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Ligand cholesterol
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Basic Ligand Information
5-cholestene-3beta-ol, cholest-5-en-3-beta-ol, cholest-5-en-3beta-ol, cholesterol[side 1], cholesterol[side 2]
Related pathways
BRENDA
KEGG
MetaCyc
alpha-tomatine biosynthesis, bile acid biosynthesis, neutral pathway, cholesterol biosynthesis (algae, late side-chain reductase), cholesterol biosynthesis (diatoms), cholesterol biosynthesis (plants, early side-chain reductase) 
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Show all BRENDA pathways known for cholesterol
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open all tablesRoles as Enzyme Ligand
In Vivo Substrate in Enzyme-catalyzed Reactions (74 results)
top
EC NUMBER 
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
cholesterol + O2 = cholest-4-en-3-one + H2O2
686044, 688918, 710959, 726533, 723968, 723899, 726408, 743737, 742709, 742970, 742238, 743637, 743585, 741512, 741650, 742798
-
cholesterol + O2 = cholest-5-en-3-one + H2O2
287659, 287660, 287675, 287677, 287679, 287643, 287658, 287666, 287654, 287671, 287669, 287672, 287678, 287645, 287644, 287651, 287661, 287664, 2892, 287653, 287657, 287670, 287673, 287674, 389381, 287662, 287648, 287652, 287646, 287656, 287663, 287667, 287668, 287676, 287650, 287649, 287642, 287665, 725743, 725869, 762592, 690066
-
cholesterol + [reduced NADPH-hemoprotein reductase] + O2 = 12-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
cholesterol + [reduced NADPH-hemoprotein reductase] + O2 = 7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
285301, 285297, 285298, 285304, 285307, 659806, 659666, 660366, 659809, 673456, 671675, 671693, 675996, 671582, 674652, 673917, 671341, 667150, 736605
-
cholesterol + reduced adrenodoxin + O2 = 24-hydroxycholesterol + oxidized adrenodoxin + H2O
-
cholesterol + [reduced NADPH-hemoprotein reductase] + H+ + O2 = (24S)-24-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
cholesterol + [reduced NADPH-hemoprotein reductase] + O2 = (24S)-cholest-5-ene-3beta,24-diol + [oxidized NADPH-hemoprotein reductase] + H2O
735877, 736502, 735602, 736072, 766389, 766729, 767362, 768081, 766625, 767109, 767288, 767285, 767662
-
cholesterol + [reduced NADPHhemoprotein reductase] + O2 = (24S)-cholest-5-ene-3beta,24-diol + [oxidized NADPH-hemoprotein reductase] + H2O
-
cholesterol + reduced adrenodoxin + H+ + O2 = 26-hydroxycholesterol + oxidized adrenodoxin + H2O
-
cholesterol + reduced adrenodoxin + O2 = 27-hydroxycholesterol + oxidized adrenodoxin + H2O
-
cholest-5-en-3-beta-ol + 6 reduced [2Fe-2S] ferredoxin + 3 O2 = (25S)-3beta-hydroxycholest-5-en-26-oate + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O
-
cholesterol + 2 reduced adrenodoxin + O2 + 2 H+ = (22R)-22-hydroxycholesterol + 2 oxidized adrenodoxin + H2O
cholesterol + 2 reduced adrenodoxin + O2 = (22R)-22-hydroxycholesterol + 2 oxidized adrenodoxin + H2O
cholesterol + 6 reduced adrenodoxin + 3 O2 + 6 H+ = pregnenolone + 4-methylpentanal + 6 oxidized adrenodoxin + 4 H2O
cholesterol + 6 reduced adrenodoxin + 3 O2 = pregnenolone + 4-methylpentanal + 6 oxidized adrenodoxin + 4 H2O
cholesterol + reduced adrenal ferredoxin + O2 = pregnenolone + 4-methylpentanal + oxidized adrenal ferredoxin
cholesterol + reduced ferredoxin + O2 = pregnenolone + 4-methylpentanal + oxidized ferredoxin
cholesterol + O2 + NADH + H+ = cholesta-5,7-dien-3beta-ol + NAD+ + H2O
-
cholesterol + O2 + NADPH + H+ = cholesta-5,7-dien-3beta-ol + NADP+ + H2O
-
cholesterol + AH2 + O2 = 25-hydroxycholesterol + A + H2O
659137, 660012, 658245, 658159, 700999, 699414, 727611, 727109, 728088, 726545, 744738, 745051, 745479, 745518, 745658, 745657, 745450, 746435, 746440
-
cholesterol + NADP+ = cholesta-5,7-dien-3beta-ol + NADPH + H+
-
acyl-CoA + cholesterol = CoA + cholesterol ester
acyl-CoA + cholesterol = CoA + cholesterol ester
acyl-CoA + cholesterol = CoA + cholesterol ester
acyl-CoA + cholesterol = CoA + cholesterol ester
acyl-CoA + cholesterol = CoA + cholesterol 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
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
phosphatidylcholine + cholesterol = 1-acylglycerophosphocholine + cholesterol ester
-
phosphatidylcholine + cholesterol = 1-acylglycerophosphocholine + cholesteryl ester
-
phosphatidylcholine + cholesterol = cholesteryl ester + lysophosphatidylcholine
-
3'-phosphoadenylyl sulfate + cholesterol = adenosine 3',5'-bisphosphate + cholesteryl 3-sulfate
-
3'-phosphoadenylylsulfate + cholesterol = adenosine 3',5'-bisphosphate + cholesterol 3-sulfate
-
3'-phosphoadenylyl sulfate + cholesterol = adenosine 3',5'-bisphosphate + cholesterol 3-sulfate
-
3'-phosphoadenylyl sulfate + cholesterol = adenosine 3',5'-bisphosphate + cholesteryl 3-sulfate
-
ATP + H2O + cholesterol[side 1] = ADP + phosphate + cholesterol[side 2]
ATP + H2O + cholesterol[side 1] = ADP + phosphate + cholesterol[side 2]
ATP + H2O + cholesterol[side 1] = ADP + phosphate + cholesterol[side 2]
ATP + H2O + cholesterol[side 1] = ADP + phosphate + cholesterol[side 2]
ATP + H2O + cholesterol[side 1] = ADP + phosphate + cholesterol[side 2]
ATP + H2O + cholesterol[side 1] = ADP + phosphate + cholesterol[side 2]
ATP + H2O + cholesterol[side 1] = ADP + phosphate + cholesterol[side 2]
ATP + H2O + cholesterol[side 1] = ADP + phosphate + cholesterol[side 2]
ATP + H2O + cholesterol[side 1] = ADP + phosphate + cholesterol[side 2]
ATP + H2O + cholesterol[side 1] = ADP + phosphate + cholesterol[side 2]
ATP + H2O + cholesterol[side 1] = ADP + phosphate + cholesterol[side 2]
ATP + H2O + cholesterol[side 1] = ADP + phosphate + cholesterol[side 2]
ATP + H2O + cholesterol[side 1] = ADP + phosphate + cholesterol[side 2]
ATP + H2O + cholesterol[side 1] = ADP + phosphate + cholesterol[side 2]
ATP + H2O + cholesterol[side 1] = ADP + phosphate + cholesterol[side 2]
ATP + H2O + cholesterol[side 1] = ADP + phosphate + cholesterol[side 2]
ATP + H2O + cholesterol[side 1] = ADP + phosphate + cholesterol[side 2]
ATP + H2O + cholesterol[side 1] = ADP + phosphate + cholesterol[side 2]
ATP + H2O + cholesterol[side 1] = ADP + phosphate + cholesterol[side 2]
ATP + H2O + cholesterol[side 1] = ADP + phosphate + cholesterol[side 2]
ATP + H2O + cholesterol[side 1] = ADP + phosphate + cholesterol[side 2]
ATP + H2O + cholesterol[side 1] = ADP + phosphate + cholesterol[side 2]
ATP + H2O + cholesterol[side 1] = ADP + phosphate + cholesterol[side 2]
In Vivo Product in Enzyme-catalyzed Reactions (59 results)
EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
5alpha-cholestan-3beta-ol + ferrocytochrome b5 + H+ + O2 = cholest-5-en-3beta-ol + ferricytochrome b5 + 2 H2O
-
-
cholesta-5,7-dien-3-beta-ol + NADPH = cholesterol + NADP+
349267, 349264, 349265, 349269, 349271, 349272, 349274, 349278, 349279, 349275, 349276, 349273, 349266, 349277, 349268, 349270
-
cholesteryl esters + H2O = cholesterol + fatty acid
133842, 133845, 133846, 133857, 133860, 133856, 133822, 133826, 133825, 80838, 133858, 133831, 133853, 133855, 133859, 133861, 133839, 133824, 133862, 133838, 133835, 133834, 133850, 133851, 133854, 133849, 133852, 133828, 133829, 133848, 133823, 133843, 133832, 133841, 133827, 133830, 133833, 133836, 133840
-
Substrate in Enzyme-catalyzed Reactions (202 results)
EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
cholesterol + O2 = cholest-4-en-3-one + H2O2
287660, 287675, 287677, 287679, 287643, 287658, 287666, 287654, 287671, 287669, 287672, 287678, 287642, 287645, 287644, 287661, 287653, 287657, 287670, 287673, 389381, 287662, 287648, 287652, 287646, 287656, 287663, 287667, 287668, 287676, 287650, 287649, 2892, 287664, 287665, 287674, 287659, 287651, 655611, 657224, 654191, 656321, 656316, 655089, 674444, 673393, 673134, 686044, 688918, 677549, 685245, 684242, 684653, 686045, 697915, 697914, 710959, 710711, 710910, 712958, 713589, 710964, 711588, 712891, 726533, 723968, 723899, 726408, 743737, 742709, 742970, 742238, 743637, 743585, 741512, 741650, 742798, 742195
-
cholesterol + O2 = cholest-5-en-3-one + H2O2
