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Information on EC 3.1.1.13 - sterol esterase and Organism(s) Homo sapiens

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.1 Carboxylic-ester hydrolases
                3.1.1.13 sterol esterase
IUBMB Comments
A group of enzymes of broad specificity, acting on esters of sterols and long-chain fatty acids, that may also bring about the esterification of sterols. Activated by bile salts.
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This record set is specific for:
Homo sapiens
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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
cease, lysosomal acid lipase, cholesterol ester hydrolase, cholesteryl ester hydrolase, pancreatic cholesterol esterase, bile salt-stimulated lipase, cholesteryl esterase, neutral cholesteryl ester hydrolase, nceh1, kiaa1363, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acid cholesterol esterase
-
-
Acid cholesteryl ester hydrolase
-
-
-
-
acid lipase
-
-
acylcholesterol lipase
-
-
-
-
bile salt-activated lipase
-
-
bile salt-dependent cholesteryl ester hydrolase
-
-
bile-salt activated lipase
-
CE hydrolase
-
-
CEase
cholesterase
-
-
-
-
cholesterol ester hydrolase
-
-
-
-
cholesterol ester synthetase
-
-
-
-
cholesterol esterase
cholesteryl ester hydrolase
cholesteryl ester synthetase
-
-
-
-
cholesteryl esterase
-
-
-
-
KIAA1263/AADACL1
-
-
KIAA1363
-
-
lysosomal acid lipase
-
-
Nceh1
neutral CE hydrolase
-
neutral cholesterol ester hydrolase
-
-
neutral cholesterol ester hydrolase 1
neutral cholesterol esterase
-
-
sterol ester hydrolase
-
-
-
-
Sterol esterase
-
-
-
-
sterol-ester acylhydrolase
-
-
-
-
triterpenol esterase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
steryl ester + H2O = sterol + fatty acid
show the reaction diagram
a group of enzymes of broad specificity, acting on esters of sterols and long-chain fatty acids, that may also bring about the esterification of sterols. Activated by bile salts
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
esterification
-
-
-
-
hydrolysis of carboxylic ester
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
steryl-ester acylhydrolase
A group of enzymes of broad specificity, acting on esters of sterols and long-chain fatty acids, that may also bring about the esterification of sterols. Activated by bile salts.
CAS REGISTRY NUMBER
COMMENTARY hide
9026-00-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-methylumbelliferyl butyrate + H2O
4-methylumbelliferol + butyrate
show the reaction diagram
-
-
-
?
4-methylumbelliferyl oleate + H2O
4-methylumbelliferol + oleate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
show the reaction diagram
-
-
-
?
cholesteryl acetate + H2O
cholesterol + acetic acid
show the reaction diagram
-
very slowly hydrolyzed by acid cholesterol esterase, only hydrolyzed by neutral cholestrol esterase at pH 8.0
-
?
cholesteryl butyrate + H2O
cholesterol + butanoic acid
show the reaction diagram
-
very slowly hydrolyzed by acid cholesterol esterase, only hydrolyzed by neutral cholesterol esterase at pH 8.0
-
?
cholesteryl caprylate + H2O
cholesterol + caprylic acid
show the reaction diagram
-
-
-
?
cholesteryl esters + H2O
cholesterol + fatty acid
show the reaction diagram
cholesteryl laurate + H2O
cholesterol + lauric acid
show the reaction diagram
-
-
-
?
cholesteryl oleate
cholesterol + oleate
show the reaction diagram
cholesteryl oleate + H2O
cholesterol + oleate
show the reaction diagram
cholesteryl oleate + H2O
cholesterol + oleic acid
show the reaction diagram
fat-soluble vitamin esters + H2O
vitamin + ?
show the reaction diagram
-
-
-
?
lipoyl 4-aminobenzoate + H2O
4-aminobenzoate + lipoic acid
show the reaction diagram
-
-
-
?
p-nitrophenyl acetate + H2O
p-nitrophenol + acetic acid
show the reaction diagram
p-nitrophenyl hexanoate + H2O
p-nitrophenol + hexanoic acid
show the reaction diagram
-
-
-
-
?
triacetin + H2O
? + acetic acid
show the reaction diagram
-
-
-
?
triolein + H2O
dioleoylglycerol + oleic acid
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
cholesteryl esters + H2O
cholesterol + fatty acid
show the reaction diagram
cholesteryl oleate
cholesterol + oleate
show the reaction diagram
-
the cholesterol which is incorporated into brush border membrane is not esterified
-
?
fat-soluble vitamin esters + H2O
vitamin + ?
