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Enzyme Nomenclature
Information on EC 3.1.1.13 - sterol esterase
for references in articles please use BRENDA:EC3.1.1.13
Word Map on EC 3.1.1.13
- 3.1.1.13
-
cessation
- women
- macrophage
- triglyceride
- children
-
smoke
- arterial
-
smoking
- infant
-
services
-
social
-
proliferate
-
decision
- pain
-
acyltransferase
- adrenal
- oleate
- atherosclerosis
-
discharge
-
physician
- triacylglycerols
-
policy
-
foam
-
esterify
-
lipases
-
psychological
-
firing
-
ethic
- taurocholate
-
professionals
-
quit
-
school
-
advice
-
practitioner
-
financial
-
unesterified
-
a:cholesterol
-
doctor
-
breastfeeding
- nurses
-
acyl-coa:cholesterol
-
legal
-
profession
-
political
- triolein
-
waking
-
legislation
-
moral
-
childbearing
-
breast-fed
- analysis
- medicine
- paper production
- nutrition
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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EC NUMBER 
COMMENTARY 
3.1.1.13
-
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RECOMMENDED NAME
GeneOntology No.
sterol esterase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a steryl ester + H2O = a sterol + a fatty acid
a group of enzymes of broad specificity, acting on esters of sterols and long-chain fatty acids, which may also bring about the esterification of sterols. Activated by bile salts; broad specificity
-
-
-
a steryl ester + H2O = a sterol + a fatty acid
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, the catalytic tiad is formed by Ser209, Glu341, and His449
-
a steryl ester + H2O = a sterol + a fatty acid
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 mechanism, catalytic triad consists of Ser194, His435, and Asp320
-
a steryl ester + H2O = a sterol + a fatty acid
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
-
a steryl ester + H2O = a sterol + a fatty acid
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
-
a steryl ester + H2O = a sterol + a fatty acid
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
-
a steryl ester + H2O = a sterol + a fatty acid
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
-
a steryl ester + H2O = a sterol + a fatty acid
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
-
a steryl ester + H2O = a sterol + a fatty acid
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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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
esterification
-
-
-
-
hydrolysis of carboxylic ester
hydrolysis of carboxylic ester
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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.
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CAS REGISTRY NUMBER
COMMENTARY
9026-00-0
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
enzyme activity in commercial lipase preparation from Asahi, comparison of different preparations
-
-
enzyme activity in commercial lipase preparation from Amano, comparison of different preparations
-
-
-
133823, 133824, 133826, 133827, 133828, 133830, 133833, 133834, 133835, 133837, 133839, 133840, 133841, 133843, 133846, 133853, 133855, 133859, 133861, 133862
-
-
-
133823, 133843, 133844, 133845, 133846, 133852, 133857, 133860, 650378, 650546, 652623, 680937, 691224, 694982, 703557, 714754, 715996, 716844, 729377, 729673
-
-
-
133822, 133826, 133829, 133844, 133848, 133850, 133851, 133854, 650358, 650646, 650664, 652274, 664455, 665965, 665983, 680113, 714754
-
-
-
133822, 133835, 133838, 133841, 133842, 133862, 651441, 664196, 665963, 666549, 677448, 677459, 680227, 681075, 693179, 693513, 693519, 715324, 715745, 715834, 730396
-
-
enzyme activity in commercial lipase preparation from Amano, comparison of different preparations
-
-
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
-
hormone-sensitive lipase deficiency remarkably reduces the neutral cholesterol ester hydrolase activity in adrenal glands. Abrogation of neutral cholesterol ester hydrolytic activity causes adrenal enlargement
malfunction
-
neutral cholesterol ester hydrolase 1/hormone-sensitive lipase-deficient mice develop atherosclerosis faster than the control and single deficient bone marrow recipients
physiological function
-
Nceh1 is involved in the adrenal cholesterol metabolism, and the cholesterol ester hydrolytic activity in adrenal glands is associated with the organ enlargement
physiological function
neutral cholesterol ester hydrolase1 is expressed in human atheromatous lesions, where it plays a critical role in the hydrolysis of cholesterol ester in human macrophage foam cells, thereby contributing to the initial part of reverse cholesterol transport in human atherosclerosis
physiological function
-
neutral cholesterol ester hydrolase 1 protects against foam cell formation and atherosclerosis
physiological function
-
neutral cholesterol ester hydrolase 1 protects against foam cell formation and atherosclerosis
physiological function
-
NCEH hydrolyzes cholesterol ester to deliver cholesterol for efflux out of the macrophage cells
physiological function
-
the enzyme plays a dominant role over hormone-sensitive lipase in the hydrolysis of cholesteryl ester and subsequent cholesterol efflux in mouse peritoneal macrophages
physiological function
-
cholesterol esterase is involved in the regulation of plasma cholesterol level
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-(diethylamino)-5,6,7,8-tetrahydro-4H-[1]benzothieno[2,3-d][1,3]oxazin-4-one + H2O
?