287659, 287660, 287675, 287677, 287679, 287643, 287658, 287666, 287654, 287671, 287669, 287672, 287678, 287645, 287644, 287651, 287661, 287664, 2892, 287653, 287657, 287670, 287673, 287674, 389381, 287662, 287648, 287652, 287646, 287656, 287663, 287667, 287668, 287676, 287650, 287649, 287642, 287665, 654343, 725743, 725869, 742201, 762592, 690066, 762864, 762784, 763627, 763624, 763673, 763714, 763712, 763720, 762731, 763140, 763212, 763254, 763666, 763657
-
cholesterol + [reduced NADPH-hemoprotein reductase] + H+ + O2 = ? + [oxidized NADPH-hemoprotein reductase] + H2O
-
cholesterol + [reduced NADPH-hemoprotein reductase] + O2 = 12-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
cholesterol + [reduced NADPH-hemoprotein reductase] + O2 = 7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
285301, 285302, 285312, 285296, 285297, 285298, 285299, 285300, 285303, 285304, 285305, 285306, 285308, 285309, 285310, 285314, 285311, 285313, 285307, 659806, 659666, 660366, 659809, 673456, 671675, 671693, 675996, 671582, 674652, 673917, 671341, 667150, 689381, 736605
-
cholesterol + reduced adrenodoxin + O2 = 24-hydroxycholesterol + oxidized adrenodoxin + H2O
-
cholesterol + [reduced NADPH-hemoprotein reductase] + H+ + O2 = (24S)-24-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
658159, 657971, 659216, 657671, 688555, 684856, 686258, 687987, 689814, 701715, 695874, 705920, 706536, 705008, 705825, 711641, 712869, 727298, 728617
-
cholesterol + [reduced NADPH-hemoprotein reductase] + O2 = (24S)-cholest-5-ene-3beta,24-diol + [oxidized NADPH-hemoprotein reductase] + H2O
735877, 736502, 735602, 736072, 766389, 766729, 767362, 768081, 766625, 767109, 767288, 767285, 767662, 766311
-
cholesterol + [reduced NADPHhemoprotein reductase] + O2 = (24S)-cholest-5-ene-3beta,24-diol + [oxidized NADPH-hemoprotein reductase] + H2O
-
cholesterol + reduced adrenodoxin + H+ + O2 = 26-hydroxycholesterol + oxidized adrenodoxin + H2O
-
cholesterol + reduced adrenodoxin + O2 = 24-hydroxycholesterol + oxidized adrenodoxin + H2O
-
cholesterol + reduced adrenodoxin + O2 = 25-hydroxycholesterol + oxidized adrenodoxin + H2O
-
cholesterol + reduced adrenodoxin + O2 = 26-hydroxycholesterol + oxidized adrenodoxin + H2O
-
cholesterol + reduced adrenodoxin + O2 = 27-hydroxycholesterol + oxidized adrenodoxin + H2O
-
cholest-5-en-3-beta-ol + 6 reduced [2Fe-2S] ferredoxin + 3 O2 = (25R)-3beta-hydroxycholest-5-en-26-oate + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O
-
cholesterol + 6 reduced [2Fe-2S] ferredoxin + 3 O2 = 3beta-hydroxycholest-5-en-26-oic acid + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O
-
cholest-5-en-3-beta-ol + 6 reduced [2Fe-2S] ferredoxin + 3 O2 = (25S)-3beta-hydroxycholest-5-en-26-oate + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O
-
cholest-5-en-3beta-ol + 6 reduced [2Fe-2S] ferredoxin + 3 O2 = (25S)-3beta-hydroxycholest-5-en-26-oate + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O
-
cholesterol + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = 27-hydroxycholesterol + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
cholesterol + reduced ferredoxin [iron-sulfur] cluster + O2 = 26-hydroxycholesterol + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
cholesterol + 2 reduced adrenodoxin + O2 + 2 H+ = (22R)-22-hydroxycholesterol + 2 oxidized adrenodoxin + H2O
cholesterol + 2 reduced adrenodoxin + O2 = (22R)-22-hydroxycholesterol + 2 oxidized adrenodoxin + H2O
cholesterol + 6 reduced adrenodoxin + 3 O2 + 6 H+ = pregnenolone + 4-methylpentanal + 6 oxidized adrenodoxin + 4 H2O
cholesterol + 6 reduced adrenodoxin + 3 O2 = pregnenolone + 4-methylpentanal + 6 oxidized adrenodoxin + 4 H2O
cholesterol + 6 reduced adrenodoxin mutant S112W + 3 O2 = pregnenolone + 4-methylpentanal + 6 oxidized adrenodoxin mutant S112W + 4 H2O
cholesterol + reduced adrenal ferredoxin + O2 = pregnenolone + 4-methylpentanal + oxidized adrenal ferredoxin
cholesterol + reduced adrenodoxin + O2 + H+ = pregnenolone + 4-methylpentanal + oxidized adrenodoxin + H2O
cholesterol + reduced adrenodoxin + O2 = ? + oxidized adrenodoxin + H2O
cholesterol + reduced adrenodoxin + O2 = pregnenolone + 4-methylpentanal + oxidized adrenodoxin + H2O
cholesterol + reduced ferredoxin + O2 = pregnenolone + 4-methylpentanal + oxidized ferredoxin
cholesterol + O2 + NAD(P)H + H+ = cholesta-5,7-dien-3beta-ol + NAD(P)+ + 2 H2O
-
cholesterol + O2 + NADH + H+ = cholesta-5,7-dien-3beta-ol + NAD+ + H2O
-
cholesterol + O2 + NADPH + H+ = cholesta-5,7-dien-3beta-ol + NADP+ + H2O
-
5-cholestene-3beta-ol + O2 + NADH + H+ = 9alpha-hydroxy-5-cholestene-3beta-ol + H2O + NAD+
-
cholesterol + AH2 + O2 = 25-hydroxycholesterol + A + H2O
659137, 660012, 658245, 658159, 658244, 658246, 700999, 699414, 727611, 727109, 728088, 726545, 744738, 745051, 745479, 745518, 745658, 745657, 745450, 746435, 746440
-
cholesterol + NADP+ = cholesta-5,7-dien-3beta-ol + NADPH + H+
-
cholesterol + O2 + NAD(P)H + H+ = cholesta-5,7-dien-3beta-ol + NAD(P)+ + 2 H2O
-
acyl-CoA + cholesterol = CoA + cholesterol ester
486687, 486677, 486691, 486676, 486679, 486684, 486678, 486680, 486685, 486686, 486688, 486689, 486682, 486683, 486690, 486681, 486674, 486675, 671677, 685611, 685979, 686560, 674216, 687687, 688227, 688287, 688767, 684800, 684799, 684780, 685566, 685899, 688060, 689426, 684773, 684882, 672494, 684786, 672617, 686600, 686931, 688139, 720018, 735754, 735756, 735970, 736580, 736719, 736937, 735753, 736702
acyl-CoA + cholesterol = CoA + cholesterol ester
486687, 486677, 486691, 486676, 486679, 486684, 486678, 486680, 486685, 486686, 486688, 486689, 486682, 486683, 486690, 486681, 486674, 486675, 671677, 685611, 685979, 686560, 674216, 687687, 688227, 688287, 688767, 684800, 684799, 684780, 685566, 685899, 688060, 689426, 684773, 684882, 672494, 684786, 672617, 686600, 686931, 688139, 720018, 735754, 735756, 735970, 736580, 736719, 736937, 735753, 736702
acyl-CoA + cholesterol = CoA + cholesterol ester
486687, 486677, 486691, 486676, 486679, 486684, 486678, 486680, 486685, 486686, 486688, 486689, 486682, 486683, 486690, 486681, 486674, 486675, 671677, 685611, 685979, 686560, 674216, 687687, 688227, 688287, 688767, 684800, 684799, 684780, 685566, 685899, 688060, 689426, 684773, 684882, 672494, 684786, 672617, 686600, 686931, 688139, 720018, 735754, 735756, 735970, 736580, 736719, 736937, 735753, 736702
acyl-CoA + cholesterol = CoA + cholesterol ester
486687, 486677, 486691, 486676, 486679, 486684, 486678, 486680, 486685, 486686, 486688, 486689, 486682, 486683, 486690, 486681, 486674, 486675, 671677, 685611, 685979, 686560, 674216, 687687, 688227, 688287, 688767, 684800, 684799, 684780, 685566, 685899, 688060, 689426, 684773, 684882, 672494, 684786, 672617, 686600, 686931, 688139, 720018, 735754, 735756, 735970, 736580, 736719, 736937, 735753, 736702
acyl-CoA + cholesterol = CoA + cholesterol ester
486687, 486677, 486691, 486676, 486679, 486684, 486678, 486680, 486685, 486686, 486688, 486689, 486682, 486683, 486690, 486681, 486674, 486675, 671677, 685611, 685979, 686560, 674216, 687687, 688227, 688287, 688767, 684800, 684799, 684780, 685566, 685899, 688060, 689426, 684773, 684882, 672494, 684786, 672617, 686600, 686931, 688139, 720018, 735754, 735756, 735970, 736580, 736719, 736937, 735753, 736702
docosahexaenoyl-CoA + cholesterol = CoA + cholesteryl docosahexaenoate
docosahexaenoyl-CoA + cholesterol = CoA + cholesteryl docosahexaenoate
docosahexaenoyl-CoA + cholesterol = CoA + cholesteryl docosahexaenoate
docosahexaenoyl-CoA + cholesterol = CoA + cholesteryl docosahexaenoate
docosahexaenoyl-CoA + cholesterol = CoA + cholesteryl docosahexaenoate
linoleoyl-CoA + cholesterol = CoA + cholesteryl linoleate
linoleoyl-CoA + cholesterol = CoA + cholesteryl linoleate
linoleoyl-CoA + cholesterol = CoA + cholesteryl linoleate
linoleoyl-CoA + cholesterol = CoA + cholesteryl linoleate
linoleoyl-CoA + cholesterol = CoA + cholesteryl linoleate
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
long-chain fatty acyl-CoA + cholesterol = CoA + cholesteryl long-chain fatty acyl ester
oleoyl-CoA + cholesterol = ?
oleoyl-CoA + cholesterol = ?
oleoyl-CoA + cholesterol = ?
oleoyl-CoA + cholesterol = ?
oleoyl-CoA + cholesterol = ?
oleoyl-CoA + cholesterol = CoA + cholesterol oleate
oleoyl-CoA + cholesterol = CoA + cholesterol oleate
oleoyl-CoA + cholesterol = CoA + cholesterol oleate