show the reaction diagram
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
activation for neutral cholesterol esterases
Mg2+
-
activation for neutral cholesterol esterases
Mn2+
-
activation for neutral cholesterol esterases
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2'-[(phenylcarbamoyl)oxy]biphenyl-2-yl octadecylcarbamate
-
-
2-(2,3-dichlorophenyl)-4H-naphtho[1,2-b]pyran-4-one
-
2-(2,4-difluorophenyl)-4H-naphtho[1,2-b]pyran-4-one
-
2-(2,4-dimethoxyphenyl)-4H-naphtho[1,2-b]pyran-4-one
-
2-(2,5-difluorophenyl)-4H-naphtho[1,2-b]pyran-4-one
-
2-(2,6-difluorophenyl)-4H-naphtho[1,2-b]pyran-4-one
-
2-(2-bromophenyl)-4H-naphtho[1,2-b]pyran-4-one
-
2-(2-fluorophenyl)-4H-naphtho[1,2-b]pyran-4-one
-
2-(2-iodophenyl)-4H-naphtho[1,2-b]pyran-4-one
-
2-(3,4-difluorophenyl)-4H-naphtho[1,2-b]pyran-4-one
-
2-(3,4-dimethoxyphenyl)-4H-naphtho[1,2-b]pyran-4-one
-
2-(3,5-difluorophenyl)-4H-naphtho[1,2-b]pyran-4-one
mixed-type inhibition. A-12 fits well in the catalytic site and is stabilized by hydrophobic interactions. It completely blocks the catalytic assembly of the enzyme and prevents it to participate in ester hydrolysis mechanism. The favorable binding confor
2-(3,5-dinitrophenyl)-4H-naphtho[1,2-b]pyran-4-one
-
2-(3-bromophenyl)-4H-naphtho[1,2-b]pyran-4-one
-
2-(3-chlorophenyl)-4H-naphtho[1,2-b]pyran-4-one
-
2-(3-fluorophenyl)-4H-naphtho[1,2-b]pyran-4-one
-
2-(3-methoxyphenyl)-4H-naphtho[1,2-b]pyran-4-one
-
2-(3-nitrophenyl)-4H-naphtho[1,2-b]pyran-4-one
-
2-(4-bromophenyl)-4H-naphtho[1,2-b]pyran-4-one
-
2-(4-fluorophenyl)-4H-naphtho[1,2-b]pyran-4-one
-
2-(4-iodophenyl)-4H-naphtho[1,2-b]pyran-4-one
-
2-(4-methoxyphenyl)-4H-naphtho[1,2-b]pyran-4-one
-
2-(4-methylphenyl)-4H-naphtho[1,2-b]pyran-4-one
-
2-(4-nitrophenyl)-4H-naphtho[1,2-b]pyran-4-one
-
2-(dimethylamino)-5,6,7,8-tetrahydro-4H-[1]benzothieno[2,3-d][1,3]oxazin-4-one
noncompetitive inhibition
2-(dimethylamino)-6,7-dihydro-4H,5H-cyclopenta[4,5]thieno[2,3-d][1,3]oxazin-4-one
noncompetitive inhibition
2-phenyl-4H-naphtho[1,2-b]pyran-4-one
-
2-[2-(trifluoromethyl)phenyl]-4H-naphtho[1,2-b]pyran-4-one
-
2-[2-fluoro-4-(trifluoromethyl)phenyl]-4H-naphtho[1,2-b]pyran-4-one
-
2-[2-fluoro-6-(trifluoromethyl)phenyl]-4H-naphtho[1,2-b]pyran-4-one
-
2-[3,5-bis(trifluoromethyl)phenyl]-4H-naphtho[1,2-b]pyran-4-one
-
2-[3-(chloromethyl)phenyl]-4H-naphtho[1,2-b]pyran-4-one
-
2-[3-(trifluoromethyl)phenyl]-4H-naphtho[1,2-b]pyran-4-one
-
2-[3-fluoro-5-(trifluoromethyl)phenyl]-4H-naphtho[1,2-b]pyran-4-one
-
2-[4-(chloromethyl)phenyl]-4H-naphtho[1,2-b]pyran-4-one
-
2-[4-(dimethylamino)phenyl]-4H-naphtho[1,2-b]pyran-4-one
-
2-[4-(trifluoromethyl)phenyl]-4H-naphtho[1,2-b]pyran-4-one
-
2-[4-fluoro-2-(trifluoromethyl)phenyl]-4H-naphtho[1,2-b]pyran-4-one
-
2-[4-fluoro-3-(trifluoromethyl)phenyl]-4H-naphtho[1,2-b]pyran-4-one
-
2-[5-fluoro-2-(trifluoromethyl)phenyl]-4H-naphtho[1,2-b]pyran-4-one
-
3,3'-[4-([2-[(4-chlorophenyl)carbonyl]hydrazinyl]sulfonyl)-1,2-oxazole-3,5-diyl]bis(N-hydroxypropanamide)
-
-
3-(2,3-dichlorophenyl)-1H-benzo[f]chromen-1-one
-
3-(2,4-difluorophenyl)-1H-benzo[f]chromen-1-one
-
3-(2,4-dimethoxyphenyl)-1H-benzo[f]chromen-1-one
-
3-(2,5-difluorophenyl)-1H-benzo[f]chromen-1-one
-
3-(2,6-difluorophenyl)-1H-benzo[f]chromen-1-one
-
3-(2-(trifluoromethyl)phenyl)-1H-benzo[f]chromen-1-one
-
3-(2-bromophenyl)-1H-benzo[f]chromen-1-one
-
3-(2-fluoro-4-(trifluoromethyl)phenyl)-1H-benzo[f]chromen-1-one
-
3-(2-fluoro-6-(trifluoromethyl)phenyl)-1H-benzo[f]chromen-1-one
-
3-(2-fluorophenyl)-1H-benzo[f]chromen-1-one
-
3-(2-iodophenyl)-1H-benzo[f]chromen-1-one
-
3-(3,4-difluorophenyl)-1H-benzo[f]chromen-1-one
-
3-(3,4-dimethoxyphenyl)-1H-benzo[f]chromen-1-one
-
3-(3,5-bis(trifluoromethyl)phenyl)-1H-benzo[f]chromen-1-one
-
3-(3,5-difluorophenyl)-1H-benzo[f]chromen-1-one
-
3-(3,5-dinitrophenyl)-1H-benzo[f]chromen-1-one
-
3-(3-(acetoxy)phenyl)-1H-benzo[f]chromen-1-one
-
3-(3-(chloromethyl)phenyl)-1H-benzo[f]chromen-1-one
-
3-(3-(trifluoromethyl)phenyl)-1H-benzo[f]chromen-1-one
-
3-(3-bromophenyl)-1H-benzo[f]chromen-1-one
-
3-(3-chlorophenyl)-1H-benzo[f]chromen-1-one
-
3-(3-fluoro-5-(trifluoromethyl)phenyl)-1H-benzo[f]chromen-1-one
-
3-(3-fluorophenyl)-1H-benzo[f]chromen-1-one
-
3-(3-nitrophenyl)-1H-benzo[f]chromen-1-one
-
3-(3-trifluoromethoxyphenyl)-1H-benzo[f]chromen-1-one
-
3-(4-(acetoxy)phenyl)-1H-benzo[f]chromen-1-one
-
3-(4-(chloromethyl)phenyl)-1H-benzo[f]chromen-1-one
-
3-(4-(dimethylamino)phenyl)-1H-benzo[f]chromen-1-one
-
3-(4-(trifluoromethyl)phenyl)-1H-benzo[f]chromen-1-one
-
3-(4-bromophenyl)-1H-benzo[f]chromen-1-one
-
3-(4-fluoro-2-(trifluoromethyl)phenyl)-1H-benzo[f]chromen-1-one
-