-
-
-
?
2-(diethylamino)-6,7-dihydro-4H,5H-cyclopenta[4,5]thieno[2,3-d][1,3]oxazin-4-one + H2O
?
-
-
-
?
2-(diethylamino)-6,7-dihydro-4H,5H-cyclopenta[4,5]thieno[2,3-d][1,3]thiazin-4-one + H2O
?
-
-
-
?
2-(dimethylamino)-1,5,6,7-tetrahydro-2H,4H-cyclopenta(4,5)thieno(2,3-d)(1,3)oxazin-4-one + H2O
?
-
-
-
-
?
4-methylumbelliferyl oleate + H2O
4-methylumbelliferone + oleic acid
-
-
-
?
cholesterol + oleate
cholesteryl oleate + H2O
-
100% esterification with 50 units of enzyme after 20 h. The enzyme is largely independent of water content in the synthesis of cholesteryl oleate, and it achieves near-complete esterification in the presence of an equimolar excess of oleate
-
-
?
cholesterol ester + H2O
cholesterol + fatty acid
-
hydrolysis level greatly exceeds the synthesis level, enzyme can simultaneously perform synthesis and hydrolysis reactions
-
r
cholesterol hexanoate + H2O
cholesterol + hexanoic acid
29% of the activity with cholesteryl linoleate
-
-
?
cholesterol palmitate + H2O
cholesterol + palmitic acid
5% of the activity with cholesteryl linoleate
-
-
?
p-nitrophenyl caprylate + H2O
p-nitrophenol + caprylic acid
-
activity increases with more lipophilic substrates
-
?
p-nitrophenyl laurate + H2O
p-nitrophenol + lauric acid
92% of the activity with cholesteryl linoleate
-
-
?
p-nitrophenyl propionate + H2O
p-nitrophenol + propionic acid
17% of the activity with cholesteryl linoleate
-
-
?
p-nitrophenyl stearate + H2O
p-nitrophenol + stearic acid
38% of the activity with cholesteryl linoleate
-
-
?
sitosterol oleate + H2O
sitosterol + oleate
-
about 60% activity compared to cholesteryl oleate
-
-
?
sitosterol palmitate + H2O
sitosterol + palmitate
-
about 30% activity compared to cholesteryl oleate
-
-
?
sitosterol stearate + H2O
sitosterol + stearate
-
about 30% activity compared to cholesteryl oleate
-
-
?
stigmastanol oleate + H2O
stigmastanol + oleate
-
about 65% activity compared to cholesteryl oleate
-
-
?
stigmastanol palmitate + H2O
stigmastanol + palmitate
-
about 30% activity compared to cholesteryl oleate
-
-
?
stigmastanol stearate + H2O
stigmastanol + stearate
-
about 20% activity compared to cholesteryl oleate
-
-
?
stigmasterol oleate + H2O
stigmasterol + oleate
-
about 35% activity compared to cholesteryl oleate
-
-
?
stigmasterol palmitate + H2O
stigmasterol + palmitate
-
about 15% activity compared to cholesteryl oleate
-
-
?
stigmasterol stearate + H2O
stigmasterol + stearate
-
about 15% activity compared to cholesteryl oleate
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
-
-
?
4-nitrophenyl myristate + H2O
4-nitrophenol + myristate
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
-
?
bis(2-ethylhexyl) phthalate + H2O
mono(2-ethylhexyl)phthalate + ?
-
complete hydrolysis within 15 min
-
-
?
bis(2-ethylhexyl) phthalate + H2O
mono(2-ethylhexyl)phthalate + ?
-
complete hydrolysis within 15 min
-
-
?
cholesterol acetate + H2O
cholesterol + acetic acid
3% of the activity with cholesteryl linoleate
-
-
?
cholesterol acetate + H2O
cholesterol + acetic acid
3% of the activity with cholesteryl linoleate
-
-
?
cholesterol butyrate + H2O
cholesterol + butyric acid
18% of the activity with cholesteryl linoleate
-
-
?
cholesterol butyrate + H2O
cholesterol + butyric acid
18% of the activity with cholesteryl linoleate
-
-
?
cholesterol decanoate + H2O
cholesterol + decanoic acid
34% of the activity with cholesteryl linoleate
-
-
?
cholesterol decanoate + H2O
cholesterol + decanoic acid
34% of the activity with cholesteryl linoleate
-
-
?
cholesterol oleate + H2O
cholesterol + oleic acid
53% of the activity with cholesteryl linoleate
-
-
?