oleoyl-CoA + cholesterol = CoA + cholesterol oleate
oleoyl-CoA + cholesterol = CoA + cholesterol oleate
oleoyl-CoA + cholesterol = CoA + cholesteryl oleate
486677, 486698, 486676, 486679, 486684, 486696, 486697, 486702, 486709, 486680, 486685, 486686, 486688, 486701, 486704, 486683, 486708, 486707, 486700, 486674, 486681, 486675, 486710, 660876, 661010, 662125, 662168, 672494, 673648, 671677, 671658, 685899, 688227, 684799, 706575, 687687, 718887, 719280, 736702
oleoyl-CoA + cholesterol = CoA + cholesteryl oleate
486677, 486698, 486676, 486679, 486684, 486696, 486697, 486702, 486709, 486680, 486685, 486686, 486688, 486701, 486704, 486683, 486708, 486707, 486700, 486674, 486681, 486675, 486710, 660876, 661010, 662125, 662168, 672494, 673648, 671677, 671658, 685899, 688227, 684799, 706575, 687687, 718887, 719280, 736702
oleoyl-CoA + cholesterol = CoA + cholesteryl oleate
486677, 486698, 486676, 486679, 486684, 486696, 486697, 486702, 486709, 486680, 486685, 486686, 486688, 486701, 486704, 486683, 486708, 486707, 486700, 486674, 486681, 486675, 486710, 660876, 661010, 662125, 662168, 672494, 673648, 671677, 671658, 685899, 688227, 684799, 706575, 687687, 718887, 719280, 736702
oleoyl-CoA + cholesterol = CoA + cholesteryl oleate
486677, 486698, 486676, 486679, 486684, 486696, 486697, 486702, 486709, 486680, 486685, 486686, 486688, 486701, 486704, 486683, 486708, 486707, 486700, 486674, 486681, 486675, 486710, 660876, 661010, 662125, 662168, 672494, 673648, 671677, 671658, 685899, 688227, 684799, 706575, 687687, 718887, 719280, 736702
oleoyl-CoA + cholesterol = CoA + cholesteryl oleate
486677, 486698, 486676, 486679, 486684, 486696, 486697, 486702, 486709, 486680, 486685, 486686, 486688, 486701, 486704, 486683, 486708, 486707, 486700, 486674, 486681, 486675, 486710, 660876, 661010, 662125, 662168, 672494, 673648, 671677, 671658, 685899, 688227, 684799, 706575, 687687, 718887, 719280, 736702
palmitoyl-CoA + cholesterol = CoA + cholesteryl palmitate
palmitoyl-CoA + cholesterol = CoA + cholesteryl palmitate
palmitoyl-CoA + cholesterol = CoA + cholesteryl palmitate
palmitoyl-CoA + cholesterol = CoA + cholesteryl palmitate
palmitoyl-CoA + cholesterol = CoA + cholesteryl palmitate
stearoyl-CoA + cholesterol = CoA + cholesteryl stearate
stearoyl-CoA + cholesterol = CoA + cholesteryl stearate
stearoyl-CoA + cholesterol = CoA + cholesteryl stearate
stearoyl-CoA + cholesterol = CoA + cholesteryl stearate
stearoyl-CoA + cholesterol = CoA + cholesteryl stearate
1,2-bis-(1-pyrenebutanoyl)-sn-glycero-3-phosphocholine + cholesterol = cholesteryl-1-pyrenebutyrate + lysophosphatidylcholine
-
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine + cholesterol = 1-palmitoyl-sn-glycero-3-phosphocholine + cholesteryl oleate
-
cholesterol + 1-O-hexadecyl-2-oleylphosphatidylcholine = cholesteryl oleate + 1-O-hexadecylglycerophosphocholine
-
cholesterol + 1-palmitoyl-2-(5Z,8Z,11Z,14Z,17Z)-eicosapenta-5,8,11,14,17-enoylphosphatidylcholine = (3beta)-cholest-5-en-3-yl (5Z,8Z,11Z,14Z,17Z)-icosa-5,8,11,14,17-pentaenoate + 1-palmitoylglycerophosphocholine
-
cholesterol + 1-palmitoyl-2-arachidonoylphosphatidylcholine = cholesteryl arachidonate + 1-palmitoylglycerophosphocholine
-
cholesterol + 1-palmitoyl-2-docosahexaenoylphosphatidylcholine = cholesteryl docosahexaenoate + 1-palmitoylglycerophosphocholine
-
cholesterol + 1-palmitoyl-2-linoleoylphosphatidylcholine = cholesteryl linoleate + 1-palmitoylglycerophosphocholine
-
cholesterol + 1-palmitoyl-2-oleoylphosphatidylcholine = cholesteryl oleate + 1-palmitoylglycerophosphocholine
-
cholesterol + 1-palmitoyl-2-phytanoylphosphatidylcholine = cholesteryl phytanoate + 1-palmitoylglycerophosphocholine
-
cholesterol + 1-phytanoyl-2-palmitoylphosphatidylcholine = cholesteryl palmitate + 1-phytanylglyerophosphocholine
-
dioleoyl-phosphatidyl choline + cholesterol = 1-oleoyl-phosphatidyl choline + cholesteryl oleate
-
L-alpha-phosphatidylcholine type XVI-E + cholesterol = 1-acylglycerophosphocholine + cholesteryl ester
-
phosphatidylcholine + cholesterol = 1-acylglycerophosphocholine + cholesterol ester
-
phosphatidylcholine + cholesterol = 1-acylglycerophosphocholine + cholesteryl ester
661227, 663302, 661231, 662168, 671676, 671959, 672155, 686547, 686317, 720368, 736674, 755762, 757930, 757014
-
phosphatidylcholine + cholesterol = cholesteryl ester + lysophosphatidylcholine
-
phosphatidylethanolamine + cholesterol = cholesteryl ester + lysophosphatidylethanolamine
-
cholesterol + 1,2-diacyl-sn-glycerol = monoacylglycerol + cholesterol-3-O-acyl ester
-
trilinoleoylglycerol + cholest-5-en-3beta-ol = dilinoleoylglycerol + cholesteryl linoleate
-
tripalmitoylglycerol + cholest-5-en-3beta-ol = dipalmitoylglycerol + cholesteryl palmitate
-
tristearoylglycerol + cholest-5-en-3beta-ol = distearoylglycerol + cholesteryl stearate
-
UDP-glucose + cholesterol = UDP + cholesterol 3-beta-D-glucoside
-
3'-phosphoadenylyl sulfate + cholesterol = adenosine 3',5'-bisphosphate + cholesterol sulfate
-
3'-phosphoadenylyl sulfate + cholesterol = adenosine 3',5'-bisphosphate + cholesteryl 3-sulfate
-
3'-phosphoadenylyl sulfate + cholesterol = adenosine 3',5'-bisphosphate + cholesteryl sulfate
-
3'-phosphoadenylylsulfate + cholesterol = adenosine 3',5'-bisphosphate + cholesterol 3-sulfate
-
3'-phosphoadenylylsulfate + cholesterol = adenosine 3',5'-bisphosphate + cholesterol sulfate
-
3'-phosphoadenylyl sulfate + cholesterol = adenosine 3',5'-bisphosphate + cholesterol 3-sulfate
-
3'-phosphoadenylyl sulfate + cholesterol = adenosine 3',5'-bisphosphate + cholesteryl 3-sulfate
-
3'-phosphoadenylylsulfate + cholesterol = adenosine 3',5'-bisphosphate + cholesterol sulfate
-
ATP + H2O + cholesterol[side 1] = ADP + phosphate + cholesterol[side 2]
ATP + H2O + cholesterol[side 1] = ADP + phosphate + cholesterol[side 2]
ATP + H2O + cholesterol[side 1] = ADP + phosphate + cholesterol[side 2]
ATP + H2O + cholesterol[side 1] = ADP + phosphate + cholesterol[side 2]
ATP + H2O + cholesterol[side 1] = ADP + phosphate + cholesterol[side 2]
ATP + H2O + cholesterol[side 1] = ADP + phosphate + cholesterol[side 2]
ATP + H2O + cholesterol[side 1] = ADP + phosphate + cholesterol[side 2]
ATP + H2O + cholesterol[side 1] = ADP + phosphate + cholesterol[side 2]
ATP + H2O + cholesterol[side 1] = ADP + phosphate + cholesterol[side 2]
ATP + H2O + cholesterol[side 1] = ADP + phosphate + cholesterol[side 2]
ATP + H2O + cholesterol[side 1] = ADP + phosphate + cholesterol[side 2]
ATP + H2O + cholesterol[side 1] = ADP + phosphate + cholesterol[side 2]
ATP + H2O + cholesterol[side 1] = ADP + phosphate + cholesterol[side 2]
ATP + H2O + cholesterol[side 1] = ADP + phosphate + cholesterol[side 2]
ATP + H2O + cholesterol[side 1] = ADP + phosphate + cholesterol[side 2]
ATP + H2O + cholesterol[side 1] = ADP + phosphate + cholesterol[side 2]
ATP + H2O + cholesterol[side 1] = ADP + phosphate + cholesterol[side 2]
ATP + H2O + cholesterol[side 1] = ADP + phosphate + cholesterol[side 2]
ATP + H2O + cholesterol[side 1] = ADP + phosphate + cholesterol[side 2]
ATP + H2O + cholesterol[side 1] = ADP + phosphate + cholesterol[side 2]
ATP + H2O + cholesterol[side 1] = ADP + phosphate + cholesterol[side 2]
ATP + H2O + cholesterol[side 1] = ADP + phosphate + cholesterol[side 2]
ATP + H2O + cholesterol[side 1] = ADP + phosphate + cholesterol[side 2]
Product in Enzyme-catalyzed Reactions (114 results)
EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
5alpha-cholestan-3beta-ol + ferrocytochrome b5 + H+ + O2 = cholest-5-en-3beta-ol + ferricytochrome b5 + 2 H2O
-
-
cholesta-5,7-dien-3-beta-ol + NADPH = cholesterol + NADP+
349267, 349264, 349265, 349269, 349271, 349272, 349274, 349278, 349279, 349275, 349276, 349273, 349266, 349277, 349268, 349270
-
cholesta-5,7-dien-3beta-ol + NADPH = cholesterol + NADP+
349267, 349277, 349279, 349264, 349265, 349266, 349268, 349269, 349270, 349271, 349274, 349276, 349278, 349275, 349273, 349272, -
-
cholesteryl esters + H2O = cholesterol + fatty acid
133842, 133845, 133846, 133857, 133860, 133856, 133822, 133826, 133825, 80838, 133858, 133831, 133853, 133855, 133859, 133861, 133839, 133824, 133862, 133838, 133835, 133834, 133850, 133851, 133854, 133849, 133852, 133828, 133829, 133848, 133823, 133843, 133832, 133841, 133827, 133830, 133833, 133836, 133840