3-(4-fluoro-3-(trifluoromethyl)phenyl)-1H-benzo[f]chromen-1-one
-
3-(4-fluorophenyl)-1H-benzo[f]chromen-1-one
-
3-(4-iodophenyl)-1H-benzo[f]chromen-1-one
-
3-(4-methoxyphenyl)-1H-benzo[f]chromen-1-one
-
3-(4-nitrophenyl)-1H-benzo[f]chromen-1-one
-
3-(4-oxo-4H-naphtho[1,2-b]pyran-2-yl)phenyl acetate
-
3-(4-trifluoromethoxyphenyl)-1H-benzo[f]chromen-1-one
-
3-(5-fluoro-2-(trifluoromethyl)phenyl)-1H-benzo[f]chromen-1-one
-
3-p-tolyl-1H-benzo[f]chromen-1-one
-
3-phenyl-1H-benzo[f]chromen-1-one
-
4-(4-oxo-4H-naphtho[1,2-b]pyran-2-yl)phenyl acetate
-
4-chloro-3-(3-cyclopentylpropoxy)-1H-isochromen-1-one
-
-
4-chloro-3-(4-cyclohexylbutoxy)-1H-isochromen-1-one
-
-
4-[3,5-bis(trifluoromethyl)phenyl]-N-[3-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)propyl]piperazine-1-carboxamide
65.2% activity compared to control, at 0.025 mM
5-[3,5-bis[3-(1H-imidazol-5-yl)propyl]-1,2-oxazol-4-yl]-3-[[(4-chlorophenyl)sulfonyl]methyl]-1,2,4-oxadiazole
-
-
6-chloro-3-(2-cyclohexylethyl)-2H-pyran-2-one
-
-
6-chloro-3-cyclopentyl-2H-pyran-2-one
-
-
ammonium chloride
AS115
nonspecific inhibitor, the enzyme is about 85% inhibited by 0.01 mM AS115
brefeldin A
-
inhibition to 80%-90% of secreted enzyme into the medium of HepG2 cells
Ca2+
-
50% inhibition at 5 mM
cardiolipin
-
inhibitory if included as aqueous sonicated dispersions at 2.5 mg/ml
CD10645
-
-
Chloropromazine
-
50% inhibition at 0.05 mM
Chloroquine
-
90% inhibition at 30 mM
dithiothreitol
-
for neutral cholesterol esterase with pH optimum at 6.0 and for acid cholesterol esterase
dodecylboronic acid
-
50% inhibition at 1 mM
E600
-
strong for neutral cholesterol esterases
EDTA
-
inhibition only for neutral cholesterol esterases
GK03167
-
-
Hg2+
-
strong for acid and less for neutral cholesterol esterases
iodoacetate
-
acid and neutral cholesterol esterases
KCl
-
25% inhibition at 0.15 M
methyl 3-[(2-ethoxy-2-oxoethyl)(methyl)sulfamoyl]-5-[2-(1H-pyrrol-2-yl)ethyl]thiophene-2-carboxylate
-
-
MgSO4
-
abolishes activity at 0.15 M
monensin
-
inhibition to 50%-60% of secreted enzyme into the medium of HepG2 cells
N,N,N',N'-tetra(prop-2-en-1-yl)propane-1,3-disulfonamide
-
-
N-(3,5-dichlorophenyl)-N'-[3-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)propyl]urea
104% activity compared to control, at 0.025 mM
N-(3,5-difluorophenyl)-N'-[3-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)propyl]urea
103% activity compared to control, at 0.025 mM
N-(3,5-dimethoxyphenyl)-N'-[3-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)propyl]urea
110% activity compared to control, at 0.025 mM
N-(3,5-dimethylphenyl)-N'-[3-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)propyl]urea
105% activity compared to control, at 0.025 mM
N-(3,5-dinitrophenyl)-N'-[3-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)propyl]urea
80.5% activity compared to control, at 0.025 mM
N-(4-bromophenyl)-N'-[3-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)propyl]urea
104% activity compared to control, at 0.025 mM
N-(4-chlorophenyl)-N'-[3-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)propyl]urea
112% activity compared to control, at 0.025 mM
N-ethylmaleimide
N-[3',5'-bis(trifluoromethyl)[1,1'-biphenyl]-2-yl]-N'-[3-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)propyl]urea
72.5% activity compared to control, at 0.025 mM
N-[3',5'-bis(trifluoromethyl)[1,1'-biphenyl]-3-yl]-N'-[3-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)propyl]urea
100% activity compared to control, at 0.025 mM
N-[3',5'-bis(trifluoromethyl)[1,1'-biphenyl]-4-yl]-N'-[3-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)propyl]urea
90.2% activity compared to control, at 0.025 mM
N-[3,5-bis(trifluoromethyl)phenyl]-5-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)pentanamide
81.3% activity compared to control, at 0.025 mM; 91.1% activity compared to control, at 0.025 mM
N-[3,5-bis(trifluoromethyl)phenyl]-N'-[2-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)ethyl]urea
97.4% activity compared to control, at 0.025 mM
N-[3,5-bis(trifluoromethyl)phenyl]-N'-[3-(1,3-dioxo-1,3,4,5,6,7-hexahydro-2H-isoindol-2-yl)propyl]urea
64.8% activity compared to control, at 0.025 mM
N-[3,5-bis(trifluoromethyl)phenyl]-N'-[3-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)propyl]urea
noncompetitive inhibition, 64.1% activity compared to control, at 0.025 mM
N-[3,5-bis(trifluoromethyl)phenyl]-N'-[3-[(3aR,4S,7R,7aS)-1,3-dioxo-1,3,3a,4,7,7a-hexahydro-2H-4,7-methanoisoindol-2-yl]propyl]urea
84.8% activity compared to control, at 0.025 mM
N-[3,5-bis(trifluoromethyl)phenyl]-N'-[3-[(3aR,7aS)-1,3-dioxo-1,3,3a,4,7,7a-hexahydro-2H-isoindol-2-yl]propyl]urea
