioxidant paraoxonase
Clin. Biochem.
40
1-5
2007
Homo sapiens
Manually annotated by BRENDA team
Bender, B.U.; Quaschning, T.; Neumann, H.P.; Schmidt, D.; Kraemer-Guth, A.
A novel frameshift mutation of the lecithin:cholesterol acyltransferase (LCAT) gene associated with renal failure in familial LCAT deficiency
Clin. Chem. Lab. Med.
45
483-486
2007
Homo sapiens
Manually annotated by BRENDA team
Nobecourt, E.; Davies, M.J.; Brown, B.E.; Curtiss, L.K.; Bonnet, D.J.; Charlton, F.; Januszewski, A.S.; Jenkins, A.J.; Barter, P.J.; Rye, K.A.
The impact of glycation on apolipoprotein A-I structure and its ability to activate lecithin:cholesterol acyltransferase
Diabetologia
50
643-653
2007
Homo sapiens
Manually annotated by BRENDA team
Reshetnyak, Y.; Tchedre, K.T.; Nair, M.P.; Pritchard, P.H.; Lacko, A.G.
Structural differences between wild-type and fish eye disease mutant of lecithin:cholesterol acyltransferase
J. Biomol. Struct. Dyn.
24
75-82
2006
Homo sapiens
Manually annotated by BRENDA team
Koukos, G.; Chroni, A.; Duka, A.; Kardassis, D.; Zannis, V.I.
Naturally occurring and bioengineered apoA-I mutations that inhibit the conversion of discoidal to spherical HDL: the abnormal HDL phenotypes can be corrected by treatment with LCAT
Biochem. J.
406
167-174
2007
Homo sapiens
Manually annotated by BRENDA team
Salvatore, A.; Cigliano, L.; Bucci, E.M.; Corpillo, D.; Velasco, S.; Carlucci, A.; Pedone, C.; Abrescia, P.
Haptoglobin binding to apolipoprotein A-I prevents damage from hydroxyl radicals on its stimulatory activity of the enzyme lecithin-cholesterol acyl-transferase
Biochemistry
46
11158-11168
2007
Homo sapiens
Manually annotated by BRENDA team
Borggreve, S.E.; de Vries, R.; Dallinga-Thie, G.M.; Wolffenbuttel, B.H.; Groen, A.K.; van Tol, A.; Dullaart, R.P.
The ability of plasma to stimulate fibroblast cholesterol efflux is associated with the -629C-->A cholesteryl ester transfer protein promoter polymorphism: role of lecithin: cholesterol acyltransferase activity
Biochim. Biophys. Acta
1781
10-15
2008
Homo sapiens
Manually annotated by BRENDA team
Nakhjavani, M.; Esteghamati, A.; Esfahanian, F.; Ghanei, A.; Rashidi, A.; Hashemi, S.
HbA1c negatively correlates with LCAT activity in type 2 diabetes
Diabetes Res. Clin. Pract.
81
38-41
2008
Homo sapiens
Manually annotated by BRENDA team
Nobecourt, E.; Zeng, J.; Davies, M.J.; Brown, B.E.; Yadav, S.; Barter, P.J.; Rye, K.A.
Effects of cross-link breakers, glycation inhibitors and insulin sensitisers on HDL function and the non-enzymatic glycation of apolipoprotein A-I
Diabetologia
51
1008-1017
2008
Homo sapiens
Manually annotated by BRENDA team
Prost, J.; Belleville, J.; Bouchenak, M.
Serum lecithin: cholesterol acyltransferase activity, HDL2 and HDL3 composition in hypertensive mothers and their small for gestational age newborns
Eur. J. Pediatr.
167
525-532
2008
Homo sapiens
Manually annotated by BRENDA team
Dullaart, R.P.; Perton, F.; Sluiter, W.J.; de Vries, R.; van Tol, A.
Plasma lecithin:cholesterol acyltransferase activity is elevated in metabolic syndrome and is an independent marker of increased carotid artery intima media thickness
J. Clin. Endocrinol. Metab.
93
4860-4866
2008
Homo sapiens
Manually annotated by BRENDA team
Cigliano, L.; Maresca, B.; Salvatore, A.; Nino, M.; Monfrecola, G.; Ayala, F.; Carlucci, A.; Pugliese, R.C.; Pedone, C.; Abrescia, P.
Haptoglobin from psoriatic patients exhibits decreased activity in binding haemoglobin and inhibiting lecithin-cholesterol acyltransferase activity
J. Eur. Acad. Dermatol. Venereol.
22
417-425
2008
Homo sapiens
Manually annotated by BRENDA team
Vaysse-Boue, C.; Dabadie, H.; Peuchant, E.; Le Ruyet, P.; Mendy, F.; Gin, H.; Combe, N.