-
cholesteryl linoleate + H2O = cholesterol + linoleic acid
-
cholesteryl oleate + H2O = cholesterol + oleate
-
cholesteryl oleate + H2O = cholesterol + oleic acid
133832, 133841, 133835, 133838, 133842, 133852, 133860, 133845, 133846, 133857, 133856, 133826, 133829, 133848, 133850, 133851, 133854, 80838, 133825, 133849, 133836, 133858, 133824, 133833, 133855, 133859, 133839, 133827, 133828, 133830, 133837, 133840, 133853, 133861, -
-
Activator in Enzyme-catalyzed Reactions (136 results)
EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
addition of cholesterol to frozen microsomes prepared from unfrozen liver tissue increases the enzyme activity
addition of cholesterol to frozen microsomes prepared from unfrozen liver tissue increases the enzyme activity
addition of cholesterol to frozen microsomes prepared from unfrozen liver tissue increases the enzyme activity
addition of cholesterol to frozen microsomes prepared from unfrozen liver tissue increases the enzyme activity
addition of cholesterol to frozen microsomes prepared from unfrozen liver tissue increases the enzyme activity
addition of cholesterol to microsomes prepared from frozen liver tissue does not further increase the enzyme activity
addition of cholesterol to microsomes prepared from frozen liver tissue does not further increase the enzyme activity
addition of cholesterol to microsomes prepared from frozen liver tissue does not further increase the enzyme activity
addition of cholesterol to microsomes prepared from frozen liver tissue does not further increase the enzyme activity
addition of cholesterol to microsomes prepared from frozen liver tissue does not further increase the enzyme activity
day 40 samples, exogenous, added as phosphatidylcholine liposomes, concentration-dependent increase in activity
day 40 samples, exogenous, added as phosphatidylcholine liposomes, concentration-dependent increase in activity
day 40 samples, exogenous, added as phosphatidylcholine liposomes, concentration-dependent increase in activity
day 40 samples, exogenous, added as phosphatidylcholine liposomes, concentration-dependent increase in activity
day 40 samples, exogenous, added as phosphatidylcholine liposomes, concentration-dependent increase in activity
exogenous cholesterol in the liposomes is absolutely necessary for activity of the reconstituted enzyme
exogenous cholesterol in the liposomes is absolutely necessary for activity of the reconstituted enzyme
exogenous cholesterol in the liposomes is absolutely necessary for activity of the reconstituted enzyme
exogenous cholesterol in the liposomes is absolutely necessary for activity of the reconstituted enzyme
exogenous cholesterol in the liposomes is absolutely necessary for activity of the reconstituted enzyme
exogenous, 25% increase of adrenal microsome activity and 2fold increase of activity in liver
exogenous, 25% increase of adrenal microsome activity and 2fold increase of activity in liver
exogenous, 25% increase of adrenal microsome activity and 2fold increase of activity in liver
exogenous, 25% increase of adrenal microsome activity and 2fold increase of activity in liver
exogenous, 25% increase of adrenal microsome activity and 2fold increase of activity in liver
exogenous, added as phosphatidylcholine liposome or in acetone solution, stimulates
exogenous, added as phosphatidylcholine liposome or in acetone solution, stimulates
exogenous, added as phosphatidylcholine liposome or in acetone solution, stimulates
exogenous, added as phosphatidylcholine liposome or in acetone solution, stimulates
exogenous, added as phosphatidylcholine liposome or in acetone solution, stimulates
exogenous, delivered as a Triton WR-1339 detergent dispersion, increases activity
exogenous, delivered as a Triton WR-1339 detergent dispersion, increases activity
exogenous, delivered as a Triton WR-1339 detergent dispersion, increases activity
exogenous, delivered as a Triton WR-1339 detergent dispersion, increases activity
exogenous, delivered as a Triton WR-1339 detergent dispersion, increases activity
presence of cholesterol stimulates reaction of ACAT1 with sitosterol up to 3fold, reaction of ACAT2 is only moderately activated
presence of cholesterol stimulates reaction of ACAT1 with sitosterol up to 3fold, reaction of ACAT2 is only moderately activated
presence of cholesterol stimulates reaction of ACAT1 with sitosterol up to 3fold, reaction of ACAT2 is only moderately activated
presence of cholesterol stimulates reaction of ACAT1 with sitosterol up to 3fold, reaction of ACAT2 is only moderately activated
presence of cholesterol stimulates reaction of ACAT1 with sitosterol up to 3fold, reaction of ACAT2 is only moderately activated
serves as an enzyme activator in vitro, in addition to its role as an enzyme substrate
serves as an enzyme activator in vitro, in addition to its role as an enzyme substrate
serves as an enzyme activator in vitro, in addition to its role as an enzyme substrate
serves as an enzyme activator in vitro, in addition to its role as an enzyme substrate
serves as an enzyme activator in vitro, in addition to its role as an enzyme substrate
significant activation of reaction with 7-ketocholesterol as substrate, decrease in Hill coefficient from 3.0 without cholesterol to 1.1 with cholesterol
significant activation of reaction with 7-ketocholesterol as substrate, decrease in Hill coefficient from 3.0 without cholesterol to 1.1 with cholesterol
significant activation of reaction with 7-ketocholesterol as substrate, decrease in Hill coefficient from 3.0 without cholesterol to 1.1 with cholesterol
significant activation of reaction with 7-ketocholesterol as substrate, decrease in Hill coefficient from 3.0 without cholesterol to 1.1 with cholesterol
significant activation of reaction with 7-ketocholesterol as substrate, decrease in Hill coefficient from 3.0 without cholesterol to 1.1 with cholesterol
DGKalpha can be activated in vitro in a Ca2+-independent manner by lipids such cholesterol
-
concentration dependent activation of alkaline phosphatase grown in low phosphate medium
-
sphingomyelinase activity is higher in the cholesterol-induced liquid-ordered phase than in the gel phase
-
sphingomyelinase is enhanced by cholesterol and by lipids with an intrinsic negative curvature, e.g. phosphatidylethanolamine
-
phospholipase C is enhanced by cholesterol and by lipids with an intrinsic negative curvature, e.g. phosphatidylethanolamine
-
in phosphatidylcholine/phosphatidylserine vesicles, cholesterol enhances Factor Va inactivation and the rate of cleavage by enzyme both at R506 and R306
-
the transport activity of P-glycoprotein is elevated by about 40% cholesterol
the transport activity of P-glycoprotein is elevated by about 40% cholesterol
the transport activity of P-glycoprotein is elevated by about 40% cholesterol
the transport activity of P-glycoprotein is elevated by about 40% cholesterol
the transport activity of P-glycoprotein is elevated by about 40% cholesterol
the transport activity of P-glycoprotein is elevated by about 40% cholesterol
the transport activity of P-glycoprotein is elevated by about 40% cholesterol
the transport activity of P-glycoprotein is elevated by about 40% cholesterol
the transport activity of P-glycoprotein is elevated by about 40% cholesterol
the transport activity of P-glycoprotein is elevated by about 40% cholesterol
the transport activity of P-glycoprotein is elevated by about 40% cholesterol
the transport activity of P-glycoprotein is elevated by about 40% cholesterol
the transport activity of P-glycoprotein is elevated by about 40% cholesterol
the transport activity of P-glycoprotein is elevated by about 40% cholesterol
the transport activity of P-glycoprotein is elevated by about 40% cholesterol
the transport activity of P-glycoprotein is elevated by about 40% cholesterol
presence of cholesterol in liposomes increases the binding affinity of small drug substrates with molecular masses below 500 Da, does not affect that of drugs with molecular mass of between 800 and 900 Da, and suppresses that of valinomycin with a molecular mass greater than 1000. Cholesterol enhances paclitaxel-stimulated ATPase activity of enzyme