72.4% activity compared to control, at 0.025 mM
N-[3,5-bis(trifluoromethyl)phenyl]-N'-[3-[(3aR,7aS)-1,3-dioxooctahydro-2H-isoindol-2-yl]propyl]urea
80.6% activity compared to control, at 0.025 mM
N-[3,5-bis(trifluoromethyl)phenyl]-N'-[4-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)butyl]urea
competitive inhibition, 68.5% activity compared to control, at 0.025 mM
N-[3,5-bis(trifluoromethyl)phenyl]-N'-[5-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)pentyl]urea
49.3% activity compared to control, at 0.025 mM
N-[3-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)propyl]-4-phenylpiperazine-1-carboxamide
106% activity compared to control, at 0.025 mM
N-[3-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)propyl]-N'-(4-fluorophenyl)urea
107% activity compared to control, at 0.025 mM
N-[3-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)propyl]-N'-(4-methoxyphenyl)urea
107% activity compared to control, at 0.025 mM
N-[3-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)propyl]-N'-(4-methylphenyl)urea
105% activity compared to control, at 0.025 mM
N-[3-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)propyl]-N'-(4-nitrophenyl)urea
85.3% activity compared to control, at 0.025 mM
N-[3-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)propyl]-N'-phenylurea
108% activity compared to control, at 0.025 mM
N-[3-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)propyl]-N'-[4-(trifluoromethyl)phenyl]urea
116% activity compared to control, at 0.025 mM
NaF
-
abolishes activity at 0.15 M
NCI0040784
-
-
O-butyl phenylcarbamothioate
-
-
OPT-GK-1
-
-
OPT-NCI-1
-
-
OPT-SEW-5
-
-
OPTCD-2
-
-
p-hydroxymercuribenzoate
phenylboronic acid
-
50% inhibition at 10 mM
phosphatidylinositol
-
inhibitory if included as aqueous sonicated dispersions at 2.5 mg/ml
phosphatidylserine
-
inhibitory if included as aqueous sonicated dispersions at 2.5 mg/ml
progesterone
-
marked inhibition, additive effect if chloroquine is present
resveratrol
-
-
SEW00846
-
-
wine polyphenolic extract
-
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
-
esterification doubled
bile salt
-
-
glycocholate
-
slightly activation at 40 mM
NaCl
-
the nCEH activity in the whole cell lysates from NCEH-transfected cells is slightly stimulated by low concentrations of NaCl (6.5% at 0.05M)
sodium cholate
-
activates optimal at 40 mM
sodium taurocholic acid
additional information
-
enzyme associates with mixed as well as triacylglycerol depleted droplets, enzyme activity is 2.5fold higher with mixed droplets
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.008
cholesteryl oleate
-
in presence of 40 mM sodium cholate
0.0122 - 0.0384
p-nitrophenyl hexanoate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00431
2-(dimethylamino)-5,6,7,8-tetrahydro-4H-[1]benzothieno[2,3-d][1,3]oxazin-4-one
pH 7.0, 30°C, recombinant enzyme
0.00434
2-(dimethylamino)-6,7-dihydro-4H,5H-cyclopenta[4,5]thieno[2,3-d][1,3]oxazin-4-one
pH 7.0, 30°C, recombinant enzyme
0.05
Chloropromazine
-
-
1
dodecylboronic acid
-
-
0.01
N-[3,5-bis(trifluoromethyl)phenyl]-N'-[3-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)propyl]urea
pH 7.0, 30°C, recombinant enzyme
0.0118
N-[3,5-bis(trifluoromethyl)phenyl]-N'-[4-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)butyl]urea
pH 7.0, 30°C, recombinant enzyme
10
phenylboronic acid
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00001085
2-(2,3-dichlorophenyl)-4H-naphtho[1,2-b]pyran-4-one
Homo sapiens
at pH 7.0 and 25°C
0.00000143
2-(2,4-difluorophenyl)-4H-naphtho[1,2-b]pyran-4-one
Homo sapiens
at pH 7.0 and 25°C
0.00000681
2-(2,5-difluorophenyl)-4H-naphtho[1,2-b]pyran-4-one
Homo sapiens
at pH 7.0 and 25°C
0.00000199
2-(2,6-difluorophenyl)-4H-naphtho[1,2-b]pyran-4-one
Homo sapiens
at pH 7.0 and 25°C
0.00001101
2-(2-bromophenyl)-4H-naphtho[1,2-b]pyran-4-one
Homo sapiens
at pH 7.0 and 25°C
0.00000322
2-(2-fluorophenyl)-4H-naphtho[1,2-b]pyran-4-one
Homo sapiens
at pH 7.0 and 25°C
0.00001612
2-(2-iodophenyl)-4H-naphtho[1,2-b]pyran-4-one
Homo sapiens
at pH 7.0 and 25°C
0.00001408
2-(3,4-difluorophenyl)-4H-naphtho[1,2-b]pyran-4-one
Homo sapiens
at pH 7.0 and 25°C
0.00000078
2-(3,5-difluorophenyl)-4H-naphtho[1,2-b]pyran-4-one
Homo sapiens
at pH 7.0 and 25°C
0.00003004
2-(3,5-dinitrophenyl)-4H-naphtho[1,2-b]pyran-4-one
Homo sapiens
at pH 7.0 and 25°C
0.00002609
2-(3-bromophenyl)-4H-naphtho[1,2-b]pyran-4-one
Homo sapiens
at pH 7.0 and 25°C
0.00000699
2-(3-chlorophenyl)-4H-naphtho[1,2-b]pyran-4-one
Homo sapiens
at pH 7.0 and 25°C
0.00000524
2-(3-fluorophenyl)-4H-naphtho[1,2-b]pyran-4-one
Homo sapiens
at pH 7.0 and 25°C
0.00002514
