2.3.1.26 acetyl-CoA + cholesterol 16% of the activity with oleoyl-CoA Saccharomyces cerevisiae CoA + cholesteryl acetate - ? 320756 2.3.1.26 acyl-CoA + 24(S)-hydroxycholesterol - Homo sapiens CoA + acyl (24S)-24-hydroxycholesterol - ? 435290 2.3.1.26 acyl-CoA + cholesterol - Gallus gallus CoA + cholesterol ester - ? 320749 2.3.1.26 acyl-CoA + cholesterol - Cricetulus griseus CoA + cholesterol ester - ? 320749 2.3.1.26 acyl-CoA + cholesterol - Cavia porcellus CoA + cholesterol ester - ? 320749 2.3.1.26 acyl-CoA + cholesterol - Mammalia CoA + cholesterol ester - ? 320749 2.3.1.26 acyl-CoA + cholesterol - Mus musculus CoA + cholesterol ester - ? 320749 2.3.1.26 acyl-CoA + cholesterol - Homo sapiens CoA + cholesterol ester - ? 320749 2.3.1.26 acyl-CoA + cholesterol - Rattus norvegicus CoA + cholesterol ester - ? 320749 2.3.1.26 acyl-CoA + cholesterol - Sus scrofa CoA + cholesterol ester - ? 320749 2.3.1.26 acyl-CoA + cholesterol - Saccharomyces cerevisiae CoA + cholesterol ester - ? 320749 2.3.1.26 acyl-CoA + cholesterol - Bos taurus CoA + cholesterol ester - ? 320749 2.3.1.26 acyl-CoA + cholesterol - Oryctolagus cuniculus CoA + cholesterol ester - ? 320749 2.3.1.26 acyl-CoA + cholesterol - Mesocricetus auratus CoA + cholesterol ester - ? 320749 2.3.1.26 acyl-CoA + cholesterol - Platyrrhini CoA + cholesterol ester - ? 320749 2.3.1.26 acyl-CoA + cholesterol - Chlorocebus aethiops CoA + cholesterol ester - ? 320749 2.3.1.26 acyl-CoA + cholesterol - Helicoverpa zea CoA + cholesterol ester - ? 320749 2.3.1.26 acyl-CoA + cholesterol - Chlorocebus sabaeus CoA + cholesterol ester - ? 320749 2.3.1.26 acyl-CoA + cholesterol - Columba sp. CoA + cholesterol ester - ? 320749 2.3.1.26 acyl-CoA + cholesterol - Rattus norvegicus CoA + cholesterol ester esterification of 3beta-hydroxy group ? 320749 2.3.1.26 acyl-CoA + cholesterol acyl-CoA derivatives can be replaced by ATP, Mg2+, CoA and fatty acids, in-situ production of acyl-CoA Rattus norvegicus CoA + cholesterol ester - ? 320749 2.3.1.26 acyl-CoA + cholesterol acyl-CoA derivatives can be replaced by ATP, Mg2+, CoA and fatty acids, in-situ production of acyl-CoA Saccharomyces cerevisiae CoA + cholesterol ester - ? 320749 2.3.1.26 acyl-CoA + cholesterol 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 Rattus norvegicus CoA + cholesterol ester - ? 320749 2.3.1.26 acyl-CoA + cholesterol ACAT-1 plays an important role in the formation of macrophage-derived foam cells in atherosclerotic lesions Homo sapiens CoA + cholesterol ester - ? 320749 2.3.1.26 acyl-CoA + cholesterol cholesterol is the preferred acceptor substrate Homo sapiens CoA + cholesterol ester - ? 320749 2.3.1.26 acyl-CoA + cholesterol cholesterol is the preferred acceptor substrate Mus musculus CoA + cholesterol ester - ? 320749 2.3.1.26 acyl-CoA + cholesterol cholesterol is the preferred acceptor substrate, and for ACAT1, the preferred fatty acyl-CoA is oleoyl coenzyme A Homo sapiens CoA + cholesterol ester - ? 320749 2.3.1.26 acyl-CoA + cholesterol cholesterol is the preferred acceptor substrate, and for ACAT1, the preferred fatty acyl-CoA is oleoyl coenzyme A Mus musculus CoA + cholesterol ester - ? 