presence of cholesterol in liposomes increases the binding affinity of small drug substrates with molecular masses below 500 Da, does not affect that of drugs with molecular mass of between 800 and 900 Da, and suppresses that of valinomycin with a molecular mass greater than 1000. Cholesterol enhances paclitaxel-stimulated ATPase activity of enzyme
presence of cholesterol in liposomes increases the binding affinity of small drug substrates with molecular masses below 500 Da, does not affect that of drugs with molecular mass of between 800 and 900 Da, and suppresses that of valinomycin with a molecular mass greater than 1000. Cholesterol enhances paclitaxel-stimulated ATPase activity of enzyme
presence of cholesterol in liposomes increases the binding affinity of small drug substrates with molecular masses below 500 Da, does not affect that of drugs with molecular mass of between 800 and 900 Da, and suppresses that of valinomycin with a molecular mass greater than 1000. Cholesterol enhances paclitaxel-stimulated ATPase activity of enzyme
presence of cholesterol in liposomes increases the binding affinity of small drug substrates with molecular masses below 500 Da, does not affect that of drugs with molecular mass of between 800 and 900 Da, and suppresses that of valinomycin with a molecular mass greater than 1000. Cholesterol enhances paclitaxel-stimulated ATPase activity of enzyme
presence of cholesterol in liposomes increases the binding affinity of small drug substrates with molecular masses below 500 Da, does not affect that of drugs with molecular mass of between 800 and 900 Da, and suppresses that of valinomycin with a molecular mass greater than 1000. Cholesterol enhances paclitaxel-stimulated ATPase activity of enzyme
presence of cholesterol in liposomes increases the binding affinity of small drug substrates with molecular masses below 500 Da, does not affect that of drugs with molecular mass of between 800 and 900 Da, and suppresses that of valinomycin with a molecular mass greater than 1000. Cholesterol enhances paclitaxel-stimulated ATPase activity of enzyme
presence of cholesterol in liposomes increases the binding affinity of small drug substrates with molecular masses below 500 Da, does not affect that of drugs with molecular mass of between 800 and 900 Da, and suppresses that of valinomycin with a molecular mass greater than 1000. Cholesterol enhances paclitaxel-stimulated ATPase activity of enzyme
presence of cholesterol in liposomes increases the binding affinity of small drug substrates with molecular masses below 500 Da, does not affect that of drugs with molecular mass of between 800 and 900 Da, and suppresses that of valinomycin with a molecular mass greater than 1000. Cholesterol enhances paclitaxel-stimulated ATPase activity of enzyme
presence of cholesterol in liposomes increases the binding affinity of small drug substrates with molecular masses below 500 Da, does not affect that of drugs with molecular mass of between 800 and 900 Da, and suppresses that of valinomycin with a molecular mass greater than 1000. Cholesterol enhances paclitaxel-stimulated ATPase activity of enzyme
presence of cholesterol in liposomes increases the binding affinity of small drug substrates with molecular masses below 500 Da, does not affect that of drugs with molecular mass of between 800 and 900 Da, and suppresses that of valinomycin with a molecular mass greater than 1000. Cholesterol enhances paclitaxel-stimulated ATPase activity of enzyme
presence of cholesterol in liposomes increases the binding affinity of small drug substrates with molecular masses below 500 Da, does not affect that of drugs with molecular mass of between 800 and 900 Da, and suppresses that of valinomycin with a molecular mass greater than 1000. Cholesterol enhances paclitaxel-stimulated ATPase activity of enzyme
presence of cholesterol in liposomes increases the binding affinity of small drug substrates with molecular masses below 500 Da, does not affect that of drugs with molecular mass of between 800 and 900 Da, and suppresses that of valinomycin with a molecular mass greater than 1000. Cholesterol enhances paclitaxel-stimulated ATPase activity of enzyme
presence of cholesterol in liposomes increases the binding affinity of small drug substrates with molecular masses below 500 Da, does not affect that of drugs with molecular mass of between 800 and 900 Da, and suppresses that of valinomycin with a molecular mass greater than 1000. Cholesterol enhances paclitaxel-stimulated ATPase activity of enzyme
presence of cholesterol in liposomes increases the binding affinity of small drug substrates with molecular masses below 500 Da, does not affect that of drugs with molecular mass of between 800 and 900 Da, and suppresses that of valinomycin with a molecular mass greater than 1000. Cholesterol enhances paclitaxel-stimulated ATPase activity of enzyme
presence of cholesterol in liposomes increases the binding affinity of small drug substrates with molecular masses below 500 Da, does not affect that of drugs with molecular mass of between 800 and 900 Da, and suppresses that of valinomycin with a molecular mass greater than 1000. Cholesterol enhances paclitaxel-stimulated ATPase activity of enzyme
presence of cholesterol in liposomes increases the binding affinity of small drug substrates with molecular masses below 500 Da, does not affect that of drugs with molecular mass of between 800 and 900 Da, and suppresses that of valinomycin with a molecular mass greater than 1000. Cholesterol enhances paclitaxel-stimulated ATPase activity of enzyme
presence of cholesterol in liposomes increases the binding affinity of small drug substrates with molecular masses below 500 Da, does not affect that of drugs with molecular mass of between 800 and 900 Da, and suppresses that of valinomycin with a molecular mass greater than 1000. Cholesterol enhances paclitaxel-stimulated ATPase activity of enzyme
presence of cholesterol in liposomes increases the binding affinity of small drug substrates with molecular masses below 500 Da, does not affect that of drugs with molecular mass of between 800 and 900 Da, and suppresses that of valinomycin with a molecular mass greater than 1000. Cholesterol enhances paclitaxel-stimulated ATPase activity of enzyme
presence of cholesterol in liposomes increases the binding affinity of small drug substrates with molecular masses below 500 Da, does not affect that of drugs with molecular mass of between 800 and 900 Da, and suppresses that of valinomycin with a molecular mass greater than 1000. Cholesterol enhances paclitaxel-stimulated ATPase activity of enzyme
presence of cholesterol in liposomes increases the binding affinity of small drug substrates with molecular masses below 500 Da, does not affect that of drugs with molecular mass of between 800 and 900 Da, and suppresses that of valinomycin with a molecular mass greater than 1000. Cholesterol enhances paclitaxel-stimulated ATPase activity of enzyme
presence of cholesterol in liposomes increases the binding affinity of small drug substrates with molecular masses below 500 Da, does not affect that of drugs with molecular mass of between 800 and 900 Da, and suppresses that of valinomycin with a molecular mass greater than 1000. Cholesterol enhances paclitaxel-stimulated ATPase activity of enzyme
presence of cholesterol in liposomes increases the binding affinity of small drug substrates with molecular masses below 500 Da, does not affect that of drugs with molecular mass of between 800 and 900 Da, and suppresses that of valinomycin with a molecular mass greater than 1000. Cholesterol enhances paclitaxel-stimulated ATPase activity of enzyme
Inhibitor in Enzyme-catalyzed Reactions (83 results)
EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
addition to a membrane preperation in vitro reduces 5-lipoxygenase activity by half. Cholesterol sulfate can inhibit 5-lipoxygenase in intact cells
-
membranes isolated from mouse brain with endogenous reduced levels of cholesterol due to targeted deletion of one seladin-I allele show a reduced amount of IDE