2-(3-nitrophenyl)-4H-naphtho[1,2-b]pyran-4-one
Homo sapiens
at pH 7.0 and 25°C
0.00002851
2-(4-bromophenyl)-4H-naphtho[1,2-b]pyran-4-one
Homo sapiens
at pH 7.0 and 25°C
0.0000201
2-(4-fluorophenyl)-4H-naphtho[1,2-b]pyran-4-one
Homo sapiens
at pH 7.0 and 25°C
0.00003415
2-(4-iodophenyl)-4H-naphtho[1,2-b]pyran-4-one
Homo sapiens
at pH 7.0 and 25°C
0.00003733
2-(4-nitrophenyl)-4H-naphtho[1,2-b]pyran-4-one
Homo sapiens
at pH 7.0 and 25°C
0.00003898
2-[2-fluoro-4-(trifluoromethyl)phenyl]-4H-naphtho[1,2-b]pyran-4-one
Homo sapiens
at pH 7.0 and 25°C
0.00003889
2-[2-fluoro-6-(trifluoromethyl)phenyl]-4H-naphtho[1,2-b]pyran-4-one
Homo sapiens
at pH 7.0 and 25°C
0.00004003
2-[3-(chloromethyl)phenyl]-4H-naphtho[1,2-b]pyran-4-one
Homo sapiens
at pH 7.0 and 25°C
0.00004299
2-[3-fluoro-5-(trifluoromethyl)phenyl]-4H-naphtho[1,2-b]pyran-4-one
Homo sapiens
at pH 7.0 and 25°C
0.00003923
2-[4-(chloromethyl)phenyl]-4H-naphtho[1,2-b]pyran-4-one
Homo sapiens
at pH 7.0 and 25°C
0.00003908
2-[4-fluoro-2-(trifluoromethyl)phenyl]-4H-naphtho[1,2-b]pyran-4-one
Homo sapiens
at pH 7.0 and 25°C
0.00004303
2-[4-fluoro-3-(trifluoromethyl)phenyl]-4H-naphtho[1,2-b]pyran-4-one
Homo sapiens
at pH 7.0 and 25°C
0.00004128
2-[5-fluoro-2-(trifluoromethyl)phenyl]-4H-naphtho[1,2-b]pyran-4-one
Homo sapiens
at pH 7.0 and 25°C
0.00000073
3-(2,3-dichlorophenyl)-1H-benzo[f]chromen-1-one
Homo sapiens
pH and temperature not specified in the publication
0.00000146
3-(2,4-difluorophenyl)-1H-benzo[f]chromen-1-one
Homo sapiens
pH and temperature not specified in the publication
0.00000108
3-(2,5-difluorophenyl)-1H-benzo[f]chromen-1-one
Homo sapiens
pH and temperature not specified in the publication
0.00000119
3-(2,6-difluorophenyl)-1H-benzo[f]chromen-1-one
Homo sapiens
pH and temperature not specified in the publication
0.00003135
3-(2-(trifluoromethyl)phenyl)-1H-benzo[f]chromen-1-one
Homo sapiens
pH and temperature not specified in the publication
0.00000469
3-(2-bromophenyl)-1H-benzo[f]chromen-1-one
Homo sapiens
pH and temperature not specified in the publication
0.00002311
3-(2-fluoro-4-(trifluoromethyl)phenyl)-1H-benzo[f]chromen-1-one
Homo sapiens
pH and temperature not specified in the publication
0.00002917
3-(2-fluoro-6-(trifluoromethyl)phenyl)-1H-benzo[f]chromen-1-one
Homo sapiens
pH and temperature not specified in the publication
0.00000259
3-(2-fluorophenyl)-1H-benzo[f]chromen-1-one
Homo sapiens
pH and temperature not specified in the publication
0.00000955
3-(2-iodophenyl)-1H-benzo[f]chromen-1-one
Homo sapiens
pH and temperature not specified in the publication
0.00000115
3-(3,4-difluorophenyl)-1H-benzo[f]chromen-1-one
Homo sapiens
pH and temperature not specified in the publication
0.00000099
3-(3,5-difluorophenyl)-1H-benzo[f]chromen-1-one
Homo sapiens
pH and temperature not specified in the publication
0.0000098
3-(3,5-dinitrophenyl)-1H-benzo[f]chromen-1-one
Homo sapiens
pH and temperature not specified in the publication
0.00002005
3-(3-(chloromethyl)phenyl)-1H-benzo[f]chromen-1-one
Homo sapiens
pH and temperature not specified in the publication
0.00000601
3-(3-bromophenyl)-1H-benzo[f]chromen-1-one
Homo sapiens
pH and temperature not specified in the publication
0.00000083
3-(3-chlorophenyl)-1H-benzo[f]chromen-1-one
Homo sapiens
pH and temperature not specified in the publication
0.00002911
3-(3-fluoro-5-(trifluoromethyl)phenyl)-1H-benzo[f]chromen-1-one
Homo sapiens
pH and temperature not specified in the publication
0.0000039
3-(3-fluorophenyl)-1H-benzo[f]chromen-1-one
Homo sapiens
pH and temperature not specified in the publication
0.00001644
3-(3-nitrophenyl)-1H-benzo[f]chromen-1-one
Homo sapiens
pH and temperature not specified in the publication
0.00002223
3-(4-(chloromethyl)phenyl)-1H-benzo[f]chromen-1-one
Homo sapiens
pH and temperature not specified in the publication
0.00000815
3-(4-bromophenyl)-1H-benzo[f]chromen-1-one
Homo sapiens
pH and temperature not specified in the publication
0.0000045
3-(4-fluorophenyl)-1H-benzo[f]chromen-1-one
Homo sapiens
pH and temperature not specified in the publication
0.00001311
3-(4-iodophenyl)-1H-benzo[f]chromen-1-one
Homo sapiens
pH and temperature not specified in the publication
0.00001801
3-(4-nitrophenyl)-1H-benzo[f]chromen-1-one
Homo sapiens
pH and temperature not specified in the publication
0.00002779
3-(5-fluoro-2-(trifluoromethyl)phenyl)-1H-benzo[f]chromen-1-one
Homo sapiens
pH and temperature not specified in the publication
0.00005106
3-phenyl-1H-benzo[f]chromen-1-one
Homo sapiens
pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.002
-
activity after 6 h in cell homogenate
0.002 - 0.009
-