320749 2.3.1.26 acyl-CoA + cholesterol - Rattus norvegicus male Wistar CoA + cholesterol ester - ? 320749 2.3.1.26 acyl-CoA + cholesterol - Mus musculus C57BL/6 CoA + cholesterol ester - ? 320749 2.3.1.26 acyl-CoA + cholesterol - Rattus norvegicus male Sprague-Dawley CoA + cholesterol ester - ? 320749 2.3.1.26 acyl-CoA + pregnenolone - Homo sapiens CoA + pregnenolyl 3-O-acyl ester - ? 435291 2.3.1.26 acyl-CoA + pregnenolone - Mus musculus CoA + pregnenolyl 3-O-acyl ester - ? 435291 2.3.1.26 docosahexaenoyl-CoA + cholesterol 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 Homo sapiens CoA + cholesteryl docosahexaenoate - ? 409334 2.3.1.26 elaidoyl-CoA + cholesterol - Rattus norvegicus CoA + cholesteryl elaidate - ? 320771 2.3.1.26 lauroyl-CoA + cholesterol 62% of the activity with oleoyl-CoA Saccharomyces cerevisiae CoA + cholesteryl laurate - ? 320755 2.3.1.26 linelaidoyl-CoA + cholesterol - Rattus norvegicus CoA + cholesteryl linelaidate - ? 320772 2.3.1.26 linoleoyl-CoA + cholesterol - Rattus norvegicus CoA + cholesteryl linoleate - ? 320758 2.3.1.26 long-chain fatty acyl-CoA + cholesterol - Cricetulus griseus CoA + cholesteryl long-chain fatty acyl ester - ? 370325 2.3.1.26 long-chain fatty acyl-CoA + cholesterol - Cavia porcellus CoA + cholesteryl long-chain fatty acyl ester - ? 370325 2.3.1.26 long-chain fatty acyl-CoA + cholesterol - Mus musculus CoA + cholesteryl long-chain fatty acyl ester - ? 370325 2.3.1.26 long-chain fatty acyl-CoA + cholesterol - Homo sapiens CoA + cholesteryl long-chain fatty acyl ester - ? 370325 2.3.1.26 long-chain fatty acyl-CoA + cholesterol - Rattus norvegicus CoA + cholesteryl long-chain fatty acyl ester - ? 370325 2.3.1.26 long-chain fatty acyl-CoA + cholesterol - Sus scrofa CoA + cholesteryl long-chain fatty acyl ester - ? 370325 2.3.1.26 long-chain fatty acyl-CoA + cholesterol - Oryctolagus cuniculus CoA + cholesteryl long-chain fatty acyl ester - ? 370325 2.3.1.26 long-chain fatty acyl-CoA + cholesterol - Platyrrhini CoA + cholesteryl long-chain fatty acyl ester - ? 370325 2.3.1.26 long-chain fatty acyl-CoA + cholesterol - Columba sp. CoA + cholesteryl long-chain fatty acyl ester - ? 370325 2.3.1.26 long-chain fatty acyl-CoA + cholesterol 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 Cricetulus griseus CoA + cholesteryl long-chain fatty acyl ester - ? 370325 2.3.1.26 long-chain fatty acyl-CoA + cholesterol 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 Cavia porcellus CoA + cholesteryl long-chain fatty acyl ester - ? 370325 2.3.1.26 long-chain fatty acyl-CoA + cholesterol 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 Mus musculus CoA + cholesteryl long-chain fatty acyl ester - ? 370325 2.3.1.26 long-chain fatty acyl-CoA + cholesterol 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 Homo sapiens CoA + cholesteryl long-chain fatty acyl ester - ? 370325 2.3.1.26 long-chain fatty acyl-CoA + cholesterol 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 Rattus norvegicus CoA + cholesteryl long-chain fatty acyl ester - ? 370325 2.3.1.26 long-chain fatty acyl-CoA + cholesterol 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 Sus scrofa CoA + cholesteryl long-chain fatty acyl ester - ? 