cholesterol oleate + H2O
cholesterol + oleic acid
53% of the activity with cholesteryl linoleate
-
-
?
cholesteryl acetate + H2O
cholesterol + acetate
-
low activity, 6% of the activity with cholesteryl linoleate
-
?
cholesteryl acetate + H2O
cholesterol + acetate
-
-
-
?
cholesteryl acetate + H2O
cholesterol + acetate
-
9% activity compared to linoleate
-
-
?
cholesteryl acetate + H2O
cholesterol + acetate
-
9% activity compared to linoleate
-
-
?
cholesteryl acetate + H2O
cholesterol + acetic acid
-
very slowly hydrolyzed by acid cholesterol esterase, only hydrolyzed by neutral cholestrol esterase at pH 8.0
-
?
cholesteryl butyrate + H2O
cholesterol + butanoic acid
-
very slowly hydrolyzed by acid cholesterol esterase, only hydrolyzed by neutral cholesterol esterase at pH 8.0
-
?
cholesteryl butyrate + H2O
cholesterol + butyrate
-
low activity, 8% of the activity with cholesteryl linoleate
-
?
cholesteryl butyrate + H2O
cholesterol + butyrate
-
121% activity compared to linoleate
-
-
?
cholesteryl caprate + H2O
cholesterol + caprate
-
40% of the activity with cholesteryl linoleate
-
?
cholesteryl caprate + H2O
cholesterol + caprate
-
21% activity compared to linoleate
-
-
?
cholesteryl caproate + H2O
cholesterol + caproate
-
22% of the activity with cholesteryl linoleate
-
?
cholesteryl caproate + H2O
cholesterol + caproate
-
37% activity compared to linoleate
-
-
?
cholesteryl caprylate + H2O
cholesterol + caprylate
-
62% of the activity with cholesteryl linoleate
-
?
cholesteryl caprylate + H2O
cholesterol + caprylate
-
79% activity compared to linoleate
-
-
?
cholesteryl erucate + H2O
cholesterol + erucic acid
-
-
13-docosenoic acid
?
cholesteryl erucate + H2O
cholesterol + erucic acid
-
-
13-docosenoic acid
?
cholesteryl esters + H2O
cholesterol + fatty acid
-
important rate-limiting step in steroidogenesis
-
-
cholesteryl esters + H2O
cholesterol + fatty acid
-
important rate-limiting step in steroidogenesis
-
-
cholesteryl esters + H2O
cholesterol + fatty acid
-
important rate-limiting step in steroidogenesis
-
-
cholesteryl esters + H2O
cholesterol + fatty acid
-
supplies free cholesterol as a precursor for steroidogenesis in steroid-producing tissues
-
-
cholesteryl esters + H2O
cholesterol + fatty acid
-
supplies free cholesterol as a precursor for steroidogenesis in steroid-producing tissues
-
-
cholesteryl esters + H2O
cholesterol + fatty acid
-
involvement in arteriosclerosis
-
-
cholesteryl esters + H2O
cholesterol + fatty acid
-
shows also lipoamidase activity
-
-
cholesteryl esters + H2O
cholesterol + fatty acid
-
acid cholesterol esterase hydrolized only long-chain cholesteryl esters, activity is low for substrate concentration below the critical micelle concentration
-
-
cholesteryl esters + H2O
cholesterol + fatty acid
-
mediating cholesterol absorption through the gastrointestinal tract, digestion and absorption of dietary fats
-
-
cholesteryl esters + H2O
cholesterol + fatty acid
-
important role in fat digestion in infants
-
-
cholesteryl esters + H2O
cholesterol + fatty acid
-
important role in fat digestion in infants
-
r
cholesteryl esters + H2O
cholesterol + fatty acid
-
involvement in arteriosclerosis
-
r
cholesteryl esters + H2O
cholesterol + fatty acid
-
involvement in arteriosclerosis
-
r
cholesteryl esters + H2O
cholesterol + fatty acid
-
important rate-limiting step in steroidogenesis
-
?