-
an increased cholesterol level suppresses the expression of 2,3-oxidosqualene cyclase
-
the transport activity of P-glycoprotein decreases by about 20% cholesterol
the transport activity of P-glycoprotein decreases by about 20% cholesterol
the transport activity of P-glycoprotein decreases by about 20% cholesterol
the transport activity of P-glycoprotein decreases by about 20% cholesterol
the transport activity of P-glycoprotein decreases by about 20% cholesterol
the transport activity of P-glycoprotein decreases by about 20% cholesterol
the transport activity of P-glycoprotein decreases by about 20% cholesterol
the transport activity of P-glycoprotein decreases by about 20% cholesterol
the transport activity of P-glycoprotein decreases by about 20% cholesterol
the transport activity of P-glycoprotein decreases by about 20% cholesterol
the transport activity of P-glycoprotein decreases by about 20% cholesterol
the transport activity of P-glycoprotein decreases by about 20% cholesterol
the transport activity of P-glycoprotein decreases by about 20% cholesterol
the transport activity of P-glycoprotein decreases by about 20% cholesterol
the transport activity of P-glycoprotein decreases by about 20% cholesterol
the transport activity of P-glycoprotein decreases by about 20% cholesterol
presence of cholesterol in liposomes increases the binding affinity of small drug substrates with molecular masses below 500 Da, does not affect that of drugs with molecular mass of between 800 and 900 Da, and suppresses that of valinomycin with a molecular mass greater than 1000
presence of cholesterol in liposomes increases the binding affinity of small drug substrates with molecular masses below 500 Da, does not affect that of drugs with molecular mass of between 800 and 900 Da, and suppresses that of valinomycin with a molecular mass greater than 1000
presence of cholesterol in liposomes increases the binding affinity of small drug substrates with molecular masses below 500 Da, does not affect that of drugs with molecular mass of between 800 and 900 Da, and suppresses that of valinomycin with a molecular mass greater than 1000
presence of cholesterol in liposomes increases the binding affinity of small drug substrates with molecular masses below 500 Da, does not affect that of drugs with molecular mass of between 800 and 900 Da, and suppresses that of valinomycin with a molecular mass greater than 1000
presence of cholesterol in liposomes increases the binding affinity of small drug substrates with molecular masses below 500 Da, does not affect that of drugs with molecular mass of between 800 and 900 Da, and suppresses that of valinomycin with a molecular mass greater than 1000
presence of cholesterol in liposomes increases the binding affinity of small drug substrates with molecular masses below 500 Da, does not affect that of drugs with molecular mass of between 800 and 900 Da, and suppresses that of valinomycin with a molecular mass greater than 1000
presence of cholesterol in liposomes increases the binding affinity of small drug substrates with molecular masses below 500 Da, does not affect that of drugs with molecular mass of between 800 and 900 Da, and suppresses that of valinomycin with a molecular mass greater than 1000
presence of cholesterol in liposomes increases the binding affinity of small drug substrates with molecular masses below 500 Da, does not affect that of drugs with molecular mass of between 800 and 900 Da, and suppresses that of valinomycin with a molecular mass greater than 1000
presence of cholesterol in liposomes increases the binding affinity of small drug substrates with molecular masses below 500 Da, does not affect that of drugs with molecular mass of between 800 and 900 Da, and suppresses that of valinomycin with a molecular mass greater than 1000
presence of cholesterol in liposomes increases the binding affinity of small drug substrates with molecular masses below 500 Da, does not affect that of drugs with molecular mass of between 800 and 900 Da, and suppresses that of valinomycin with a molecular mass greater than 1000
presence of cholesterol in liposomes increases the binding affinity of small drug substrates with molecular masses below 500 Da, does not affect that of drugs with molecular mass of between 800 and 900 Da, and suppresses that of valinomycin with a molecular mass greater than 1000
presence of cholesterol in liposomes increases the binding affinity of small drug substrates with molecular masses below 500 Da, does not affect that of drugs with molecular mass of between 800 and 900 Da, and suppresses that of valinomycin with a molecular mass greater than 1000
presence of cholesterol in liposomes increases the binding affinity of small drug substrates with molecular masses below 500 Da, does not affect that of drugs with molecular mass of between 800 and 900 Da, and suppresses that of valinomycin with a molecular mass greater than 1000
presence of cholesterol in liposomes increases the binding affinity of small drug substrates with molecular masses below 500 Da, does not affect that of drugs with molecular mass of between 800 and 900 Da, and suppresses that of valinomycin with a molecular mass greater than 1000
presence of cholesterol in liposomes increases the binding affinity of small drug substrates with molecular masses below 500 Da, does not affect that of drugs with molecular mass of between 800 and 900 Da, and suppresses that of valinomycin with a molecular mass greater than 1000
presence of cholesterol in liposomes increases the binding affinity of small drug substrates with molecular masses below 500 Da, does not affect that of drugs with molecular mass of between 800 and 900 Da, and suppresses that of valinomycin with a molecular mass greater than 1000
presence of cholesterol in liposomes increases the binding affinity of small drug substrates with molecular masses below 500 Da, does not affect that of drugs with molecular mass of between 800 and 900 Da, and suppresses that of valinomycin with a molecular mass greater than 1000
presence of cholesterol in liposomes increases the binding affinity of small drug substrates with molecular masses below 500 Da, does not affect that of drugs with molecular mass of between 800 and 900 Da, and suppresses that of valinomycin with a molecular mass greater than 1000
presence of cholesterol in liposomes increases the binding affinity of small drug substrates with molecular masses below 500 Da, does not affect that of drugs with molecular mass of between 800 and 900 Da, and suppresses that of valinomycin with a molecular mass greater than 1000
presence of cholesterol in liposomes increases the binding affinity of small drug substrates with molecular masses below 500 Da, does not affect that of drugs with molecular mass of between 800 and 900 Da, and suppresses that of valinomycin with a molecular mass greater than 1000
presence of cholesterol in liposomes increases the binding affinity of small drug substrates with molecular masses below 500 Da, does not affect that of drugs with molecular mass of between 800 and 900 Da, and suppresses that of valinomycin with a molecular mass greater than 1000
presence of cholesterol in liposomes increases the binding affinity of small drug substrates with molecular masses below 500 Da, does not affect that of drugs with molecular mass of between 800 and 900 Da, and suppresses that of valinomycin with a molecular mass greater than 1000
presence of cholesterol in liposomes increases the binding affinity of small drug substrates with molecular masses below 500 Da, does not affect that of drugs with molecular mass of between 800 and 900 Da, and suppresses that of valinomycin with a molecular mass greater than 1000
presence of cholesterol in the bilayer modulates the basal and drug-stimulated ATPase activity of reconstituted Pgp in vesicles. Both the ability of drugs to bind to the protein and the drug transport and phospholipid flippase functions of Pgp are also affected by cholesterol. The effects of cholesterol on drug binding affinity are unrelated to the size of the compound. Increasing cholesterol content greatly alters the partitioning of hydrophobic drug substrates into the membrane, which may account for some of the effects of cholesterol on Pgp-mediated drug transport