370325 2.3.1.26 long-chain fatty acyl-CoA + cholesterol 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 Oryctolagus cuniculus CoA + cholesteryl long-chain fatty acyl ester - ? 370325 2.3.1.26 long-chain fatty acyl-CoA + cholesterol 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 Platyrrhini CoA + cholesteryl long-chain fatty acyl ester - ? 370325 2.3.1.26 long-chain fatty acyl-CoA + cholesterol 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 Columba sp. CoA + cholesteryl long-chain fatty acyl ester - ? 370325 2.3.1.26 long-chain fatty acyl-CoA + cholesterol responsible for cellular synthesis of cholesterol esters in various cell types Cricetulus griseus CoA + cholesteryl long-chain fatty acyl ester - ? 370325 2.3.1.26 long-chain fatty acyl-CoA + cholesterol responsible for cellular synthesis of cholesterol esters in various cell types Cavia porcellus CoA + cholesteryl long-chain fatty acyl ester - ? 370325 2.3.1.26 long-chain fatty acyl-CoA + cholesterol responsible for cellular synthesis of cholesterol esters in various cell types Mus musculus CoA + cholesteryl long-chain fatty acyl ester - ? 370325 2.3.1.26 long-chain fatty acyl-CoA + cholesterol responsible for cellular synthesis of cholesterol esters in various cell types Homo sapiens CoA + cholesteryl long-chain fatty acyl ester - ? 370325 2.3.1.26 long-chain fatty acyl-CoA + cholesterol responsible for cellular synthesis of cholesterol esters in various cell types Rattus norvegicus CoA + cholesteryl long-chain fatty acyl ester - ? 370325 2.3.1.26 long-chain fatty acyl-CoA + cholesterol responsible for cellular synthesis of cholesterol esters in various cell types Sus scrofa CoA + cholesteryl long-chain fatty acyl ester - ? 370325 2.3.1.26 long-chain fatty acyl-CoA + cholesterol responsible for cellular synthesis of cholesterol esters in various cell types Oryctolagus cuniculus CoA + cholesteryl long-chain fatty acyl ester - ? 370325 2.3.1.26 long-chain fatty acyl-CoA + cholesterol responsible for cellular synthesis of cholesterol esters in various cell types Platyrrhini CoA + cholesteryl long-chain fatty acyl ester - ? 370325 2.3.1.26 long-chain fatty acyl-CoA + cholesterol responsible for cellular synthesis of cholesterol esters in various cell types Columba sp. CoA + cholesteryl long-chain fatty acyl ester - ? 370325 2.3.1.26 long-chain fatty acyl-CoA + cholesterol role in lipoprotein metabolism and atherogenesis Rattus norvegicus CoA + cholesteryl long-chain fatty acyl ester - ? 370325 2.3.1.26 long-chain fatty acyl-CoA + cholesterol 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 Homo sapiens CoA + cholesteryl long-chain fatty acyl ester - ? 370325 2.3.1.26 long-chain fatty acyl-CoA + cholesterol the high activity of intestinal enzyme renders it possible that the enzyme plays a role in cholesterol absorption Homo sapiens CoA + cholesteryl long-chain fatty acyl ester - ? 370325 2.3.1.26 long-chain fatty acyl-CoA + cholesterol the enzyme plays an important role in maintenance of hepatic cholesterol homeostasis Rattus norvegicus CoA + cholesteryl long-chain fatty acyl ester - ? 