2.3.1.43: phosphatidylcholine-sterol O-acyltransferase
This is an abbreviated version!
For detailed information about phosphatidylcholine-sterol O-acyltransferase, go to the full flat file.
Word Map on EC 2.3.1.43
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2.3.1.43
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lipoprotein
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hdl
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apolipoproteins
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cholesteryl
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high-density
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triglyceride
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esterification
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apoa-i
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atherosclerosis
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lipase
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esterify
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low-density
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coronary
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cardiovascular
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hdl-cholesterol
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unesterified
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opacity
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apoproteins
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hypercholesterolemia
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corneal
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discoidal
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atherogenic
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subfractions
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hdl-associated
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triglyceride-rich
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apoc-iii
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postheparin
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synthesis
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hyperlipoproteinemia
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lysolecithin
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vldl-c
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tg-rich
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dimyristoyl
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antiatherogenic
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b-containing
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normolipidemic
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cholesterol-loaded
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xanthoma
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medicine
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lipoprotein-cholesterol
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chylomicron
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acyl-coa:cholesterol
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lipid-free
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paraoxonase
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apob-containing
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hdl-mediated
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3hcholesterol
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drug development
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lipid-poor
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hypertriglyceridemia
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tangier
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very-low-density
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non-hdl
- 2.3.1.43
- lipoprotein
- hdl
-
apolipoproteins
-
cholesteryl
-
high-density
- triglyceride
- esterification
- apoa-i
- atherosclerosis
- lipase
-
esterify
-
low-density
- coronary
- cardiovascular
-
hdl-cholesterol
-
unesterified
- opacity
- apoproteins
- hypercholesterolemia
- corneal
-
discoidal
-
atherogenic
-
subfractions
-
hdl-associated
-
triglyceride-rich
- apoc-iii
-
postheparin
- synthesis
- hyperlipoproteinemia
- lysolecithin
-
vldl-c
-
tg-rich
-
dimyristoyl
-
antiatherogenic
-
b-containing
-
normolipidemic
-
cholesterol-loaded
-
xanthoma
- medicine
-
lipoprotein-cholesterol
- chylomicron
-
acyl-coa:cholesterol
-
lipid-free
- paraoxonase
-
apob-containing
-
hdl-mediated
-
3hcholesterol
- drug development
-
lipid-poor
- hypertriglyceridemia
- tangier
-
very-low-density
-
non-hdl
Reaction
Synonyms
acyltransferase, lecithin-cholesterol, cholesterol transacyltransferase, LAT, LCAT, lecithin cholesterol acyl transferase, lecithin cholesterol acyltransferase, lecithin-cholesterol acyl transferase, lecithin-cholesterol acyltransferase, lecithin/cholesterol acyltransferase, lecithin: cholesterol acyltransferase, lecithin:cholesterol acyl-transferase, lecithin:cholesterol acyltransferase, lysolecithin acyltransferase, phospholipid-cholesterol acyltransferase, plasma lecithin-cholesterol acyltransferase, TgLCAT, TGME49_272420
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General Information
General Information on EC 2.3.1.43 - phosphatidylcholine-sterol O-acyltransferase
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evolution
malfunction
metabolism
physiological function
additional information
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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
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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
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a high LCAT level is associated with an increased coronary artery disease risk in women
malfunction
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inborn enzyme deficiency leads to the fish-eye disease, as well as anemia, proteinuria, renal failure, hepatosplenomegaly, and lymphadenopathy
malfunction
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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
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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
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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
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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
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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
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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
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Toxoplasma gondii lacking LCAT shows delayed egress whereas parasites overexpressing LCAT exit faster from host cells than parental parasites
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LCAT catalyzes esterification of free cholesterol on the surface of HDL and is involved in HDL metabolism regulation
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
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LCAT expression is inversely related to atherosclerosis, the enzyme is not atheroprotective
physiological function
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LCAT is a key enzyme in the metabolism of high-density lipoprotein, HDL
physiological function
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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
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LCAT is necessary for reverse cholesterol transport from peripheral tissues
physiological function
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LCAT might have a beneficial role in reducing atherosclerosis
physiological function
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LCAT might have a beneficial role in reducing atherosclerosis
physiological function
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LCAT might have a beneficial role in reducing atherosclerosis
physiological function
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LCAT plays a major role in reverse cholesterol transport, RCT
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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