activities of secreted enzyme from 0 h up to 102 h
0.027
-
in absence of taurocholic acid
0.045
-
in presence of 2 mM taurocholic acid
0.066
-
in presence of 10 mM taurocholic acid
0.15
-
-
234.6
-
lipase activity in presence of 10 mM sodium taurocholic acid
47.7
-
esterase activity in absence of sodium taurocholic acid
98.1
-
esterase activity in presence of 10 mM sodium taurocholic acid
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5
-
hydrolysis of cholesteryl esters
5 - 6
-
in presence of 0.05-0.5 M NaCl, bovine serum albumin or ovalbumin
6.2
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
assay at
30
assay at
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
expressed at high levels in kidney
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
redistribution of enzyme from cytosol to lipid droplets upon lipid loading of THP-1 macrophages. Enzyme associates with mixed as well as triacylglycerol depleted droplets, enzyme activity is 2.5fold higher with mixed droplets
Manually annotated by BRENDA team
-
redistribution of enzyme from cytosol to lipid droplets upon lipid loading of THP-1 macrophages. Enzyme associates with mixed as well as triacylglycerol depleted droplets, enzyme activity is 2.5fold higher with mixed droplets
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
enzyme inhibition has a hypocholesterolaemic effect. Inhibition of the enzyme by bitter melon aqueous extract can play a role in decreased intestinal cholesterol absorption, and micelle formation
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
EST1_HUMAN
567
0
62521
Swiss-Prot
Secretory Pathway (Reliability: 2)
CEL_HUMAN
753
0
79322
Swiss-Prot
Secretory Pathway (Reliability: 1)
LICH_HUMAN
399
0
45419
Swiss-Prot
Secretory Pathway (Reliability: 1)
NCEH1_HUMAN
408
1
45808
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
105000
-
SDS-PAGE
106000
-
x * 106000, SDS-PAGE
40000
45000
x * 45000, human NCEH1 protein is recognized as duplets with molecular mass of 40000 and 45000 Da, SDS-PAGE
66000
-
x * 66000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 105000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
-
side-chain modification
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N270Q
-
enzyme activity level of the mutant is significantly reduced compared with wild type
N367Q
-
enzyme activity level of the mutant is significantly reduced compared with wild type
N389Q
-
the mutant shows incomplete glycosylation
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
-
discriminated at acid pH, neutral cholesterol esterases more heat-labile than acid cholesterol esterase
90
-
complete loss of activity after 15 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
highly unstable at 4°C
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
thiols required for stabilizing activity
-
133842
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 80% loss of activity, 2 weeks
-
4°C, 0.02 mM bovine serum albumin, 20 h
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
2-step chromatography techniques to homogeneity
-
butyl-Sepharose column chromatography and SP-Sepharose column chromatography
-
recombinant C-terminally double-StrepII-tagged enzyme from HEK-293 EBNA cells by affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in HEK-293 cells
-
expressed in Mus musculus liver
-
expressed in Nicotiana benthamiana
-
expression in lal-/- mice and macrophages
-
expression in LDL receptor null mice
-
GFP-tagged enzyme is overexpressed in RAW264.7 cells
-
overexpression in doxycycline-controlled system in mouse respiratory epithelial cells
-
recombinant expression of C-terminally double-StrepII-tagged enzyme in HEK-293 EBNA cells
stable overexpression in human cell line THP1
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
hormone-sensitive lipase inhibition does not decrease neutral cholesterol ester hydrolase 1 activity
monocyte-derived macrophages show a robust increase in neutral cholesterol ester hydrolase activity during the differentiation from monocytes up to day 8 (14.9fold). Treatment by macrophage colony-stimulating factor and granulocyte/macrophage colony-stimulating factor increases the amounts of NCEH1 protein 2.4fold and 3.5fold, repsectively
NCEH1 becomes up-regulated during macrophage differentiation
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
nutrition
-
resveratrol and red wine polyphenolic extraxts decrease enzyme activity. In vivo, these effects can decrease hydrolysis of dietary lipid esters and the absorption of free cholesterol
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tanaka, H.; Mierau, I.; Ito, F.