Moderate dietary intake of myristic and alpha-linolenic acids increases lecithin-cholesterol acyltransferase activity in humans
Lipids
42
717-722
2007
Homo sapiens
Manually annotated by BRENDA team
Dullaart, R.P.; Perton, F.; van der Klauw, M.M.; Hillege, H.L.; Sluiter, W.J.; Sluiter, W.J.
High plasma lecithin:cholesterol acyltransferase activity does not predict low incidence of cardiovascular events: Possible attenuation of cardioprotection associated with high HDL cholesterol
Atherosclerosis
208
537-542
2010
Homo sapiens
Manually annotated by BRENDA team
Jones, M.K.; Catte, A.; Li, L.; Segrest, J.P.
Dynamics of activation of lecithin:cholesterol acyltransferase by apolipoprotein A-I
Biochemistry
48
11196-11210
2009
Homo sapiens
Manually annotated by BRENDA team
Dullaart, R.P.; Perton, F.; Kappelle, P.J.; de Vries, R.; Sluiter, W.J.; van Tol, A.
Plasma lecithin: cholesterol acyltransferase activity modifies the inverse relationship of C-reactive protein with HDL cholesterol in nondiabetic men
Biochim. Biophys. Acta
1801
84-88
2010
Homo sapiens
Manually annotated by BRENDA team
Tanigawa, H.; Billheimer, J.T.; Tohyama, J.; Fuki, I.V.; Ng, D.S.; Rothblat, G.H.; Rader, D.J.
Lecithin: cholesterol acyltransferase expression has minimal effects on macrophage reverse cholesterol transport in vivo
Circulation
120
160-169
2009
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Rader, D.
Lecithin: cholesterol acyltransferase and atherosclerosis: another high-density lipoprotein story that doesnt quite follow the script
Circulation
120
549-552
2009
Homo sapiens
Manually annotated by BRENDA team
Rousset, X.; Vaisman, B.; Amar, M.; Sethi, A.; Remaley, A.
Lecithin: cholesterol acyltransferase - from biochemistry to role in cardiovascular disease
Curr. Opin. Endocrinol. Diabetes Obes.
16
163-171
2009
Oryctolagus cuniculus, Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Cigliano, L.; Pugliese, C.R.; Spagnuolo, M.S.; Palumbo, R.; Abrescia, P.
Haptoglobin binds the antiatherogenic protein apolipoprotein E - impairment of apolipoprotein E stimulation of both lecithin:cholesterol acyltransferase activity and cholesterol uptake by hepatocytes
FEBS J.
276
6158-6171
2009
Homo sapiens
Manually annotated by BRENDA team
Pavlovic, N.; Orem, W.; Tatu, C.; Lerch, H.; Bunnell, J.; Feder, G.; Kostic, E.; Ordodi, V.
The role of lecithin cholesterol acyltransferase and organic substances from coal in the etiology of Balkan endemic nephropathy: A new hypothesis
Food Chem. Toxicol.
46
949-954
2008
Homo sapiens
Manually annotated by BRENDA team
Holleboom, A.G.; Kuivenhoven, J.A.; Vergeer, M.; Hovingh, G.K.; van Miert, J.N.; Wareham, N.J.; Kastelein, J.J.; Khaw, K.T.; Boekholdt, S.M.
Plasma levels of lecithin:cholesterol acyltransferase and risk of future coronary artery disease in apparently healthy men and women: a prospective case-control analysis nested in the EPIC-Norfolk population study
J. Lipid Res.
51
416-421
2010
Homo sapiens
Manually annotated by BRENDA team
Sarkar, P.; Bharill, S.; Gryczynski, I.; Gryczynski, Z.; Nair, M.; Lacko, A.
Binding of 8-anilino-1-naphthalenesulfonate to lecithin:cholesterol acyltransferase studied by fluorescence techniques
J. Photochem. Photobiol. B Biol.
92
19-23
2008
Homo sapiens
Manually annotated by BRENDA team
Amar, M.J.; Shamburek, R.D.; Vaisman, B.; Knapper, C.L.; Foger, B.; Hoyt, R.F.; Santamarina-Fojo, S.; Brewer, H.B.; Remaley, A.T.
Adenoviral expression of human lecithin-cholesterol acyltransferase in nonhuman primates leads to an antiatherogenic lipoprotein phenotype by increasing high-density lipoprotein and lowering low-density lipoprotein
Metab. Clin. Exp.
58
568-575
2009
Homo sapiens
Manually annotated by BRENDA team
Pahl, M.V.; Ni, Z.; Sepassi, L.; Moradi, H.; Vaziri, N.D.
