2.3.1.26: sterol O-acyltransferase
This is an abbreviated version!
For detailed information about sterol O-acyltransferase, go to the full flat file.
Word Map on EC 2.3.1.26
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2.3.1.26
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keratinocytes
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lipoprotein
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immortalize
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tnf
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dermal
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esterification
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psoriasis
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esterify
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erk
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mapks
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chemokine
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collagen
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atopic
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uvb-induced
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nanoparticles
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atherosclerosis
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keratin
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cosmetic
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dermatitis
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caspase-3
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drug development
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radiation-induced
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photoaging
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macrophage-derived
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cox-2
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filaggrin
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7alpha-hydroxylase
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hairless
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sunscreen
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nutrition
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scratch
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pharmacology
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sunburn
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antiatherosclerotic
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phototoxicity
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hypocholesterolemic
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foam
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hmg-coa
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photoprotective
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desmogleins
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dermatology
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keratinocyte-derived
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ad-like
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suprabasal
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medicine
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cholesterol-fed
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hyperproliferation
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transdermal
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mmp-1
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analysis
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imiquimod
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uvb-irradiated
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involucrin
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cyclobutane
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re-epithelialization
- 2.3.1.26
- keratinocytes
- lipoprotein
-
immortalize
- tnf
- dermal
- esterification
- psoriasis
-
esterify
- erk
- mapks
- chemokine
- collagen
-
atopic
-
uvb-induced
- nanoparticles
- atherosclerosis
- keratin
-
cosmetic
- dermatitis
- caspase-3
- drug development
-
radiation-induced
-
photoaging
-
macrophage-derived
- cox-2
- filaggrin
-
7alpha-hydroxylase
- hairless
-
sunscreen
- nutrition
-
scratch
- pharmacology
- sunburn
-
antiatherosclerotic
- phototoxicity
-
hypocholesterolemic
-
foam
- hmg-coa
-
photoprotective
-
desmogleins
-
dermatology
-
keratinocyte-derived
-
ad-like
-
suprabasal
- medicine
-
cholesterol-fed
-
hyperproliferation
-
transdermal
- mmp-1
- analysis
- imiquimod
-
uvb-irradiated
- involucrin
-
cyclobutane
-
re-epithelialization
Reaction
Synonyms
A2, ACAT, ACAT-1, ACAT-2, ACAT1, ACAT2, acyl coenzyme A-cholesterol-O-acyltransferase, acyl coenzyme A: cholesteryl acyltransferase, acyl-CoA cholesterol acyltransferase, acyl-CoA cholesterol O-acyltransferase, acyl-CoA: cholesterol acyltransferase, acyl-CoA:cholesterol acyltransferase, acyl-CoA:cholesterol acyltransferase 1, acyl-CoA:cholesterol acyltransferase 2, acyl-coA:cholesterol o-acyl transferase 2, acyl-coenzyme A: cholesterol acyltransferase, acyl-coenzyme A:cholesterol acyltransferase, acyl-coenzyme A:cholesterol acyltransferase 1, acyl-coenzyme A:cholesterol acyltransferase 2, acyl-coenzyme A:cholesterol acyltransferase-1, acyl-coenzyme A:cholesterol O-acyltransferase, acyl-coenzymeA cholesterol acyltransferase, acyl-coenzymeA:cholesterol acyl-transferase, acylcoenzyme A:cholesterol O-acyltransferase, acyltransferase, cholesterol, AsAT, cholesterol acyltransferase, cholesterol acyltransferase 2, cholesterol ester synthase, cholesterol ester synthetase, cholesteryl ester synthetase, hACAT, hACAT-1, hACAT-2, hACAT1, SOAT, SOAT!, Soat1, Soat2, sterol O-acyltransferase 2, sterol-ester synthase, sterol-ester synthetase, steroyl O-acyltransferase 1, steroyl O-acyltransferase 2
ECTree
2.3.1.26 sterol O-acyltransferaseAdvanced search results
results (
results (Activating Compound
Activating Compound on EC 2.3.1.26 - sterol O-acyltransferase
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ACTIVATING COMPOUND 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
6-ketocholestanol
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added at high concentration causes modest increase in enzyme activity
7-ketocholesterol
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added at high concentration causes modest increase in enzyme activity
liver fatty acid binding protein/bovine serum albumin
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small increase in activity
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Mevalonolactone
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intragastric administration, increasing sterol biosynthesis and increasing enzyme activity
25-hydroxycholesterol
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stimulates enzyme activity in liver microsomes in vitro with half-maximal stimulation at 0.0168 mM oxysterol. A major part of the activation of microsomal enzyme is not ascribable to increased substrate availability for the enzyme
albumin
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required in the assay medium to prevent the high concentration of oleoly-CoA from inhibiting the enzyme presumably by disrupting the microsomal membrane
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cholesterol
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day 40 samples, exogenous, added as phosphatidylcholine liposomes, concentration-dependent increase in activity
cholesterol