cholesteryl esters + H2O
cholesterol + fatty acid
-
long-chain fatty acid cholesterol esters more easily synthesized, synthetic activity highest in chloroform, activity enhanced in degree of unsaturation of fatty acids
-
r
cholesteryl esters + H2O
cholesterol + fatty acid
-
shows also lipoamidase activity
-
-
cholesteryl esters + H2O
cholesterol + fatty acid
-
mediating cholesterol absorption through the gastrointestinal tract, digestion and absorption of dietary fats
-
-
cholesteryl esters + H2O
cholesterol + fatty acid
-
mediating cholesterol absorption through the gastrointestinal tract, digestion and absorption of dietary fats
-
-
cholesteryl esters + H2O
cholesterol + fatty acid
-
involvement in inhibition of spermatogenesis
-
-
cholesteryl esters + H2O
cholesterol + fatty acid
-
involvement in inhibition of spermatogenesis
-
-
cholesteryl esters + H2O
cholesterol + fatty acid
-
fatty acid binding site more hydrophobic than steroid binding site
-
r
cholesteryl esters + H2O
cholesterol + fatty acid
-
important role in fat digestion in infants
-
-
cholesteryl esters + H2O
cholesterol + fatty acid
-
important role in fat digestion in infants
-
-
cholesteryl esters + H2O
cholesterol + fatty acid
-
important role in fat digestion in infants
-
r
cholesteryl esters + H2O
cholesterol + fatty acid
-
involvement in arteriosclerosis
-
-
cholesteryl esters + H2O
cholesterol + fatty acid
-
involvement in arteriosclerosis
-
-
cholesteryl esters + H2O
cholesterol + fatty acid
-
involvement in arteriosclerosis
-
r
cholesteryl esters + H2O
cholesterol + fatty acid
-
involvement in arteriosclerosis
-
r
cholesteryl esters + H2O
cholesterol + fatty acid
-
hydrolytic activity toward liposomal and microcrystallic substrates
-
-
cholesteryl esters + H2O
cholesterol + fatty acid
-
absoprtion of free cholesterol
-
r
cholesteryl esters + H2O
cholesterol + fatty acid
-
fatty acid binding site more hydrophobic than steroid binding site
-
r
cholesteryl esters + H2O
cholesterol + fatty acid
-
important role in fat digestion in infants
-
r
cholesteryl laurate + H2O
cholesterol + laurate
-
41% of the activity with cholesteryl linoleate
-
?
cholesteryl laurate + H2O
cholesterol + laurate
-
35% activity compared to linoleate
-
-
?
cholesteryl linoleate + H2O
cholesterol + linoleate
-
best substrate
-
-
?
cholesteryl linoleate + H2O
cholesterol + linoleate
-
best substrate
-
?
cholesteryl linoleate + H2O
cholesterol + linoleate
-
best substrate
-
?
cholesteryl linoleate + H2O
cholesterol + linoleate
-
-
-
?
cholesteryl linoleate + H2O
cholesterol + linoleate
-
100% activity
-
-
?
cholesteryl linoleate + H2O
cholesterol + linoleic acid
-
most suitable substrate
-
?
cholesteryl linoleate + H2O
cholesterol + linoleic acid
-
synthesis of cholesterol linoleate from polyethylene glycol-modified enzyme only in water-immiscible solvents
-
r
cholesteryl linoleate + H2O
cholesterol + linoleic acid
-
activity lower than with oleate esters
-
r
cholesteryl myristate + H2O
cholesterol + myristate
-
58% of the activity with cholesteryl linoleate
-
?
cholesteryl myristate + H2O
cholesterol + myristate
-
42% activity compared to linoleate
-
-
?
cholesteryl nervonate + H2O
cholesterol + nervonic acid
-
especially for temperature-labile cholesteryl esterase
-
?
cholesteryl oleate
cholesterol + oleate
-
the cholesterol which is incorporated into brush border membrane is not esterified
-
?
cholesteryl oleate
cholesterol + oleate
-
the cholesterol which is incorporated into brush border membrane is not esterified
-
?
cholesteryl oleate + H2O
cholesterol + oleate
-
92% of the activity with cholesteryl linoleate
-
?
cholesteryl oleate + H2O
cholesterol + oleate
-
100% activity, best substrate
-
-
?
cholesteryl oleate + H2O
cholesterol + oleate
-
21% activity compared to linoleate
-
-
?
cholesteryl oleate + H2O
cholesterol + oleate
-
21% activity compared to linoleate
-
-
?
cholesteryl palmitate + H2O
cholesterol + palmitate
-
75% of the activity with cholesteryl linoleate
-
?
cholesteryl palmitate + H2O
cholesterol + palmitate
-
-
-
?
cholesteryl palmitate + H2O
cholesterol + palmitate
-
about 50% activity compared to cholesteryl oleate
-
-
?
cholesteryl palmitate + H2O
cholesterol + palmitate
-
38% activity compared to linoleate
-
-
?
cholesteryl palmitate + H2O
cholesterol + palmitate
-
38% activity compared to linoleate
-
-
?
cholesteryl palmitate + H2O
cholesterol + palmitic acid
-
low activity
-
?
cholesteryl stearate + H2O
cholesterol + stearate
-
80% of the activity with cholesteryl linoleate
-
?
cholesteryl stearate + H2O
cholesterol + stearate
-
about 45% activity compared to cholesteryl oleate
-
-
?
cholesteryl stearate + H2O
cholesterol + stearate
-
18% activity compared to linoleate
-
-
?