Plasma phospholipid transfer protein, cholesteryl ester transfer protein and lecithin:cholesterol acyltransferase in end-stage renal disease (ESRD)
Nephrol. Dial. Transplant.
24
2541-2546
2009
Homo sapiens
Manually annotated by BRENDA team
Chen, Z.; Wang, S.P.; Krsmanovic, M.L.; Castro-Perez, J.; Gagen, K.; Mendoza, V.; Rosa, R.; Shah, V.; He, T.; Stout, S.J.; Geoghagen, N.S.; Lee, S.H.; McLaren, D.G.; Wang, L.; Roddy, T.P.; Plump, A.S.; Hubbard, B.K.; Sinz, C.J.; Johns, D.G.
Small molecule activation of lecithin cholesterol acyltransferase modulates lipoprotein metabolism in mice and hamsters
Metab. Clin. Exp.
61
470-481
2012
Homo sapiens, Macaca mulatta, Mus musculus, Cricetidae
Manually annotated by BRENDA team
Homan, R.; Esmaeil, N.; Mendelsohn, L.; Kato, G.J.
A fluorescence method to detect and quantitate sterol esterification by lecithin:cholesterol acyltransferase
Anal. Biochem.
441
80-86
2013
Homo sapiens (P04180), Homo sapiens
Manually annotated by BRENDA team
Aguilar-Espinosa, S.L.; Mendoza-Espinosa, P.; Delgado-Coello, B.; Mas-Oliva, J.
Lecithin cholesterol acyltransferase (LCAT) activity in the presence of Apo-AI-derived peptides exposed to disorder-order conformational transitions
Biochem. Biophys. Res. Commun.
441
469-475
2013
Homo sapiens (P04180), Homo sapiens
Manually annotated by BRENDA team
Gu, X.; Wu, Z.; Huang, Y.; Wagner, M.A.; Baleanu-Gogonea, C.; Mehl, R.A.; Buffa, J.A.; DiDonato, A.J.; Hazen, L.B.; Fox, P.L.; Gogonea, V.; Parks, J.S.; DiDonato, J.A.; Hazen, S.L.
A systematic investigation of structure/function requirements for the apolipoprotein A-I - lecithin cholesterol acyltransferase interaction loop of HDL
J. Biol. Chem.
291
6386-6395
2016
Homo sapiens (P04180), Homo sapiens
Manually annotated by BRENDA team
La Marca, V.; Spagnuolo, M.S.; Cigliano, L.; Marasco, D.; Abrescia, P.
The enzyme lecithin-cholesterol acyltransferase esterifies cerebrosterol and limits the toxic effect of this oxysterol on SH-SY5Y cells
J. Neurochem.
130
97-108
2014
Homo sapiens (P04180)
Manually annotated by BRENDA team
Glukhova, A.; Hinkovska-Galcheva, V.; Kelly, R.; Abe, A.; Shayman, J.A.; Tesmer, J.J.
Structure and function of lysosomal phospholipase A2 and lecithin:cholesterol acyltransferase
Nat. Commun.
6
6250
2015
Homo sapiens
Manually annotated by BRENDA team
La Marca, V.; Maresca, B.; Spagnuolo, M.S.; Cigliano, L.; Dal Piaz, F.; Di Iorio, G.; Abrescia, P.
Lecithin-cholesterol acyltransferase in brain: does oxidative stress influence the 24-hydroxycholesterol esterification?
Neurosci. Res.
105
19-27
2016
Homo sapiens (P04180), Homo sapiens
Manually annotated by BRENDA team
Romanow, W.G.; Piper, D.E.; Fordstrom, P.; Thibault, S.; Zhou, M.; Walker, N.P.
BacMam production of active recombinant lecithin-cholesterol acyltransferase: expression, purification and characterization
Protein Expr. Purif.
105
1-6
2016
Homo sapiens (P04180)
Manually annotated by BRENDA team
Spahr, C.; Kim, J.J.; Deng, S.; Kodama, P.; Xia, Z.; Tang, J.; Zhang, R.; Siu, S.; Nuanmanee, N.; Estes, B.; Stevens, J.; Zhou, M.; Lu, H.S.
Recombinant human lecithin-cholesterol acyltransferase Fc fusion: analysis of N- and O-linked glycans and identification and elimination of a xylose-based O-linked tetrasaccharide core in the linker region
Protein Sci.
