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
-
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
- 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 (Substrates Products
Substrates Products on EC 2.3.1.26 - sterol O-acyltransferase
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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
acetyl-CoA + cholesterol
CoA + cholesteryl acetate
-
16% of the activity with oleoyl-CoA
-
?
acyl-CoA + 24(S)-hydroxycholesterol
CoA + acyl (24S)-24-hydroxycholesterol
-
-
-
?
docosahexaenoyl-CoA + cholesterol
CoA + cholesteryl docosahexaenoate
-
rate of cholesteryl ester formation is faster and more cholesteryl ester is formed with oleic acid compared to docosahexanoic acid. Docosahexanoic acid substantially reduces cholesteryl ester formation when given in combination with oleic acid
-
-
?
lauroyl-CoA + cholesterol
CoA + cholesteryl laurate
-
62% of the activity with oleoyl-CoA
-
?
myristoyl-CoA + cholesterol
CoA + cholesteryl myristate
-
37% of the activity with oleoyl-CoA
-
?
oleoyl-CoA + 4alpha-methylcholest-7-en-3beta-ol
CoA + (3beta,4alpha)-4-methylcholest-7-en-3-yl (9Z)-octadec-9-enoate
-
-
-
?
oleoyl-CoA + 5alpha,6alpha-epoxycholesterol
CoA + 5alpha,6alpha-epoxycholesteryl oleate
-
activity comparable to cholesterol
-
-
?
oleoyl-CoA + 5alpha-cholest-8(14)-en-3beta-ol-15-one
CoA + 15-oxo-5alpha-cholest-8(14)-en-3beta-yl (9Z)-octadec-9-enoate
oleoyl-CoA + 5alpha-cholest-8(14)-en-3beta-ol-15-one
CoA + oleate ester of 5alpha-cholest-8(14)-en-3beta-ol-15-one
oleoyl-CoA + 7alpha-hydroxycholesterol
CoA + 7alpha-hydroxycholesteryl oleate
-
activity comparable to cholesterol
-
-
?
oleoyl-CoA + episterol
CoA + episteryl oleate
-
62% of the activity with cholesterol
-
?
oleoyl-CoA + fecosterol
CoA + fecosteryl oleate
-
48% of the activity with cholesterol
-
?
oleoyl-CoA + lanosterol
CoA + lanosteryl oleate
-
65% of the activity with cholesterol
-
?
oleoyl-CoA + zymosterol
CoA + zymosteryl oleate
-
93% of the activity with cholesterol
-
?
palmitoleoyl-CoA + cholesterol
CoA + cholesteryl palmitoleate
-
91% of the activity with oleoyl-CoA
-
?
acyl-CoA + cholesterol
CoA + cholesterol ester
-
-
684773, 684780, 684786, 684799, 684800, 684882, 685566, 685611, 685899, 686600, 688060, 688139, 688767, 689426, 736937
-
-
?
acyl-CoA + cholesterol
CoA + cholesterol ester
ACAT-1 plays an important role in the formation of macrophage-derived foam cells in atherosclerotic lesions
-
-
?
acyl-CoA + cholesterol
CoA + cholesterol ester
cholesterol is the preferred acceptor substrate
-
-
?
acyl-CoA + cholesterol
CoA + cholesterol ester
cholesterol is the preferred acceptor substrate, and for ACAT1, the preferred fatty acyl-CoA is oleoyl coenzyme A
-
-
?
acyl-CoA + cholesterol
CoA + cholesterol ester
cholesterol is the preferred acceptor substrate
-
-
?
acyl-CoA + cholesterol
CoA + cholesterol ester
cholesterol is the preferred acceptor substrate, and for ACAT1, the preferred fatty acyl-CoA is oleoyl coenzyme A
-
-
?
acyl-CoA + cholesterol
CoA + cholesterol ester
-
-
-
-
?
acyl-CoA + cholesterol
CoA + cholesterol ester
-
-
esterification of 3beta-hydroxy group
?
acyl-CoA + cholesterol
CoA + cholesterol ester
-
acyl-CoA derivatives can be replaced by ATP, Mg2+, CoA and fatty acids, in-situ production of acyl-CoA
-
?