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
5% of the activity with cholesteryl linoleate
-
-
?
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
5% of the activity with cholesteryl linoleate
-
-
?
p-nitrophenyl hexanoate + H2O
p-nitrophenol + hexanoic acid
53% of the activity with cholesteryl linoleate
-
-
?
p-nitrophenyl myristate + H2O
p-nitrophenol + myristic acid
100% of the activity with cholesteryl linoleate
-
-
?
p-nitrophenyl octanoate + H2O
p-nitrophenol + octanoic acid
79% of the activity with cholesteryl linoleate
-
-
?
p-nitrophenyl palmitate + H2O
p-nitrophenol + palmitic acid
68% of the activity with cholesteryl linoleate
-
-
?
triolein + H2O
diolein + oleate
-
positional specificity for sn-2-position, lower affinity for the sn-1- and sn-3-position
-
?
additional information
?
-
-
rank of the relative rates of hydrolysis by Acinetobacter sp. strain CHE4-1 enzyme are linoleate > oleate > acetate > palmitate > butyrate > laurate > caproate
-
-
-
additional information
?
-
-
rank of the relative rates of hydrolysis by Acinetobacter sp. strain CHE4-1 enzyme are linoleate > oleate > acetate > palmitate > butyrate > laurate > caproate
-
-
-
additional information
?
-
-
enzyme is involved in fatty acid catabolism
-
?
additional information
?
-
-
the enzyme accelerates the incorporation of cholesterol into human adenocarcinomal Caco-2 cells, which is not influenced by addition of exogenous oleic acid, the enzyme also significantly increases the incorporation of cholesterol into the intestinal brush border membranes of rat
-
?
additional information
?
-
-
enzyme catalyzes cleavage of fatty acid residues in both the sn-1 and sn-2 positions of phospholipids
-
-
-
additional information
?
-
-
CRL1 slowly hydrolyzes 6-chloro-2-pyrones
-
?
additional information
?
-
-
enzyme prefers substrates of long-chain fatty acids and unsaturated fatty acids
-
?
additional information
?
-
-
in aqueous dispersion, reaction proceeds slowly. Addition of surfactant Thesit accelerates initial reaction rate
-
-
-
additional information
?
-
-
the enzyme accelerates the incorporation of cholesterol into human adenocarcinomal Caco-2 cells, which is not influenced by addition of exogenous oleic acid
-
?
additional information
?
-
-
neutral lipid metabolism in macrophages contributes to organ inflammation and pathogenesis
-
-
-
additional information
?
-
-
neutral cholesterol ester hydrolase is not a target of protein kinase A
-
-
-
additional information
?
-
-
no activity with triacetin, enzyme activity increases with increasing chain lebgth and number of double bonds, no interfacial activation
-
?
additional information
?
-
-
the enzyme does not hydrolyze bis(2-ethylhexyl) phthalate, diethyl phthalate, di-n-propyl phthalate, di-n-butyl phthalate, di-n-pentyl phthalate, di-n-hexyl phthalate, n-butyl benzyl phthalate and dicyclohexyl phthalate
-
-
-
additional information
?
-
-
the enzyme within the pancreatic juice significantly increased the incorporation of cholesterol into the intestinal brush border membranes of rat
-
?
additional information
?
-
-
the enzyme is also active on fatty acid esters of methanol and 4-nitrophenol
-
-
-
additional information
?
-
-
the enzyme catalyzes reactions between cholesterol and methyl oleate/triolein. The degree of esterification of cholesterol with methyl oleate is 31% at the most after 19 h. The use of triolein as acyl donor results in lower esterification
-
-
-
additional information
?
-
-
the hydrolytic activity of the enzyme increases from cholesterol acetate to caproate, then decreases sharply from caproate to caprate, with a further gradual decrease through stearate. In esterification there is virtually no activity with short-chain free fatty acids from acetate through caproate, a marked increase with caprylate, and a constant level from caprylate through stearate
-
-
-
additional information
?
-
-
the enzyme catalyzes reactions between cholesterol and methyl oleate/triolein. The degree of esterification of cholesterol with methyl oleate is 31% at the most after 19 h. The use of triolein as acyl donor results in lower esterification
-
-
-
additional information
?
-
-
the hydrolytic activity of the enzyme increases from cholesterol acetate to caproate, then decreases sharply from caproate to caprate, with a further gradual decrease through stearate. In esterification there is virtually no activity with short-chain free fatty acids from acetate through caproate, a marked increase with caprylate, and a constant level from caprylate through stearate
-
-
-
additional information
?