370325 2.3.1.26 long-chain fatty acyl-CoA + cholesterol the enzyme plays an important role in maintenance of hepatic cholesterol homeostasis Rattus norvegicus male Sprague-Dawley CoA + cholesteryl long-chain fatty acyl ester - ? 370325 2.3.1.26 additional information - Homo sapiens ? - ? 89 2.3.1.26 additional information - Saccharomyces cerevisiae ? - ? 89 2.3.1.26 additional information oleic acid is not incorporated into cholesterol esters by placental microsomes even in the presence of ATP, CoA and MgCl2 Homo sapiens ? - ? 89 2.3.1.26 additional information structural requirements of sterol substrate Rattus norvegicus ? - ? 89 2.3.1.26 additional information enzyme activity is regulated by the acyl-CoA binding protein ACBP Homo sapiens ? - ? 89 2.3.1.26 additional information the enzyme has a broad substrate specificity for sterols and acyl-CoAs Saccharomyces cerevisiae ? - ? 89 2.3.1.26 additional information campesterol is a poor substrate, indicating the alkyl side chain plays an important role in the enzyme reaction Rattus norvegicus ? - ? 89 2.3.1.26 additional information 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 Rattus norvegicus ? - ? 89 2.3.1.26 additional information 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 Rattus norvegicus ? - ? 89 2.3.1.26 additional information investigations into the sterol specificity of the enzyme Rattus norvegicus ? - ? 89 2.3.1.26 additional information sitosterol, stigmasterol, ergosterol, lanosterol, cycloartenol are not substrates Rattus norvegicus ? - ? 89 2.3.1.26 additional information 3-epicholesterol is not a substrate, indicating a requirement for a 3beta-hydroxyl group Rattus norvegicus ? - ? 89 2.3.1.26 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 Platyrrhini ? - ? 89 2.3.1.26 additional information isoform ACAT2 displays significantly greater selectivity for cholesterol compared with sitosterol than ACAT1 Chlorocebus aethiops ? - ? 89 2.3.1.26 additional information stereochemistry of 3-hydroxyl group at steroid ring is a critical structural feature for ACAT1 isoform Homo sapiens ? - ? 89 2.3.1.26 additional information very poor substrates: 7-ketocholesterol, 7beta-hydroxycholesterol, 5beta,6beta-epoxycholesterol, 24(S),25-epoxycholesterol Homo sapiens ? - ? 89 2.3.1.26 additional information hepatic ACAT2 plays a critical role in driving the production of atherogenic lipoproteins Mus musculus ? - ? 89 2.3.1.26 additional information ACAT2 plays an important role in intestinal cholesterol absorption Homo sapiens ? - ? 89 2.3.1.26 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 Homo sapiens ? - ? 89 2.3.1.26 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 Mus musculus ? - ? 89 2.3.1.26 additional information NBD22-steryl ester fluorescence assay Homo sapiens ? - ? 89 2.3.1.26 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 Homo sapiens ? - ? 89 2.3.1.26 additional information structural requirements of sterol substrate Rattus norvegicus male Sprague-Dawley ? - ? 89 2.3.1.26 additional information campesterol is a poor substrate, indicating the alkyl side chain plays an important role in the enzyme reaction Rattus norvegicus male Sprague-Dawley ? - ? 89 2.3.1.26 additional information 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 Rattus norvegicus male Sprague-Dawley ? - ? 