acyl-CoA + cholesterol
CoA + cholesterol ester
-
the animal enzyme is highly specific for transfer of acyl groups with a single cis-double-bond 9 carbon atoms distant from the carboxyl group
-
?
acyl-CoA + cholesterol
CoA + cholesterol ester
-
-
-
?
acyl-CoA + cholesterol
CoA + cholesterol ester
-
-
-
?
acyl-CoA + cholesterol
CoA + cholesterol ester
-
acyl-CoA derivatives can be replaced by ATP, Mg2+, CoA and fatty acids, in-situ production of acyl-CoA
-
?
long-chain fatty acyl-CoA + cholesterol
CoA + cholesteryl long-chain fatty acyl ester
-
-
-
?
long-chain fatty acyl-CoA + cholesterol
CoA + cholesteryl long-chain fatty acyl ester
-
may play an important role in regulation of the accumulation of cholesterol esters within smooth muscle cells of the artery wall during atherogenesis and in synthesis of cholesterol esters during hepatic very low-density lipoprotein synthesis and secretion
-
?
long-chain fatty acyl-CoA + cholesterol
CoA + cholesteryl long-chain fatty acyl ester
-
responsible for cellular synthesis of cholesterol esters in various cell types
-
?
long-chain fatty acyl-CoA + cholesterol
CoA + cholesteryl long-chain fatty acyl ester
-
-
-
?
long-chain fatty acyl-CoA + cholesterol
CoA + cholesteryl long-chain fatty acyl ester
-
may play an important role in regulation of the accumulation of cholesterol esters within smooth muscle cells of the artery wall during atherogenesis and in synthesis of cholesterol esters during hepatic very low-density lipoprotein synthesis and secretion
-
?
long-chain fatty acyl-CoA + cholesterol
CoA + cholesteryl long-chain fatty acyl ester
-
responsible for cellular synthesis of cholesterol esters in various cell types
-
?
long-chain fatty acyl-CoA + cholesterol
CoA + cholesteryl long-chain fatty acyl ester
-
-
-
?
long-chain fatty acyl-CoA + cholesterol
CoA + cholesteryl long-chain fatty acyl ester
-
may play an important role in regulation of the accumulation of cholesterol esters within smooth muscle cells of the artery wall during atherogenesis and in synthesis of cholesterol esters during hepatic very low-density lipoprotein synthesis and secretion
-
?
long-chain fatty acyl-CoA + cholesterol
CoA + cholesteryl long-chain fatty acyl ester
-
responsible for cellular synthesis of cholesterol esters in various cell types
-
?
long-chain fatty acyl-CoA + cholesterol
CoA + cholesteryl long-chain fatty acyl ester
-
-
-
?
long-chain fatty acyl-CoA + cholesterol
CoA + cholesteryl long-chain fatty acyl ester
-
may play an important role in regulation of the accumulation of cholesterol esters within smooth muscle cells of the artery wall during atherogenesis and in synthesis of cholesterol esters during hepatic very low-density lipoprotein synthesis and secretion
-
?
long-chain fatty acyl-CoA + cholesterol
CoA + cholesteryl long-chain fatty acyl ester
-
responsible for cellular synthesis of cholesterol esters in various cell types
-
?
long-chain fatty acyl-CoA + cholesterol
CoA + cholesteryl long-chain fatty acyl ester
-
the enzyme is relevant for cellular cholesterol esterification in vivo, the regulation in human mononuclear phagocytes indicates that the enzyme is also involved in foam cell formation during early atherogenesis
-
?
long-chain fatty acyl-CoA + cholesterol
CoA + cholesteryl long-chain fatty acyl ester
-
the high activity of intestinal enzyme renders it possible that the enzyme plays a role in cholesterol absorption
-
?
long-chain fatty acyl-CoA + cholesterol
CoA + cholesteryl long-chain fatty acyl ester
-
-
-
?
long-chain fatty acyl-CoA + cholesterol
CoA + cholesteryl long-chain fatty acyl ester
-
may play an important role in regulation of the accumulation of cholesterol esters within smooth muscle cells of the artery wall during atherogenesis and in synthesis of cholesterol esters during hepatic very low-density lipoprotein synthesis and secretion
-
?