-
-
the enzyme is also active on fatty acid esters of methanol and 4-nitrophenol
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
cholesteryl esters + H2O
cholesterol + fatty acid
-
important rate-limiting step in steroidogenesis
-
-
cholesteryl esters + H2O
cholesterol + fatty acid
-
important rate-limiting step in steroidogenesis
-
-
cholesteryl esters + H2O
cholesterol + fatty acid
-
important rate-limiting step in steroidogenesis
-
-
cholesteryl esters + H2O
cholesterol + fatty acid
-
supplies free cholesterol as a precursor for steroidogenesis in steroid-producing tissues
-
-
cholesteryl esters + H2O
cholesterol + fatty acid
-
supplies free cholesterol as a precursor for steroidogenesis in steroid-producing tissues
-
-
cholesteryl esters + H2O
cholesterol + fatty acid
-
involvement in arteriosclerosis
-
-
cholesteryl esters + H2O
cholesterol + fatty acid
-
shows also lipoamidase activity
-
-
cholesteryl esters + H2O
cholesterol + fatty acid
-
acid cholesterol esterase hydrolized only long-chain cholesteryl esters, activity is low for substrate concentration below the critical micelle concentration
-
-
cholesteryl esters + H2O
cholesterol + fatty acid
-
mediating cholesterol absorption through the gastrointestinal tract, digestion and absorption of dietary fats
-
-
cholesteryl esters + H2O
cholesterol + fatty acid
-
important role in fat digestion in infants
-
-
cholesteryl esters + H2O
cholesterol + fatty acid
-
important role in fat digestion in infants
-
r
cholesteryl esters + H2O
cholesterol + fatty acid
-
involvement in arteriosclerosis
-
r
cholesteryl esters + H2O
cholesterol + fatty acid
-
involvement in arteriosclerosis
-
r
cholesteryl esters + H2O
cholesterol + fatty acid
-
important rate-limiting step in steroidogenesis
-
?
cholesteryl esters + H2O
cholesterol + fatty acid
-
long-chain fatty acid cholesterol esters more easily synthesized, synthetic activity highest in chloroform, activity enhanced in degree of unsaturation of fatty acids
-
r
cholesteryl esters + H2O
cholesterol + fatty acid
-
shows also lipoamidase activity
-
-
cholesteryl esters + H2O
cholesterol + fatty acid
-
mediating cholesterol absorption through the gastrointestinal tract, digestion and absorption of dietary fats
-
-
cholesteryl esters + H2O
cholesterol + fatty acid
-
mediating cholesterol absorption through the gastrointestinal tract, digestion and absorption of dietary fats
-
-
cholesteryl esters + H2O
cholesterol + fatty acid
-
involvement in inhibition of spermatogenesis
-
-
cholesteryl esters + H2O
cholesterol + fatty acid
-
involvement in inhibition of spermatogenesis
-
-
cholesteryl esters + H2O
cholesterol + fatty acid
-
fatty acid binding site more hydrophobic than steroid binding site
-
r
cholesteryl esters + H2O
cholesterol + fatty acid
-
important role in fat digestion in infants
-
-
cholesteryl esters + H2O
cholesterol + fatty acid
-
important role in fat digestion in infants
-
-
cholesteryl esters + H2O
cholesterol + fatty acid
-
important role in fat digestion in infants
-
r
cholesteryl esters + H2O
cholesterol + fatty acid
-
involvement in arteriosclerosis
-
-
cholesteryl esters + H2O
cholesterol + fatty acid
-
involvement in arteriosclerosis
-
-
cholesteryl esters + H2O
cholesterol + fatty acid
-
involvement in arteriosclerosis
-
r
cholesteryl esters + H2O
cholesterol + fatty acid
-
involvement in arteriosclerosis
-
r
cholesteryl esters + H2O
cholesterol + fatty acid
-
hydrolytic activity toward liposomal and microcrystallic substrates
-
-
cholesteryl esters + H2O
cholesterol + fatty acid
-
absoprtion of free cholesterol
-
r
cholesteryl esters + H2O
cholesterol + fatty acid
-
fatty acid binding site more hydrophobic than steroid binding site
-
r
cholesteryl esters + H2O
cholesterol + fatty acid
-
important role in fat digestion in infants
-
r
cholesteryl oleate
cholesterol + oleate
-
the cholesterol which is incorporated into brush border membrane is not esterified
-
?
cholesteryl oleate
cholesterol + oleate
-
the cholesterol which is incorporated into brush border membrane is not esterified
-
?
additional information
?
-
-
enzyme is involved in fatty acid catabolism
-
?
additional information
?
-
-
the enzyme accelerates the incorporation of cholesterol into human adenocarcinomal Caco-2 cells, which is not influenced by addition of exogenous oleic acid, the enzyme also significantly increases the incorporation of cholesterol into the intestinal brush border membranes of rat
-
?
additional information
?