presence of cholesterol in the bilayer modulates the basal and drug-stimulated ATPase activity of reconstituted Pgp in vesicles. Both the ability of drugs to bind to the protein and the drug transport and phospholipid flippase functions of Pgp are also affected by cholesterol. The effects of cholesterol on drug binding affinity are unrelated to the size of the compound. Increasing cholesterol content greatly alters the partitioning of hydrophobic drug substrates into the membrane, which may account for some of the effects of cholesterol on Pgp-mediated drug transport
presence of cholesterol in the bilayer modulates the basal and drug-stimulated ATPase activity of reconstituted Pgp in vesicles. Both the ability of drugs to bind to the protein and the drug transport and phospholipid flippase functions of Pgp are also affected by cholesterol. The effects of cholesterol on drug binding affinity are unrelated to the size of the compound. Increasing cholesterol content greatly alters the partitioning of hydrophobic drug substrates into the membrane, which may account for some of the effects of cholesterol on Pgp-mediated drug transport
presence of cholesterol in the bilayer modulates the basal and drug-stimulated ATPase activity of reconstituted Pgp in vesicles. Both the ability of drugs to bind to the protein and the drug transport and phospholipid flippase functions of Pgp are also affected by cholesterol. The effects of cholesterol on drug binding affinity are unrelated to the size of the compound. Increasing cholesterol content greatly alters the partitioning of hydrophobic drug substrates into the membrane, which may account for some of the effects of cholesterol on Pgp-mediated drug transport
presence of cholesterol in the bilayer modulates the basal and drug-stimulated ATPase activity of reconstituted Pgp in vesicles. Both the ability of drugs to bind to the protein and the drug transport and phospholipid flippase functions of Pgp are also affected by cholesterol. The effects of cholesterol on drug binding affinity are unrelated to the size of the compound. Increasing cholesterol content greatly alters the partitioning of hydrophobic drug substrates into the membrane, which may account for some of the effects of cholesterol on Pgp-mediated drug transport
presence of cholesterol in the bilayer modulates the basal and drug-stimulated ATPase activity of reconstituted Pgp in vesicles. Both the ability of drugs to bind to the protein and the drug transport and phospholipid flippase functions of Pgp are also affected by cholesterol. The effects of cholesterol on drug binding affinity are unrelated to the size of the compound. Increasing cholesterol content greatly alters the partitioning of hydrophobic drug substrates into the membrane, which may account for some of the effects of cholesterol on Pgp-mediated drug transport
presence of cholesterol in the bilayer modulates the basal and drug-stimulated ATPase activity of reconstituted Pgp in vesicles. Both the ability of drugs to bind to the protein and the drug transport and phospholipid flippase functions of Pgp are also affected by cholesterol. The effects of cholesterol on drug binding affinity are unrelated to the size of the compound. Increasing cholesterol content greatly alters the partitioning of hydrophobic drug substrates into the membrane, which may account for some of the effects of cholesterol on Pgp-mediated drug transport
presence of cholesterol in the bilayer modulates the basal and drug-stimulated ATPase activity of reconstituted Pgp in vesicles. Both the ability of drugs to bind to the protein and the drug transport and phospholipid flippase functions of Pgp are also affected by cholesterol. The effects of cholesterol on drug binding affinity are unrelated to the size of the compound. Increasing cholesterol content greatly alters the partitioning of hydrophobic drug substrates into the membrane, which may account for some of the effects of cholesterol on Pgp-mediated drug transport
presence of cholesterol in the bilayer modulates the basal and drug-stimulated ATPase activity of reconstituted Pgp in vesicles. Both the ability of drugs to bind to the protein and the drug transport and phospholipid flippase functions of Pgp are also affected by cholesterol. The effects of cholesterol on drug binding affinity are unrelated to the size of the compound. Increasing cholesterol content greatly alters the partitioning of hydrophobic drug substrates into the membrane, which may account for some of the effects of cholesterol on Pgp-mediated drug transport
presence of cholesterol in the bilayer modulates the basal and drug-stimulated ATPase activity of reconstituted Pgp in vesicles. Both the ability of drugs to bind to the protein and the drug transport and phospholipid flippase functions of Pgp are also affected by cholesterol. The effects of cholesterol on drug binding affinity are unrelated to the size of the compound. Increasing cholesterol content greatly alters the partitioning of hydrophobic drug substrates into the membrane, which may account for some of the effects of cholesterol on Pgp-mediated drug transport
presence of cholesterol in the bilayer modulates the basal and drug-stimulated ATPase activity of reconstituted Pgp in vesicles. Both the ability of drugs to bind to the protein and the drug transport and phospholipid flippase functions of Pgp are also affected by cholesterol. The effects of cholesterol on drug binding affinity are unrelated to the size of the compound. Increasing cholesterol content greatly alters the partitioning of hydrophobic drug substrates into the membrane, which may account for some of the effects of cholesterol on Pgp-mediated drug transport
presence of cholesterol in the bilayer modulates the basal and drug-stimulated ATPase activity of reconstituted Pgp in vesicles. Both the ability of drugs to bind to the protein and the drug transport and phospholipid flippase functions of Pgp are also affected by cholesterol. The effects of cholesterol on drug binding affinity are unrelated to the size of the compound. Increasing cholesterol content greatly alters the partitioning of hydrophobic drug substrates into the membrane, which may account for some of the effects of cholesterol on Pgp-mediated drug transport
presence of cholesterol in the bilayer modulates the basal and drug-stimulated ATPase activity of reconstituted Pgp in vesicles. Both the ability of drugs to bind to the protein and the drug transport and phospholipid flippase functions of Pgp are also affected by cholesterol. The effects of cholesterol on drug binding affinity are unrelated to the size of the compound. Increasing cholesterol content greatly alters the partitioning of hydrophobic drug substrates into the membrane, which may account for some of the effects of cholesterol on Pgp-mediated drug transport
presence of cholesterol in the bilayer modulates the basal and drug-stimulated ATPase activity of reconstituted Pgp in vesicles. Both the ability of drugs to bind to the protein and the drug transport and phospholipid flippase functions of Pgp are also affected by cholesterol. The effects of cholesterol on drug binding affinity are unrelated to the size of the compound. Increasing cholesterol content greatly alters the partitioning of hydrophobic drug substrates into the membrane, which may account for some of the effects of cholesterol on Pgp-mediated drug transport
presence of cholesterol in the bilayer modulates the basal and drug-stimulated ATPase activity of reconstituted Pgp in vesicles. Both the ability of drugs to bind to the protein and the drug transport and phospholipid flippase functions of Pgp are also affected by cholesterol. The effects of cholesterol on drug binding affinity are unrelated to the size of the compound. Increasing cholesterol content greatly alters the partitioning of hydrophobic drug substrates into the membrane, which may account for some of the effects of cholesterol on Pgp-mediated drug transport
