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
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apolipoproteins
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cholesteryl
-
high-density
- triglyceride
- esterification
- apoa-i
- atherosclerosis
- lipase
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esterify
-
low-density
- coronary
- cardiovascular
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hdl-cholesterol
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unesterified
- opacity
- apoproteins
- hypercholesterolemia
- corneal
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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
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lipid-poor
- hypertriglyceridemia
- tangier
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very-low-density
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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
ECTree
2.3.1.43 phosphatidylcholine-sterol O-acyltransferaseAdvanced search results
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results (Activating Compound
Activating Compound on EC 2.3.1.43 - phosphatidylcholine-sterol O-acyltransferase
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ACTIVATING COMPOUND 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
alpha-linolenic acid
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a moderate dietary intake of myristic acid (1.8% total energy) and alpha-linolenic acid (0.9% total energy) increases LCAT activity
atorvastatin
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significant increase in serum LCAT activity in patients with hyperlipoproteinemia during atorvastatin therapy for 3 months, overview
ceramide
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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
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
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myristic acid
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a moderate dietary intake of myristic acid (1.8% total energy) and alpha-linolenic acid (0.9% total energy) increases LCAT activity
3-{[5-(ethylsulfanyl)-1,3,4-thiadiazol-2-yl]sulfanyl}pyrazine-2-carbonitrile
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compound activates plasma LCAT from multiple species in vitro
3-{[5-(ethylsulfanyl)-1,3,4-thiadiazol-2-yl]sulfanyl}pyrazine-2-carbonitrile
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compound activates plasma LCAT from multiple species in vitro
3-{[5-(ethylsulfanyl)-1,3,4-thiadiazol-2-yl]sulfanyl}pyrazine-2-carbonitrile
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compound activates plasma LCAT from multiple species in vitro
3-{[5-(ethylsulfanyl)-1,3,4-thiadiazol-2-yl]sulfanyl}pyrazine-2-carbonitrile
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compound activates plasma LCAT from multiple species in vitro
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
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antibody 27C3
antibody 27C3 binds to and substantially enhances the activity of the enzyme
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apolipoprotein A-I
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the naturally occurring mutant T123I is defective in activation by apo A-I
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apolipoprotein A-I
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required for hydrolysis of ester linkage at carbon-2 position of phosphatidylcholine and for transesterification
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apolipoprotein A-I
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required for transferase and phospholipase activity
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apolipoprotein A-I
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a disulfide-linked apoprotein dimer is less effective as activator than apo A-I
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apolipoprotein A-I
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absolute requirement with phosphatidylcholine-cholesterol vesicles as a substrate
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apolipoprotein A-I
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glycosylated, the alpha-helix formed by residues 143-165 is essential for full activation activity
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apolipoprotein A-I
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principal apolipoprotein of HDL, activates the enzyme, mutations of the activation site residues 110-160 of the apolipoprotein, responsible for activation, lead to loss of the activation activity, e.g. mutations A95D, Y100H, E110K, V156E, and H162Q of the protein
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apolipoprotein A-I
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principal apolipoprotein of HDL, activates the enzyme, the negative net charge of the protein is important for function in interaction with the enzyme, mutation of the negative charges to uncharged, or mutational doubling of the negatively charged residues, overview
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apolipoprotein A-I
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glycation affects the structure of apoA-I and its ability to activate the enzyme
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apolipoprotein A-I
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decreased stimulation of LCAT is observed when liposomes oxidized without haptoglobin are used
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apolipoprotein A-I
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the impact of glycation on apolipoprotein A-I structure and its ability to activate LCAT is investigated: The rate of LCAT-mediated cholesterol esterification in reconstituted HDL containing phosphatidylcholine and apoA-I varied according to the level of apoA-I glycation and progressively decreases as the extent of apoA-I glycation increases
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apolipoprotein A-I
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ApoA-I, required for activity, activation in inhibited by binding of haptoglobin
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apolipoprotein A-I
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kinetic analysis of radioiodinated ApoA-I associated with HDL and radioiodinated ApoB on LDL, mechanism for the effect of LCAT on lipid and lipoprotein changes, overview
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apolipoprotein A-I
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the central helix 4-helix 5-helix 6 domain in apoA-I is the unique structural element that provides full specificity to apoA-I activation of LCAT through substantially more LCAT binding and substrate binding and presentation to LCAT thorough the presentation tunnel, molecular dynamics, role of apoA-I in activation of LCAT involved simulations of discoidal particles, overview
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apolipoprotein A-I
association of Apo AI with HDLs activates LCAT activity, molecular mechanism, conformational changes in several exposed regions of Apo-AI might cause enzyyme LCAT activation. Apo AI-derived peptides display a disordered arrangement, with a strong tendency to adopt beta-sheet and random conformational structures as a function of concentration, but in the presence of lyso-C12-phosphocholine, maximal percentages of alpha-helical structures are observed
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apolipoprotein A-I
in proteoliposomes, that stimulate the enzyme activity
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apolipoprotein A-I
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both human and pig ApoA-1 can activate pig LCAT in cholesterol-lecithin liposomes
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apolipoprotein E
in proteoliposomes, that stimulate the enzyme activity
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additional information
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apo-A-II, apo-C-III and apo-D inhibit activation of enzyme by apo-A-1
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additional information
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apo-A-II, apo-C-III and apo-D inhibit activation of enzyme by apo-A-1
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additional information
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apo-A-II, apo-C-III and apo-D inhibit activation of enzyme by apo-A-1
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additional information
peptides, initially present in a disordered conformation, are able to sense the lipid environment provided by lipoproteins of plasma and following a disorder-to-order transition, change their conformation to an ordered alpha-helix
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additional information
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peptides, initially present in a disordered conformation, are able to sense the lipid environment provided by lipoproteins of plasma and following a disorder-to-order transition, change their conformation to an ordered alpha-helix
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additional information
antibody 14F11 does not enhances the enzyme activity
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additional information
antibody 14F11 does not enhances the enzyme activity
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additional information
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antibody 14F11 does not enhances the enzyme activity
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