-
-
the enzyme accelerates the incorporation of cholesterol into human adenocarcinomal Caco-2 cells, which is not influenced by addition of exogenous oleic acid
-
?
additional information
?
-
-
neutral lipid metabolism in macrophages contributes to organ inflammation and pathogenesis
-
-
-
additional information
?
-
-
the enzyme within the pancreatic juice significantly increased the incorporation of cholesterol into the intestinal brush border membranes of rat
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cAMP
-
activation only for neutral CEase; as cofactor for cAMP-dependent protein kinase
MgATP2-
-
activation only for neutral CEase; increasing activity with addition of cAMP-dependend protein kinase
MgATP2-
-
increasing activity with addition of cAMP-dependend protein kinase
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Cu2+
Mg2+
additional information
Mg2+
-
activation in a reaction mixture containing cAMP, protein kinase A and ATP
additional information
-
divalent metal ions do not influence the enzyme activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(R)-exo-2-norbornyl-N-n-butylcarbamate
-
the R-enantiomer is 6.8times more potent than the S-enantiomer
(S)-endo-2-norbornyl-N-n-butyl-carbamate
-
the S-enantiomer is 4.6times more potent than the R-enantiomer
2-(5,6,7,8)-tetrahydronaphthyl-N-hexyl carbamate
-
biphasic inhibition time-course
2-(diethylamino)-5,6,7,8-tetrahydro-4H-[1]benzothieno[2,3-d][1,3]oxazin-4-one
-
substrate inhibitor
2-(diethylamino)-5-methyl-5,6,7,8-tetrahydro-4H-(1)benzothieno(2,3-d)(1,3)oxazin-4-one
-
-
2-(diethylamino)-6,7,8,9-tetrahydro-4H,5H-cyclohepta(4,5)thieno(2,3-d)(1,3)oxazin-4-one
-
-
2-(diethylamino)-6,7-dihydro-4H,5H-cyclopenta(4,5)thieno(2,3-d)(1,3)oxazin-4-one
-
i.e. DO-3, significant inhibition of cleavage of cholesteryl esters in high density lipoproteins
2-(diethylamino)-6,7-dihydro-4H,5H-cyclopenta[4,5]thieno[2,3-d][1,3]oxazin-4-one
-
substrate inhibitor
2-(diethylamino)-6,7-dihydro-4H,5H-cyclopenta[4,5]thieno[2,3-d][1,3]thiazin-4-one
-
substrate inhibitor
2-(dimethylamino)-1,2,5,6,7,8-hexahydro-4H-(1)benzothieno(2,3-d)(1,3)oxazin-4-one
-
-
2-(dimethylamino)-1,5,6,7-tetrahydro-2H,4H-cyclopenta(4,5)thieno(2,3-d)(1,3)oxazin-4-one
-
-
2-(dimethylamino)-1,5,6,8-tetrahydro-2H,4H-thiopyrano(4',3':4,5)thieno(2,3-d)(1,3)oxazin-4-one
-
-
2-[3,4-bis[(diethoxyphosphinyl)oxy]phenyl]-4-oxo-4H-1-benzopyran-3,5,7-triyl phosphoric acid hexaethyl ester
-
-
2-[3,4-bis[(diethoxyphosphinyl)oxy]phenyl]-5-hydroxy-4-oxo-4H-1-benzopyran-3,7-diyl phosphoric acid tetraethyl ester
-
-
2-[3,4-bis[(diethoxyphosphoryl)oxy]phenyl]-4-oxo-4H-chromene-5,7-diyl tetraethyl bis(phosphate)
-
-
2-[3-[(diethoxyphosphinyl)oxy]-4-methoxy-phenyl]-4-oxo-4H-1-benzopyran-5,7-diyl phosphoric acid tetraethyl ester
-
-
2-[4-[(diethoxyphosphoryl)oxy]phenyl]-4-oxo-4H-chromene-5,7-diyl tetraethyl bis(phosphate)
-
-
2-[7-chloro-1-ethoxy-3-(4-ethylphenyl)-1-oxido-1H-2,1-benzoxaphosphinin-4-yl]-1-phenylethanone
-
-
2-[[4-(diethoxyphosphinyl)oxy]phenyl]-5-hydroxy-4-oxo-4H-1-benzopyran-7-yl phosphoric acid diethyl ester
-
-
3,3'-[4-([2-[(4-chlorophenyl)carbonyl]hydrazinyl]sulfonyl)-1,2-oxazole-3,5-diyl]bis(N-hydroxypropanamide)
-
-
3-[[4-(diethoxyphosphinyl)oxy]phenyl]-4-oxo-4H-1-benzopyran-5,7-diyl phosphoric acid tetraethyl ester
-
-
3-[[4-(diethoxyphosphinyl)oxy]phenyl]-4-oxo-4H-1-benzopyran-7-yl phosphoric acid diethyl ester
-
-
3-[[4-(diethoxyphosphinyl)oxy]phenyl]-5-hydroxy-4-oxo-4H-1-benzopyran-7-yl phosphoric acid diethyl ester
-
-