Purification and characterization of bovine pancreatic bile salt-activated lipase
J. Biochem.
125
883-890
1999
Bos taurus, Homo sapiens
Manually annotated by BRENDA team
Winkler, K.E.; Harrison, E.H.; Marsh, J.B.; Glick, J.M.
Characterization of a bile salt-dependent cholesteryl ester hydrolase activity secreted from HepG2 cells
Biochim. Biophys. Acta
1126
151-158
1992
Homo sapiens, Rattus sp.
Manually annotated by BRENDA team
Negre, A.; Salvayre, R.; Rogalle, P.; Dang, Q.Q.; Douste-Blazy, L.
Acyl-chain specificity and properties of cholesterol esterases from normal and Wolman lymphoid cell lines
Biochim. Biophys. Acta
918
76-82
1987
Homo sapiens
Manually annotated by BRENDA team
Slotte, J.P.; Ekman, S.
Synthesis and hydrolysis of cholesteryl esters by isolated rat-liver lysosomes and cell-free extracts of human lung fibroblasts
Biochim. Biophys. Acta
879
221-228
1986
Homo sapiens, Rattus sp.
Manually annotated by BRENDA team
Sando, G.N.; Rosenbaum, L.M.
Human lysosomal acid lipase/cholesteryl ester hydrolase. Purification and properties of the form secreted by fibroblasts in microcarrier culture
J. Biol. Chem.
260
15186-15193
1985
Homo sapiens
Manually annotated by BRENDA team
Hui, D.Y.; Hayakawa, K.; Oizum, J.
Lipoamidase activity in normal and mutagenized pancreatic cholesterol esterase (bile salt-stimulated lipase)
Biochem. J.
291
65-69
1993
Homo sapiens, Rattus sp.
-
Manually annotated by BRENDA team
Ikeda, I.; Mitsui, K.; Matsuoka, R.; Hamada, T.; Imabayashi, S.; Uchino, A.; Yamada, K.; Imaizumi, K.
Cholesterol esterase bound to intestinal brush border membranes does not accelerate incorporation of micellar cholesterol into absorptive cells
Biosci. Biotechnol. Biochem.
67
2381-2387
2003
Bos taurus, Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Fresnedo, O.; De Heredia, M.L.; Martinez, M.J.; Cristobal, S.; Rejas, M.T.; Cuezva, J.M.; Ochoa, B.
Immunolocalization of a novel cholesteryl ester hydrolase in the endoplasmic reticulum of murine and human hepatocytes
Hepatology
33
662-667
2001
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Sbarra, V.; Ristorcelli, E.; Petit-Thevenin, J.L.; Teissedre, P.L.; Lombardo, D.; Verine, A.
In vitro polyphenol effects on activity, expression and secretion of pancreatic bile salt-dependent lipase
Biochim. Biophys. Acta
1736
67-76
2005
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Zhao, B.; Fisher, B.J.; St Clair, R.W.; Rudel, L.L.; Ghosh, S.
Redistribution of macrophage cholesteryl ester hydrolase from cytoplasm to lipid droplets upon lipid loading
J. Lipid Res.
46
2114-2121
2005
Homo sapiens
Manually annotated by BRENDA team
Zhao, B.; Natarajan, R.; Ghosh, S.
Human liver cholesteryl ester hydrolase: cloning, molecular characterization, and role in cellular cholesterol homeostasis
Physiol. Genomics
23
304-310
2005
Homo sapiens
Manually annotated by BRENDA team
Yan, C.; Lian, X.; Li, Y.; Dai, Y.; White, A.; Qin, Y.; Li, H.; Hume, D.A.; Du, H.
Macrophage-specific expression of human lysosomal acid lipase corrects inflammation and pathogenic phenotypes in lal-/- mice
Am. J. Pathol.
169
916-926
2006
Homo sapiens
Manually annotated by BRENDA team
Zhao, B.; Song, J.; St Clair, R.W.; Ghosh, S.
Stable overexpression of human macrophage cholesteryl ester hydrolase results in enhanced free cholesterol efflux from human THP1 macrophages
Am. J. Physiol. Cell Physiol.
292
C405-C412
2007
Homo sapiens
Manually annotated by BRENDA team
Li, Y.; Qin, Y.; Li, H.; Wu, R.; Yan, C.; Du, H.
Lysosomal acid lipase over-expression disrupts lamellar body genesis and alveolar structure in the lung
Int. J. Exp. Pathol.