22
1739-1753
2013
Homo sapiens (P04180), Homo sapiens
Manually annotated by BRENDA team
Fountoulakis, N.; Lioudaki, E.; Lygerou, D.; Dermitzaki, E.K.; Papakitsou, I.; Kounali, V.; Holleboom, A.G.; Stratigis, S.; Belogianni, C.; Syngelaki, P.; Stratakis, S.; Evangeliou, A.; Gakiopoulou, H.; Kuivenhoven, J.A.; Wevers, R.; Dafnis, E.; Stylianou, K.
The P274S mutation of lecithin-cholesterol acyltransferase (LCAT) and its clinical manifestations in a large kindred
Am. J. Kidney Dis.
74
510-522
2019
Homo sapiens (P04180), Homo sapiens
Manually annotated by BRENDA team
Ossoli, A.; Simonelli, S.; Varrenti, M.; Morici, N.; Oliva, F.; Stucchi, M.; Gomaraschi, M.; Strazzella, A.; Arnaboldi, L.; Thomas, M.J.; Sorci-Thomas, M.G.; Corsini, A.; Veglia, F.; Franceschini, G.; Karathanasis, S.K.; Calabresi, L.
Recombinant LCAT (lecithin cholesterol acyltransferase) rescues defective HDL (high-density lipoprotein)-mediated endothelial protection in acute coronary syndrome
Arterioscler. Thromb. Vasc. Biol.
39
915-924
2019
Homo sapiens (P04180)
Manually annotated by BRENDA team
Yokoyama, K.; Tani, S.; Matsuo, R.; Matsumoto, N.
Association of lecithin-cholesterol acyltransferase activity and low-density lipoprotein heterogeneity with atherosclerotic cardiovascular disease risk a longitudinal pilot study
BMC Cardiovasc. Disord.
18
224
2018
Homo sapiens (P04180), Homo sapiens
Manually annotated by BRENDA team
Manthei, K.A.; Patra, D.; Wilson, C.J.; Fawaz, M.V.; Piersimoni, L.; Shenkar, J.C.; Yuan, W.; Andrews, P.C.; Engen, J.R.; Schwendeman, A.; Ohi, M.D.; Tesmer, J.J.G.
Structural analysis of lecithin cholesterol acyltransferase bound to high density lipoprotein particles
Commun. Biol.
3
28
2020
Homo sapiens (P04180)
Manually annotated by BRENDA team
Nass, K.J.; van den Berg, E.H.; Gruppen, E.G.; Dullaart, R.P.F.
Plasma lecithin cholesterol acyltransferase and phospholipid transfer protein activity independently associate with nonalcoholic fatty liver disease
Eur. J. Clin. Invest.
48
e12988
2018
Homo sapiens (P04180), Homo sapiens
Manually annotated by BRENDA team
Soupene, E.; Borja, M.S.; Borda, M.; Larkin, S.K.; Kuypers, F.A.
Featured article alterations of lecithin cholesterol acyltransferase activity and apolipoprotein A-I functionality in human sickle blood
Exp. Biol. Med. (Maywood)
241
1933-1942
2016
Homo sapiens (P04180), Homo sapiens
Manually annotated by BRENDA team
Gunawardane, R.; Fordstrom, P.; Piper, D.; Masterman, S.; Siu, S.; Liu, D.; Brown, M.; Lu, M.; Tang, J.; Zhang, R.; Cheng, J.; Gates, A.; Meininger, D.; Chan, J.; Carlson, T.; Walker, N.; Schwarz, M.; Delaney, J.; Zhou, M.
Agonistic human antibodies binding to lecithin-cholesterol acyltransferase modulate high density lipoprotein metabolism
J. Biol. Chem.
291
2799-2811
2016
Macaca fascicularis (A0A2K5WDQ7), Macaca fascicularis, Homo sapiens (P04180), Homo sapiens
Manually annotated by BRENDA team
Casteleijn, M.G.; Parkkila, P.; Viitala, T.; Koivuniemi, A.
Interaction of lecithin cholesterol acyltransferase with lipid surfaces and apolipoprotein A-I-derived peptides
J. Lipid Res.
59
670-683
2018
Homo sapiens (P04180)
Manually annotated by BRENDA team
Dobiasova, M.
Atherogenic impact of lecithin-cholesterol acyltransferase and its relation to cholesterol esterification rate in HDL (FER(HDL)) and AIP [log(TG/HDL-C)] biomarkers the butterfly effect?
Physiol. Res.
66
193-203
2017
Homo sapiens (P04180)
Manually annotated by BRENDA team
Romanow, W.; Piper, D.; Fordstrom, P.; Thibault, S.; Zhou, M.; Walker, N.
BacMam production of active recombinant lecithin-cholesterol acyltransferase Expression, purification and characterization
Protein Expr. Purif.
125
1-6
2016
Homo sapiens (P04180)
Manually annotated by BRENDA team