long-chain fatty acyl-CoA + cholesterol
CoA + cholesteryl long-chain fatty acyl ester
-
responsible for cellular synthesis of cholesterol esters in various cell types
-
?
long-chain fatty acyl-CoA + cholesterol
CoA + cholesteryl long-chain fatty acyl ester
-
-
-
?
long-chain fatty acyl-CoA + cholesterol
CoA + cholesteryl long-chain fatty acyl ester
-
may play an important role in regulation of the accumulation of cholesterol esters within smooth muscle cells of the artery wall during atherogenesis and in synthesis of cholesterol esters during hepatic very low-density lipoprotein synthesis and secretion
-
?
long-chain fatty acyl-CoA + cholesterol
CoA + cholesteryl long-chain fatty acyl ester
-
responsible for cellular synthesis of cholesterol esters in various cell types
-
?
long-chain fatty acyl-CoA + cholesterol
CoA + cholesteryl long-chain fatty acyl ester
-
responsible for cellular synthesis of cholesterol esters in various cell types
-
?
long-chain fatty acyl-CoA + cholesterol
CoA + cholesteryl long-chain fatty acyl ester
-
-
-
?
long-chain fatty acyl-CoA + cholesterol
CoA + cholesteryl long-chain fatty acyl ester
-
-
-
?
long-chain fatty acyl-CoA + cholesterol
CoA + cholesteryl long-chain fatty acyl ester
-
-
-
?
long-chain fatty acyl-CoA + cholesterol
CoA + cholesteryl long-chain fatty acyl ester
-
may play an important role in regulation of the accumulation of cholesterol esters within smooth muscle cells of the artery wall during atherogenesis and in synthesis of cholesterol esters during hepatic very low-density lipoprotein synthesis and secretion
-
?
long-chain fatty acyl-CoA + cholesterol
CoA + cholesteryl long-chain fatty acyl ester
-
responsible for cellular synthesis of cholesterol esters in various cell types
-
?
long-chain fatty acyl-CoA + cholesterol
CoA + cholesteryl long-chain fatty acyl ester
-
-
-
?
long-chain fatty acyl-CoA + cholesterol
CoA + cholesteryl long-chain fatty acyl ester
-
-
-
?
long-chain fatty acyl-CoA + cholesterol
CoA + cholesteryl long-chain fatty acyl ester
-
may play an important role in regulation of the accumulation of cholesterol esters within smooth muscle cells of the artery wall during atherogenesis and in synthesis of cholesterol esters during hepatic very low-density lipoprotein synthesis and secretion
-
?
long-chain fatty acyl-CoA + cholesterol
CoA + cholesteryl long-chain fatty acyl ester
-
responsible for cellular synthesis of cholesterol esters in various cell types
-
?
long-chain fatty acyl-CoA + cholesterol
CoA + cholesteryl long-chain fatty acyl ester
-
responsible for cellular synthesis of cholesterol esters in various cell types
-
?
long-chain fatty acyl-CoA + cholesterol
CoA + cholesteryl long-chain fatty acyl ester
-
role in lipoprotein metabolism and atherogenesis
-
?
long-chain fatty acyl-CoA + cholesterol
CoA + cholesteryl long-chain fatty acyl ester
-
the enzyme plays an important role in maintenance of hepatic cholesterol homeostasis
-
?
long-chain fatty acyl-CoA + cholesterol
CoA + cholesteryl long-chain fatty acyl ester
-
the enzyme plays an important role in maintenance of hepatic cholesterol homeostasis
-
?
long-chain fatty acyl-CoA + cholesterol
CoA + cholesteryl long-chain fatty acyl ester
-
-
-
?
long-chain fatty acyl-CoA + cholesterol
CoA + cholesteryl long-chain fatty acyl ester
-
-
-
?
long-chain fatty acyl-CoA + cholesterol
CoA + cholesteryl long-chain fatty acyl ester
-
may play an important role in regulation of the accumulation of cholesterol esters within smooth muscle cells of the artery wall during atherogenesis and in synthesis of cholesterol esters during hepatic very low-density lipoprotein synthesis and secretion
-
?