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exogenous cholesterol in the liposomes is absolutely necessary for activity of the reconstituted enzyme
cholesterol
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addition of cholesterol to frozen microsomes prepared from unfrozen liver tissue increases the enzyme activity
cholesterol
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serves as an enzyme activator in vitro, in addition to its role as an enzyme substrate
cholesterol
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exogenous cholesterol in the liposomes is absolutely necessary for activity of the reconstituted enzyme
cholesterol
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addition of cholesterol to microsomes prepared from frozen liver tissue does not further increase the enzyme activity
cholesterol
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presence of cholesterol stimulates reaction of ACAT1 with sitosterol up to 3fold, reaction of ACAT2 is only moderately activated
cholesterol
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significant activation of reaction with 7-ketocholesterol as substrate, decrease in Hill coefficient from 3.0 without cholesterol to 1.1 with cholesterol
cholesterol
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exogenous, added as phosphatidylcholine liposome or in acetone solution, stimulates
cholesterol
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exogenous, delivered as a Triton WR-1339 detergent dispersion, increases activity
cholesterol
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exogenous, 25% increase of adrenal microsome activity and 2fold increase of activity in liver
additional information
enzyme ACAT1 can be activated by a variety of sterols. All sterols that possess the iso-octyl side chain including cholesterol, oxysterols, various plant sterols can all be activators of ACAT. Pregnenolone can only be an ACAT substrate because it lacks the iso-octyl side chain required to be an ACAT activator. The unnatural cholesterol analogs epi-cholesterol (with 3-alpha OH in steroid ring B) and ent-cholesterol (the mirror image of cholesterol) contain the iso-octyl side chain but do not have the 3-beta OH at C-3. Thus, they can only serve as activators and cannot serve as substrates
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additional information
enzyme ACAT1 can be activated by a variety of sterols. All sterols that possess the iso-octyl side chain including cholesterol, oxysterols, various plant sterols can all be activators of ACAT. Pregnenolone can only be an ACAT substrate because it lacks the iso-octyl side chain required to be an ACAT activator. The unnatural cholesterol analogs epi-cholesterol (with 3-alpha OH in steroid ring B) and ent-cholesterol (the mirror image of cholesterol) contain the iso-octyl side chain but do not have the 3-beta OH at C-3. Thus, they can only serve as activators and cannot serve as substrates
-
additional information
-
enzyme ACAT1 can be activated by a variety of sterols. All sterols that possess the iso-octyl side chain including cholesterol, oxysterols, various plant sterols can all be activators of ACAT. Pregnenolone can only be an ACAT substrate because it lacks the iso-octyl side chain required to be an ACAT activator. The unnatural cholesterol analogs epi-cholesterol (with 3-alpha OH in steroid ring B) and ent-cholesterol (the mirror image of cholesterol) contain the iso-octyl side chain but do not have the 3-beta OH at C-3. Thus, they can only serve as activators and cannot serve as substrates
-
additional information
enzyme ACAT1 can be activated by a variety of sterols. All sterols that possess the iso-octyl side chain including cholesterol, oxysterols, various plant sterols can all be activators of ACAT. Pregnenolone can only be an ACAT substrate because it lacks the iso-octyl side chain required to be an ACAT activator. The unnatural cholesterol analogs epi-cholesterol (with 3-alpha OH in steroid ring B) and ent-cholesterol (the mirror image of cholesterol) contain the iso-octyl side chain but do not have the 3-beta OH at C-3. Thus, they can only serve as activators and cannot serve as substrates. When pregnenolone and cholesterol (or other sterol analogues) are both present, binding of cholesterol at site A causes conformational changes, enabling the enzyme to increase the rate of esterification reaction much more efficiently
-
additional information
enzyme ACAT1 can be activated by a variety of sterols. All sterols that possess the iso-octyl side chain including cholesterol, oxysterols, various plant sterols can all be activators of ACAT. Pregnenolone can only be an ACAT substrate because it lacks the iso-octyl side chain required to be an ACAT activator. The unnatural cholesterol analogs epi-cholesterol (with 3-alpha OH in steroid ring B) and ent-cholesterol (the mirror image of cholesterol) contain the iso-octyl side chain but do not have the 3-beta OH at C-3. Thus, they can only serve as activators and cannot serve as substrates. When pregnenolone and cholesterol (or other sterol analogues) are both present, binding of cholesterol at site A causes conformational changes, enabling the enzyme to increase the rate of esterification reaction much more efficiently
-
additional information
-
enzyme ACAT1 can be activated by a variety of sterols. All sterols that possess the iso-octyl side chain including cholesterol, oxysterols, various plant sterols can all be activators of ACAT. Pregnenolone can only be an ACAT substrate because it lacks the iso-octyl side chain required to be an ACAT activator. The unnatural cholesterol analogs epi-cholesterol (with 3-alpha OH in steroid ring B) and ent-cholesterol (the mirror image of cholesterol) contain the iso-octyl side chain but do not have the 3-beta OH at C-3. Thus, they can only serve as activators and cannot serve as substrates. When pregnenolone and cholesterol (or other sterol analogues) are both present, binding of cholesterol at site A causes conformational changes, enabling the enzyme to increase the rate of esterification reaction much more efficiently
-
additional information
enzyme ACAT1 can be activated by a variety of sterols. All sterols that possess the iso-octyl side chain including cholesterol, oxysterols, various plant sterols can all be activators of ACAT. Pregnenolone can only be an ACAT substrate because it lacks the iso-octyl side chain required to be an ACAT activator. The unnatural cholesterol analogs epi-cholesterol (with 3-alpha OH in steroid ring B) and ent-cholesterol (the mirror image of cholesterol) contain the iso-octyl side chain but do not have the 3-beta OH at C-3. Thus, they can only serve as activators and cannot serve as substrates
-
additional information
enzyme ACAT1 can be activated by a variety of sterols. All sterols that possess the iso-octyl side chain including cholesterol, oxysterols, various plant sterols can all be activators of ACAT. Pregnenolone can only be an ACAT substrate because it lacks the iso-octyl side chain required to be an ACAT activator. The unnatural cholesterol analogs epi-cholesterol (with 3-alpha OH in steroid ring B) and ent-cholesterol (the mirror image of cholesterol) contain the iso-octyl side chain but do not have the 3-beta OH at C-3. Thus, they can only serve as activators and cannot serve as substrates
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