88
427-436
2007
Homo sapiens
Manually annotated by BRENDA team
Zhao, B.; Song, J.; Chow, W.N.; St Clair, R.W.; Rudel, L.L.; Ghosh, S.
Macrophage-specific transgenic expression of cholesteryl ester hydrolase significantly reduces atherosclerosis and lesion necrosis in Ldlr mice
J. Clin. Invest.
117
2983-2992
2007
Homo sapiens
Manually annotated by BRENDA team
Okazaki, H.; Igarashi, M.; Nishi, M.; Sekiya, M.; Tajima, M.; Takase, S.; Takanashi, M.; Ohta, K.; Tamura, Y.; Okazaki, S.; Yahagi, N.; Ohashi, K.; Amemiya-Kudo, M.; Nakagawa, Y.; Nagai, R.; Kadowaki, T.; Osuga, J.; Ishibashi, S.
Identification of neutral cholesterol ester hydrolase, a key enzyme removing cholesterol from macrophages
J. Biol. Chem.
283
33357-33364
2008
Homo sapiens, Mus musculus (Q8BLF1), Mus musculus
Manually annotated by BRENDA team
Du, H.; Cameron, T.L.; Garger, S.J.; Pogue, G.P.; Hamm, L.A.; White, E.; Hanley, K.M.; Grabowski, G.A.
Wolman disease/cholesteryl ester storage disease: efficacy of plant-produced human lysosomal acid lipase in mice
J. Lipid Res.
49
1646-1657
2008
Homo sapiens
Manually annotated by BRENDA team
Zhao, B.; Song, J.; Ghosh, S.
Hepatic overexpression of cholesteryl ester hydrolase enhances cholesterol elimination and in vivo reverse cholesterol transport
J. Lipid Res.
49
2212-2217
2008
Homo sapiens
Manually annotated by BRENDA team
Igarashi, M.; Osuga, J.; Uozaki, H.; Sekiya, M.; Nagashima, S.; Takahashi, M.; Takase, S.; Takanashi, M.; Li, Y.; Ohta, K.; Kumagai, M.; Nishi, M.; Hosokawa, M.; Fledelius, C.; Jacobsen, P.; Yagyu, H.; Fukayama, M.; Nagai, R.; Kadowaki, T.; Ohashi, K.; Ishibashi, S.
The critical role of neutral cholesterol ester hydrolase 1 in cholesterol removal from human macrophages
Circ. Res.
107
1387-1395
2010
Homo sapiens (Q6PIU2), Homo sapiens
Manually annotated by BRENDA team
Sekiya, M.; Osuga, J.; Igarashi, M.; Okazaki, H.; Ishibashi, S.
The role of neutral cholesterol ester hydrolysis in macrophage foam cells
J. Artheroscler. Thromb.
18
359-364
2011
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
John, S.; Thangapandian, S.; Sakkiah, S.; Lee, K.W.
Discovery of potential pancreatic cholesterol esterase inhibitors using pharmacophore modelling, virtual screening, and optimization studies
J. Enzyme Inhib. Med. Chem.
26
535-545
2011
Homo sapiens
Manually annotated by BRENDA team
Igarashi, M.; Osuga, J.; Isshiki, M.; Sekiya, M.; Okazaki, H.; Takase, S.; Takanashi, M.; Ohta, K.; Kumagai, M.; Nishi, M.; Fujita, T.; Nagai, R.; Kadowaki, T.; Ishibashi, S.
Targeting of neutral cholesterol ester hydrolase to the endoplasmic reticulum via its N-terminal sequence
J. Lipid Res.
51
274-285
2010
Homo sapiens
Manually annotated by BRENDA team
John, S.; Thangapandian, S.; Lazar, P.; Son, M.; Park, C.; Lee, K.W.
New insights in the activation of human cholesterol esterase to design potent anti-cholesterol drugs
Mol. Divers.
18
119-131
2014
Homo sapiens
Manually annotated by BRENDA team
Singh, H.; Singh, J.V.; Gupta, M.K.; Singh, P.; Sharma, S.; Nepali, K.; Bedi, P.M.S.
Benzoflavones as cholesterol esterase inhibitors Synthesis, biological evaluation and docking studies
Bioorg. Med. Chem. Lett.
27
850-854
2017
Homo sapiens (P19835)
Manually annotated by BRENDA team
Dato, F.M.; Sheikh, M.; Uhl, R.Z.; Schueller, A.W.; Steinkrueger, M.; Koch, P.; Neudoerfl, J.M.; Guetschow, M.; Goldfuss, B.; Pietsch, M.
omega-Phthalimidoalkyl aryl ureas as potent and selective inhibitors of cholesterol esterase
ChemMedChem
13
1833-1847
2018
Homo sapiens (P19835), Mus musculus (Q64285)
Manually annotated by BRENDA team
Su, J.; Wang, H.; Ma, C.; Liu, C.; Gao, C.; Nie, R.; Tanver Rahman, M.R.
Hypocholesterolaemic mechanism of bitter melon aqueous extracts via inhibition of pancreatic cholesterol esterase and reduction of cholesterol micellar solubility
Int. J. Food Sci. Nutr.
67
20-28
2016
Homo sapiens (P19835)
Manually annotated by BRENDA team
Singh, J.V.; Kaur, A.; Bhagat, K.; Gupta, M.K.; Singh, M.; Singh, H.; Bedi, P.M.S.
5,6-Benzoflavones as cholesterol esterase inhibitors synthesis, biological evaluation and docking studies
MedChemComm
9
490-502
2018
Homo sapiens (P19835)
Manually annotated by BRENDA team