long-chain fatty acyl-CoA + cholesterol
CoA + cholesteryl long-chain fatty acyl ester
-
responsible for cellular synthesis of cholesterol esters in various cell types
-
?
oleoyl-CoA + 4alpha-methylcholest-7-en-3beta-ol
CoA + 4alpha-methylcholest-7-en 3-oleate
-
-
-
?
oleoyl-CoA + 4alpha-methylcholest-7-en-3beta-ol
CoA + 4alpha-methylcholest-7-en 3-oleate
-
-
-
?
oleoyl-CoA + 5alpha-cholest-8(14)-en-3beta-ol-15-one
CoA + 15-oxo-5alpha-cholest-8(14)-en-3beta-yl (9Z)-octadec-9-enoate
-
-
-
?
oleoyl-CoA + 5alpha-cholest-8(14)-en-3beta-ol-15-one
CoA + 15-oxo-5alpha-cholest-8(14)-en-3beta-yl (9Z)-octadec-9-enoate
-
-
-
?
oleoyl-CoA + 5alpha-cholest-8(14)-en-3beta-ol-15-one
CoA + oleate ester of 5alpha-cholest-8(14)-en-3beta-ol-15-one
-
-
-
?
oleoyl-CoA + 5alpha-cholest-8(14)-en-3beta-ol-15-one
CoA + oleate ester of 5alpha-cholest-8(14)-en-3beta-ol-15-one
-
-
-
?
oleoyl-CoA + campesterol
CoA + campesteryl oleate
-
campesterol is a poor substrate
-
?
oleoyl-CoA + campesterol
CoA + campesteryl oleate
-
20% of the activity with cholesterol
-
?
oleoyl-CoA + cholest-4-en-3beta-ol
CoA + cholest-4-en 3-oleate
-
low activity
-
?
oleoyl-CoA + cholest-4-en-3beta-ol
CoA + cholest-4-en 3-oleate
-
low activity
-
?
oleoyl-CoA + cholestanol
CoA + cholestanyl oleate
-
cholestanol is esterified by the enzyme at almost the same rate as cholesterol
-
?
oleoyl-CoA + cholesterol
?
-
activity assay
-
-
?
oleoyl-CoA + cholesterol
CoA + cholesteryl oleate
-
recombinant enzyme
-
?
oleoyl-CoA + cholesterol
CoA + cholesteryl oleate
-
the dimeric enzyme responds to cholesterol in essentially the same manner as the tetrameric enzyme
-
?
oleoyl-CoA + cholesterol
CoA + cholesteryl oleate
-
rate of cholesteryl ester formation is faster and more cholesteryl ester is formed with oleic acid compared to docosahexanoic acid. Docosahexanoic acid substantially reduces cholesteryl ester formation when given in combination with oleic acid
-
-
?
oleoyl-CoA + cholesterol
CoA + cholesteryl oleate
-
intrinsic fluorescence spectroscopy is used to study the binding between the enzyme and its substrates in CHAPS/phospholipid mixed micelles. Results show that oleoyl-CoA binds to ACAT1 with Kd=1.9 µM and elicits significant structural changes of the protein as manifested by the significantly positive changes in its fluorescence spectrum
-
-
?
oleoyl-CoA + cholesterol
CoA + cholesteryl oleate
cholesterol is the preferred acceptor substrate, and for ACAT1, the preferred fatty acyl-CoA is oleoyl coenzyme A
-
-
?
oleoyl-CoA + cholesterol
CoA + cholesteryl oleate
cholesterol is the preferred acceptor substrate, and for ACAT1, the preferred fatty acyl-CoA is oleoyl coenzyme A
-
-
?
oleoyl-CoA + cholesterol
CoA + cholesteryl oleate
-
highest activity
-
?
oleoyl-CoA + cholesterol
CoA + cholesteryl oleate
-
highest activity
-
?
oleoyl-CoA + cholesterol
CoA + cholesteryl oleate
-
highest activity
-
?
oleoyl-CoA + cholesterol
CoA + cholesteryl oleate
-
highest activity
-
?
oleoyl-CoA + cholesterol
CoA + cholesteryl oleate
-
-
-
?