4-bromo-7-chloro-1-ethoxy-3-(4-methoxyphenyl)-1H-2,1-benzoxaphosphinine 1-oxide
-
-
4-nitrophenyl-N-allyl carbamate
-
mechanism of inhibition by these pseudo-substrate inhibitors, via a 2-step reaction including the formation of a tetrahedral enzyme-inhibitor adduct and the formation of the carbamyl-enzyme, inhibition kinetics
4-nitrophenyl-N-butyl carbamate
-
mechanism of inhibition by these pseudo-substrate inhibitors, via a 2-step reaction including the formation of a tetrahedral enzyme-inhibitor adduct and the formation of the carbamyl-enzyme, inhibition kinetics
4-nitrophenyl-N-chloroethyl carbamate
-
mechanism of inhibition by these pseudo-substrate inhibitors, via a 2-step reaction including the formation of a tetrahedral enzyme-inhibitor adduct and the formation of the carbamyl-enzyme, inhibition kinetics
4-nitrophenyl-N-hexyl carbamate
-
mechanism of inhibition by these pseudo-substrate inhibitors, via a 2-step reaction including the formation of a tetrahedral enzyme-inhibitor adduct and the formation of the carbamyl-enzyme, inhibition kinetics
4-nitrophenyl-N-methylphenyl carbamate
-
mechanism of inhibition by these pseudo-substrate inhibitors, via a 2-step reaction including the formation of a tetrahedral enzyme-inhibitor adduct and the formation of the carbamyl-enzyme, inhibition kinetics
4-nitrophenyl-N-octyl carbamate
-
mechanism of inhibition by these pseudo-substrate inhibitors, via a 2-step reaction including the formation of a tetrahedral enzyme-inhibitor adduct and the formation of the carbamyl-enzyme, inhibition kinetics
5-hydroxy-4-oxo-2-phenyl-4H-1-benzopyran-6,7-diyl phosphoric acid tetraethyl ester
-
-
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-(1-ethyl-2-cyclohexyl)-2-pyrone
-
selective, potent, and reversible inhibitor, not toxic in vivo, enzyme inhibition effectively reduces cholesterol uptake in vivo
7-chloro-1-ethoxy-3-(4-ethylphenyl)-4-(phenylethynyl)-1H-2,1-benzoxaphosphinine 1-oxide
-
-
7-chloro-1-ethoxy-4-iodo-3-(4-methoxyphenyl)-1H-2,1-benzoxaphosphinine 1-oxide
-
-
albumin
-
50% inhibition by addition of 0.015-0.045 mg, increasing inhibition after heat treatment of albumin
-
amlodipine
-
mixed-type, study on kinetics in presence of Triton X-100 or taurocholate
AS115
nonspecific inhibitor, the enzyme is about 85% inhibited by 0.01 mM AS115
besylate
-
mixed-type, study on kinetics in presence of Triton X-100 or taurocholate
bisphenol A dimethacrylate
-
computational study on inhibitory effect. Bisphenol A dimethacrylate mimics chemical properties of reported enzyme inhibitors, particularly concerning maximum oxygen valency and molecular shape/size
brefeldin A
-
inhibition to 80%-90% of secreted enzyme into the medium of HepG2 cells
cardiolipin
-
inhibitory if included as aqueous sonicated dispersions at 2.5 mg/ml
cholesteryl esters
-
inhibition at 0.2 mM with cholesteryl-stearate, -oleate, -eicosenoate, -arachidonate, -erucate and -nervonate
heparin
-
50% inhibition for CEase-ISF II at 0.025 mM, no inhibition for CEase-IF I
hydralazine hydrochloride
-
mixed-type, study on kinetics in presence of Triton X-100 or taurocholate
lovastatin
-
mixed-type, study on kinetics in presence of Triton X-100 or taurocholate
methyl 3-[(2-ethoxy-2-oxoethyl)(methyl)sulfamoyl]-5-[2-(1H-pyrrol-2-yl)ethyl]thiophene-2-carboxylate
-
-
monensin
-
inhibition to 50%-60% of secreted enzyme into the medium of HepG2 cells
nifedipine
-
mixed-type, study on kinetics in presence of Triton X-100 or taurocholate
phosphatidylinositol
-
inhibitory if included as aqueous sonicated dispersions at 2.5 mg/ml