89 2.3.1.26 additional information sitosterol, stigmasterol, ergosterol, lanosterol, cycloartenol are not substrates Rattus norvegicus male Sprague-Dawley ? - ? 89 2.3.1.26 additional information 3-epicholesterol is not a substrate, indicating a requirement for a 3beta-hydroxyl group Rattus norvegicus male Sprague-Dawley ? - ? 89 2.3.1.26 myristoyl-CoA + cholesterol 37% of the activity with oleoyl-CoA Saccharomyces cerevisiae CoA + cholesteryl myristate - ? 320754 2.3.1.26 oleoyl-CoA + 4alpha-methylcholest-7-en-3beta-ol - Rattus norvegicus CoA + 4alpha-methylcholest-7-en 3-oleate - ? 320765 2.3.1.26 oleoyl-CoA + 4alpha-methylcholest-7-en-3beta-ol - Rattus norvegicus CoA + (3beta,4alpha)-4-methylcholest-7-en-3-yl (9Z)-octadec-9-enoate - ? 320774 2.3.1.26 oleoyl-CoA + 5alpha,6alpha-epoxycholesterol activity comparable to cholesterol Homo sapiens CoA + 5alpha,6alpha-epoxycholesteryl oleate - ? 380169 2.3.1.26 oleoyl-CoA + 5alpha-cholest-8(14)-en-3beta-ol-15-one - Rattus norvegicus CoA + 15-oxo-5alpha-cholest-8(14)-en-3beta-yl (9Z)-octadec-9-enoate - ? 320770 2.3.1.26 oleoyl-CoA + 5alpha-cholest-8(14)-en-3beta-ol-15-one - Rattus norvegicus male Sprague-Dawley CoA + 15-oxo-5alpha-cholest-8(14)-en-3beta-yl (9Z)-octadec-9-enoate - ? 320770 2.3.1.26 oleoyl-CoA + 5alpha-cholest-8(14)-en-3beta-ol-15-one - Rattus norvegicus CoA + oleate ester of 5alpha-cholest-8(14)-en-3beta-ol-15-one - ? 320773 2.3.1.26 oleoyl-CoA + 5alpha-cholest-8(14)-en-3beta-ol-15-one - Rattus norvegicus male Sprague-Dawley CoA + oleate ester of 5alpha-cholest-8(14)-en-3beta-ol-15-one - ? 320773 2.3.1.26 oleoyl-CoA + 7alpha-hydroxycholesterol activity comparable to cholesterol Homo sapiens CoA + 7alpha-hydroxycholesteryl oleate - ? 380170 2.3.1.26 oleoyl-CoA + campesterol campesterol is a poor substrate Rattus norvegicus CoA + campesteryl oleate - ? 320764 2.3.1.26 oleoyl-CoA + campesterol 20% of the activity with cholesterol Rattus norvegicus CoA + campesteryl oleate - ? 320764 2.3.1.26 oleoyl-CoA + cholest-4-en-3beta-ol low activity Rattus norvegicus CoA + cholest-4-en 3-oleate - ? 320769 2.3.1.26 oleoyl-CoA + cholestanol - Rattus norvegicus CoA + cholestanyl oleate - ? 320766 2.3.1.26 oleoyl-CoA + cholestanol cholestanol is esterified by the enzyme at almost the same rate as cholesterol Rattus norvegicus CoA + cholestanyl oleate - ? 320766 2.3.1.26 oleoyl-CoA + cholesterol - Mus musculus CoA + cholesteryl oleate - ? 320750 2.3.1.26 oleoyl-CoA + cholesterol - Homo sapiens CoA + cholesteryl oleate - ? 320750 2.3.1.26 oleoyl-CoA + cholesterol - Rattus norvegicus CoA + cholesteryl oleate - ? 320750 2.3.1.26 oleoyl-CoA + cholesterol - Sus scrofa CoA + cholesteryl oleate - ? 320750 2.3.1.26 oleoyl-CoA + cholesterol - Oryctolagus cuniculus CoA + cholesteryl oleate - ? 320750 2.3.1.26 oleoyl-CoA + cholesterol - Platyrrhini CoA + cholesteryl oleate - ? 320750 2.3.1.26 oleoyl-CoA + cholesterol - Candida albicans CoA + cholesteryl oleate - ? 320750 2.3.1.26 oleoyl-CoA + cholesterol - Chlorocebus aethiops CoA + cholesteryl oleate - ? 320750 2.3.1.26 oleoyl-CoA + cholesterol - Alligator mississippiensis CoA + cholesteryl oleate - ? 