oleoyl-CoA + cholesterol
CoA + cholesteryl oleate
-
-
-
?
oleoyl-CoA + cholesterol
CoA + cholesteryl oleate
-
-
-
?
oleoyl-CoA + cholesterol
CoA + cholesteryl oleate
-
-
-
?
oleoyl-CoA + cholesterol
CoA + cholesteryl oleate
-
-
?
oleoyl-CoA + cholesterol
CoA + cholesteryl oleate
-
highest activity
-
?
oleoyl-CoA + cholesterol
CoA + cholesteryl oleate
-
highest activity
-
?
oleoyl-CoA + desmosterol
CoA + desmosteryl oleate
-
62% of the activity with cholesterol
-
?
oleoyl-CoA + ergosterol
CoA + ergosteryl oleate
-
53% of the activity with cholesterol
-
-
?
oleoyl-CoA + ergosterol
CoA + ergosteryl oleate
-
recombinant enzyme: restores ergosteryl oleate formation in vivo to only approximately 8% of that catalysed by yeast enzyme in wild-type cells
-
-
?
oleoyl-CoA + ergosterol
CoA + ergosteryl oleate
endogenous ergosterol as substrate or exogenous ergosterol in the form of ergosterol/phosphatidylcholine vesicles as substrate
-
?
oleoyl-CoA + ergosterol
CoA + ergosteryl oleate
-
147% of the activity with cholesterol
-
?
oleoyl-CoA + lathosterol
CoA + lathosteryl oleate
-
41% of the activity with cholesterol
-
?
palmitoyl-CoA + cholesterol
CoA + cholesteryl palmitate
-
approximately 50% of the activity with oleoyl-CoA
-
?
palmitoyl-CoA + cholesterol
CoA + cholesteryl palmitate
-
-
-
?
palmitoyl-CoA + cholesterol
CoA + cholesteryl palmitate
-
47% of the activity with oleoyl-CoA
-
?
pregnenolone + oleoyl-CoA
20-oxopregn-5-en-3beta-yl (9Z)-octadec-9-enoate + CoA
without cholesterol, pregnenolone is a poor ACAT substrate, with cholesterol, the Vmax for PREG esterification increases by 100fold
-
-
?
pregnenolone + oleoyl-CoA
20-oxopregn-5-en-3beta-yl (9Z)-octadec-9-enoate + CoA
without cholesterol, pregnenolone is a poor ACAT substrate, with cholesterol, the Vmax for pregnenolone esterification increases by 100fold
-
-
?
additional information
?
-
-
isoform ACAT2 displays significantly greater selectivity for cholesterol compared with sitosterol than ACAT1
-
-
?
additional information
?
-
-
oleic acid is not incorporated into cholesterol esters by placental microsomes even in the presence of ATP, CoA and MgCl2
-
-
?
additional information
?
-
-
enzyme activity is regulated by the acyl-CoA binding protein ACBP
-
-
?
additional information
?
-
-
stereochemistry of 3-hydroxyl group at steroid ring is a critical structural feature for ACAT1 isoform
-
-
?
additional information
?
-
-
very poor substrates: 7-ketocholesterol, 7beta-hydroxycholesterol, 5beta,6beta-epoxycholesterol, 24(S),25-epoxycholesterol
-
-
?
additional information
?
-
ACAT2 plays an important role in intestinal cholesterol absorption
-
-
?
additional information
?
-
-
ACAT2 plays an important role in intestinal cholesterol absorption
-
-
?
additional information
?
-
the enzyme contains two different binding sites for steroidal molecules. In addition to cholesterol, other sterols that possess the 3-beta OH at C-3, including pregnenolone, oxysterols such as 24(S)-hydroxycholesterol and 27-hydroxycholesterol, etc., and various plant sterols, can all be ACAT substrates. 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
?
-
the enzyme contains two different binding sites for steroidal molecules. In addition to cholesterol, other sterols that possess the 3-beta OH at C-3, including pregnenolone, oxysterols such as 24(S)-hydroxycholesterol and 27-hydroxycholesterol, etc., and various plant sterols, can all be ACAT substrates. 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
?