320750 2.3.1.26 oleoyl-CoA + cholesterol - Saccharomyces cerevisiae CoA + cholesteryl oleate - ? 320750 2.3.1.26 oleoyl-CoA + cholesterol highest activity Rattus norvegicus CoA + cholesteryl oleate - ? 320750 2.3.1.26 oleoyl-CoA + cholesterol highest activity Saccharomyces cerevisiae CoA + cholesteryl oleate - ? 320750 2.3.1.26 oleoyl-CoA + cholesterol recombinant enzyme Homo sapiens CoA + cholesteryl oleate - ? 320750 2.3.1.26 oleoyl-CoA + cholesterol the dimeric enzyme responds to cholesterol in essentially the same manner as the tetrameric enzyme Homo sapiens CoA + cholesteryl oleate - ? 320750 2.3.1.26 oleoyl-CoA + cholesterol activity assay Homo sapiens CoA + cholesteryl oleate - ? 320750 2.3.1.26 oleoyl-CoA + cholesterol activity assay Chlorocebus sabaeus CoA + cholesteryl oleate - ? 320750 2.3.1.26 oleoyl-CoA + cholesterol 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 Homo sapiens CoA + cholesteryl oleate - ? 320750 2.3.1.26 oleoyl-CoA + cholesterol 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 Homo sapiens CoA + cholesteryl oleate - ? 320750 2.3.1.26 oleoyl-CoA + cholesterol cholesterol is the preferred acceptor substrate, and for ACAT1, the preferred fatty acyl-CoA is oleoyl coenzyme A Homo sapiens CoA + cholesteryl oleate - ? 320750 2.3.1.26 oleoyl-CoA + cholesterol cholesterol is the preferred acceptor substrate, and for ACAT1, the preferred fatty acyl-CoA is oleoyl coenzyme A Mus musculus CoA + cholesteryl oleate - ? 320750 2.3.1.26 oleoyl-CoA + cholesterol - Rattus norvegicus male Wistar CoA + cholesteryl oleate - ? 320750 2.3.1.26 oleoyl-CoA + cholesterol - Rattus norvegicus male Sprague-Dawley CoA + cholesteryl oleate - ? 320750 2.3.1.26 oleoyl-CoA + cholesterol - Rattus norvegicus CoA + cholesterol oleate - ? 389448 2.3.1.26 oleoyl-CoA + cholesterol - Danio rerio CoA + cholesterol oleate - ? 389448 2.3.1.26 oleoyl-CoA + cholesterol - Homo sapiens CoA + cholesterol oleate - ? 389448 2.3.1.26 oleoyl-CoA + cholesterol - Mus musculus CoA + cholesterol oleate - ? 389448 2.3.1.26 oleoyl-CoA + cholesterol - Chlorocebus aethiops CoA + cholesterol oleate - ? 389448 2.3.1.26 oleoyl-CoA + cholesterol - Mus musculus C57BL/6 CoA + cholesterol oleate - ? 389448 2.3.1.26 oleoyl-CoA + cholesterol activity assay Homo sapiens ? - ? 398011 2.3.1.26 oleoyl-CoA + cholesterol activity assay Rattus norvegicus ? - ? 398011 2.3.1.26 oleoyl-CoA + cholesterol activity assay Oryctolagus cuniculus ? - ? 398011 2.3.1.26 oleoyl-CoA + cholesterol activity assay Chlorocebus aethiops ? - ? 398011 2.3.1.26 oleoyl-CoA + cholesterol ACAT activity assay Homo sapiens ? - ? 398011 2.3.1.26 oleoyl-CoA + desmosterol - Rattus norvegicus CoA + desmosteryl oleate - ? 320767 2.3.1.26 oleoyl-CoA + desmosterol 62% of the activity with cholesterol Rattus norvegicus CoA + desmosteryl oleate - ? 320767 2.3.1.26 oleoyl-CoA + episterol 62% of the activity with cholesterol Saccharomyces cerevisiae CoA + episteryl oleate - ? 320761 2.3.1.26 oleoyl-CoA + ergosterol - Homo sapiens CoA + ergosteryl oleate - ? 320759 2.3.1.26 oleoyl-CoA + ergosterol - Saccharomyces cerevisiae CoA + ergosteryl oleate - ? 