-
-
the enzyme contains two different binding sites for steroidal molecules. In addition to cholesterol, other sterols that possess the 3-beta OH at C-3, including pregnenolone, oxysterols such as 24(S)-hydroxycholesterol and 27-hydroxycholesterol, etc., and various plant sterols, can all be ACAT substrates. 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
?
-
when assayed in reconstituted liposomes or in mixed micelles, the purified recombinant enzyme responds to cholesterol as its substrate in a sigmoidal manner. 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
?
-
when assayed in reconstituted liposomes or in mixed micelles, the purified recombinant enzyme responds to cholesterol as its substrate in a sigmoidal manner. 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
?
-
-
when assayed in reconstituted liposomes or in mixed micelles, the purified recombinant enzyme responds to cholesterol as its substrate in a sigmoidal manner. 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
?
-
hepatic ACAT2 plays a critical role in driving the production of atherogenic lipoproteins
-
-
?
additional information
?
-
the enzyme contains two different binding sites for steroidal molecules. In addition to cholesterol, other sterols that possess the 3-beta OH at C-3, including pregnenolone, oxysterols such as 24(S)-hydroxycholesterol and 27-hydroxycholesterol, etc., and various plant sterols, can all be ACAT substrates. 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
?
-
the enzyme contains two different binding sites for steroidal molecules. In addition to cholesterol, other sterols that possess the 3-beta OH at C-3, including pregnenolone, oxysterols such as 24(S)-hydroxycholesterol and 27-hydroxycholesterol, etc., and various plant sterols, can all be ACAT substrates. 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
?
-
-
two closely related enzymes identified that catalyse the esterification of cholesterol using acyl-CoA substrates, namely ACAT1 and ACAT2, the orientation of ACAT2 in the endoplasmic reticulum membrane, in addition to its expression only in liver and intestine, suggests that this enzyme may have as a primary function, the secretion of cholesteryl esters into apolipoprotein B-containing lipoproteins
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additional information
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two closely related enzymes identified that catalyse the esterification of cholesterol using acyl-CoA substrates, namely ACAT1 and ACAT2, the orientation of ACAT2 in the endoplasmic reticulum membrane, in addition to its expression only in liver and intestine, suggests that this enzyme may have as a primary function, the secretion of cholesteryl esters into apolipoprotein B-containing lipoproteins
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additional information
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structural requirements of sterol substrate
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additional information
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campesterol is a poor substrate, indicating the alkyl side chain plays an important role in the enzyme reaction
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additional information
?
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campesterol is a poor substrate, indicating the alkyl side chain plays an important role in the enzyme reaction
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?
additional information
?
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maximal ester formation is obtained when the longest chain on C-20 has five carbons and either an increase or decrease in the number of carbons reduce the amount of ester formed
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?
additional information
?
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a part of the substrate selectivity may be due to the presence of acyl-CoA hydrolase in the microsomal preparations. For this enzyme, the preferred substrate is palmitoyl-CoA which is hydrolysed about 8times faster than oleoyl-CoA
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additional information
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investigations into the sterol specificity of the enzyme
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additional information
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sitosterol, stigmasterol, ergosterol, lanosterol, cycloartenol are not substrates
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additional information
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sitosterol, stigmasterol, ergosterol, lanosterol, cycloartenol are not substrates
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additional information
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3-epicholesterol is not a substrate, indicating a requirement for a 3beta-hydroxyl group
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?
additional information
?
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3-epicholesterol is not a substrate, indicating a requirement for a 3beta-hydroxyl group
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?
additional information
?
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structural requirements of sterol substrate
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?
additional information
?
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campesterol is a poor substrate, indicating the alkyl side chain plays an important role in the enzyme reaction
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-
?
additional information
?
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maximal ester formation is obtained when the longest chain on C-20 has five carbons and either an increase or decrease in the number of carbons reduce the amount of ester formed
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?
additional information
?
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sitosterol, stigmasterol, ergosterol, lanosterol, cycloartenol are not substrates
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?
additional information
?
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3-epicholesterol is not a substrate, indicating a requirement for a 3beta-hydroxyl group
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?
additional information
?
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the enzyme has a broad substrate specificity for sterols and acyl-CoAs
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?