320759 2.3.1.26 oleoyl-CoA + ergosterol endogenous ergosterol as substrate or exogenous ergosterol in the form of ergosterol/phosphatidylcholine vesicles as substrate Saccharomyces cerevisiae CoA + ergosteryl oleate - ? 320759 2.3.1.26 oleoyl-CoA + ergosterol recombinant enzyme: restores ergosteryl oleate formation in vivo to only approximately 8% of that catalysed by yeast enzyme in wild-type cells Homo sapiens CoA + ergosteryl oleate - ? 320759 2.3.1.26 oleoyl-CoA + ergosterol 147% of the activity with cholesterol Saccharomyces cerevisiae CoA + ergosteryl oleate - ? 320759 2.3.1.26 oleoyl-CoA + ergosterol 53% of the activity with cholesterol Candida albicans CoA + ergosteryl oleate - ? 320759 2.3.1.26 oleoyl-CoA + fecosterol 48% of the activity with cholesterol Saccharomyces cerevisiae CoA + fecosteryl oleate - ? 320762 2.3.1.26 oleoyl-CoA + lanosterol 65% of the activity with cholesterol Saccharomyces cerevisiae CoA + lanosteryl oleate - ? 320763 2.3.1.26 oleoyl-CoA + lathosterol - Rattus norvegicus CoA + lathosteryl oleate - ? 320768 2.3.1.26 oleoyl-CoA + lathosterol 41% of the activity with cholesterol Rattus norvegicus CoA + lathosteryl oleate - ? 320768 2.3.1.26 oleoyl-CoA + sitosterol - Homo sapiens CoA + sitosteryl oleate - ? 380171 2.3.1.26 oleoyl-CoA + sitosterol - Chlorocebus aethiops CoA + sitosteryl oleate - ? 380171 2.3.1.26 oleoyl-CoA + zymosterol 93% of the activity with cholesterol Saccharomyces cerevisiae CoA + zymosteryl oleate - ? 320760 2.3.1.26 palmitoleoyl-CoA + cholesterol 91% of the activity with oleoyl-CoA Saccharomyces cerevisiae CoA + cholesteryl palmitoleate - ? 320751 2.3.1.26 palmitoyl-CoA + cholesterol - Gallus gallus CoA + cholesteryl palmitate - ? 320752 2.3.1.26 palmitoyl-CoA + cholesterol - Mus musculus CoA + cholesteryl palmitate - ? 320752 2.3.1.26 palmitoyl-CoA + cholesterol - Rattus norvegicus CoA + cholesteryl palmitate - ? 320752 2.3.1.26 palmitoyl-CoA + cholesterol - Saccharomyces cerevisiae CoA + cholesteryl palmitate - ? 320752 2.3.1.26 palmitoyl-CoA + cholesterol - Bos taurus CoA + cholesteryl palmitate - ? 320752 2.3.1.26 palmitoyl-CoA + cholesterol - Oryctolagus cuniculus CoA + cholesteryl palmitate - ? 320752 2.3.1.26 palmitoyl-CoA + cholesterol approximately 50% of the activity with oleoyl-CoA Rattus norvegicus CoA + cholesteryl palmitate - ? 320752 2.3.1.26 palmitoyl-CoA + cholesterol 47% of the activity with oleoyl-CoA Saccharomyces cerevisiae CoA + cholesteryl palmitate - ? 320752 2.3.1.26 pregnenolone + oleoyl-CoA without cholesterol, pregnenolone is a poor ACAT substrate, with cholesterol, the Vmax for PREG esterification increases by 100fold Homo sapiens 20-oxopregn-5-en-3beta-yl (9Z)-octadec-9-enoate + CoA - ? 421216 2.3.1.26 pregnenolone + oleoyl-CoA without cholesterol, pregnenolone is a poor ACAT substrate, with cholesterol, the Vmax for pregnenolone esterification increases by 100fold Homo sapiens 20-oxopregn-5-en-3beta-yl (9Z)-octadec-9-enoate + CoA - ? 421216 2.3.1.26 stearoyl-CoA + cholesterol - Homo sapiens CoA + cholesteryl stearate - ? 320757 2.3.1.26 stearoyl-CoA + cholesterol - Rattus norvegicus CoA + cholesteryl stearate - ? 320757 2.3.1.26 stearyl-CoA + cholesterol - Rattus norvegicus CoA + cholesteryl stearate - ? 320753