presence of cholesterol in the bilayer modulates the basal and drug-stimulated ATPase activity of reconstituted Pgp in vesicles. Both the ability of drugs to bind to the protein and the drug transport and phospholipid flippase functions of Pgp are also affected by cholesterol. The effects of cholesterol on drug binding affinity are unrelated to the size of the compound. Increasing cholesterol content greatly alters the partitioning of hydrophobic drug substrates into the membrane, which may account for some of the effects of cholesterol on Pgp-mediated drug transport
presence of cholesterol in the bilayer modulates the basal and drug-stimulated ATPase activity of reconstituted Pgp in vesicles. Both the ability of drugs to bind to the protein and the drug transport and phospholipid flippase functions of Pgp are also affected by cholesterol. The effects of cholesterol on drug binding affinity are unrelated to the size of the compound. Increasing cholesterol content greatly alters the partitioning of hydrophobic drug substrates into the membrane, which may account for some of the effects of cholesterol on Pgp-mediated drug transport
presence of cholesterol in the bilayer modulates the basal and drug-stimulated ATPase activity of reconstituted Pgp in vesicles. Both the ability of drugs to bind to the protein and the drug transport and phospholipid flippase functions of Pgp are also affected by cholesterol. The effects of cholesterol on drug binding affinity are unrelated to the size of the compound. Increasing cholesterol content greatly alters the partitioning of hydrophobic drug substrates into the membrane, which may account for some of the effects of cholesterol on Pgp-mediated drug transport
presence of cholesterol in the bilayer modulates the basal and drug-stimulated ATPase activity of reconstituted Pgp in vesicles. Both the ability of drugs to bind to the protein and the drug transport and phospholipid flippase functions of Pgp are also affected by cholesterol. The effects of cholesterol on drug binding affinity are unrelated to the size of the compound. Increasing cholesterol content greatly alters the partitioning of hydrophobic drug substrates into the membrane, which may account for some of the effects of cholesterol on Pgp-mediated drug transport
presence of cholesterol in the bilayer modulates the basal and drug-stimulated ATPase activity of reconstituted Pgp in vesicles. Both the ability of drugs to bind to the protein and the drug transport and phospholipid flippase functions of Pgp are also affected by cholesterol. The effects of cholesterol on drug binding affinity are unrelated to the size of the compound. Increasing cholesterol content greatly alters the partitioning of hydrophobic drug substrates into the membrane, which may account for some of the effects of cholesterol on Pgp-mediated drug transport
presence of cholesterol in the bilayer modulates the basal and drug-stimulated ATPase activity of reconstituted Pgp in vesicles. Both the ability of drugs to bind to the protein and the drug transport and phospholipid flippase functions of Pgp are also affected by cholesterol. The effects of cholesterol on drug binding affinity are unrelated to the size of the compound. Increasing cholesterol content greatly alters the partitioning of hydrophobic drug substrates into the membrane, which may account for some of the effects of cholesterol on Pgp-mediated drug transport
presence of cholesterol in the bilayer modulates the basal and drug-stimulated ATPase activity of reconstituted Pgp in vesicles. Both the ability of drugs to bind to the protein and the drug transport and phospholipid flippase functions of Pgp are also affected by cholesterol. The effects of cholesterol on drug binding affinity are unrelated to the size of the compound. Increasing cholesterol content greatly alters the partitioning of hydrophobic drug substrates into the membrane, which may account for some of the effects of cholesterol on Pgp-mediated drug transport
presence of cholesterol in the bilayer modulates the basal and drug-stimulated ATPase activity of reconstituted Pgp in vesicles. Both the ability of drugs to bind to the protein and the drug transport and phospholipid flippase functions of Pgp are also affected by cholesterol. The effects of cholesterol on drug binding affinity are unrelated to the size of the compound. Increasing cholesterol content greatly alters the partitioning of hydrophobic drug substrates into the membrane, which may account for some of the effects of cholesterol on Pgp-mediated drug transport
3D Structure of Enzyme-Ligand-Complex (PDB) (979 results)
EC NUMBER
ENZYME 3D STRUCTURE
Enzyme Kinetic Parameters
kcat Value (Turnover Number) (91 results)
EC NUMBER
TURNOVER NUMBER [1/S]
TURNOVER NUMBER MAXIMUM [1/S]
COMMENTARY
LITERATURE
0.035
-
apparent value, mutant enzyme N485L, pH 5.1, temperature not specified in the publication
0.044
-
apparent value, mutant enzyme N485L, pH 7.0, temperature not specified in the publication
0.073
-
apparent value, mutant enzyme N485D, pH 7.0, temperature not specified in the publication
0.55
-
H69A mutant enzyme, steady state, 50 mM phosphate buffer, 1% thesit, 1% 2-propanol
0.8
-
assay relies on spectroscopic detection of 4-cholesten-3-one formation, decreasing length of C17 chain affects turnover negatively
1.4
-
apparent value, mutant enzyme N485D, pH 5.1, temperature not specified in the publication
1.6
-
H69A mutant enzyme, cholesterol oxidation, 50 mM phosphate buffer, 1% thesit, 1% 2-propanol
3
-
substrate cholesterol, polarographic determination of the rate of oxygen consumption. 1% thesit (polyoxyethylene(9)-lauryl-ether), 10% propan-2-ol and 50 mM phosphate, 25°C and pH 7.5
6
-
substrate cholesterol, polarographic determination of the rate of oxygen consumption. 1% thesit (polyoxyethylene(9)-lauryl-ether), 10% propan-2-ol and 50 mM phosphate, 25°C and pH 7.5
9
-
substrate cholesterol, polarographic determination of the rate of oxygen consumption. 0.5 M potassium phosphate, 1% thesit (polyoxyethylene(9)-lauryl-ether), 1.25% propan-2-ol, 25°C and pH 7.5
11
-
substrate cholesterol, detection of product formation (cholest-4-en-3-one) at 240 nm. 0.5 M potassium phosphate, 1% thesit (polyoxyethylene(9)-lauryl-ether), 1.25% propan-2-ol, 25°C and pH 7.5
23
-
pH 7.0, 37°C, mutant enzyme A32C/S129C/T371C/A423C, cholesterol solubilized in detergent micelles as a substrate
30
-
pH 7.0, 37°C, mutant enzyme A32C/T168C/S312C/A465C, cholesterol solubilized in detergent micelles as a substrate
32
-
substrate cholesterol, rate of H2O2 formation detected with o-dianisidine and horseradish peroxidase. 0.1 M potassium phosphate, 1% Triton X-100, 1.25% propan-2-ol, 25°C and pH 7.5
43
-
substrate cholesterol, polarographic determination of the rate of oxygen consumption. 1% thesit (polyoxyethylene(9)-lauryl-ether), 10% propan-2-ol and 50 mM phosphate, 25°C and pH 7.5
46
-
apparent value, wild type enzyme, pH 5.1, temperature not specified in the publication
46
-
pH 7.0, 37°C, mutant enzyme T168C/A276C, cholesterol solubilized in detergent micelles as a substrate
47
-
apparent value, wild type enzyme, pH 7.0, temperature not specified in the publication
48
-
substrate cholesterol, detection of product formation (cholest-4-en-3-one) at 240 nm. 0.1 M potassium phosphate, 1% Triton X-100, 1.25% propan-2-ol, 25°C and pH 7.5
48
-
substrate cholesterol, rate of H2O2 formation detected with o-dianisidine and horseradish peroxidase. 0.1 M potassium phosphate, 1% Triton X-100, 1.25% propan-2-ol, 25°C and pH 7.5
48.1
-
product formation followed at 240 nm in the presence of 0.02 ml H2O2, substrate dissolved in Triton X-100, 100 mM phosphate buffer
56
-
substrate cholesterol, polarographic determination of the rate of oxygen consumption. 0.5 M potassium phosphate, 1% thesit (polyoxyethylene(9)-lauryl-ether), 1.25% propan-2-ol, 25°C and pH 7.5
57
-
pH 7.0, 37°C, mutant enzyme A184C/A301C/T394C, cholesterol solubilized in detergent micelles as a substrate
57
-
substrate cholesterol, polarographic determination of the rate of oxygen consumption. 1% thesit (polyoxyethylene(9)-lauryl-ether), 10% propan-2-ol and 50 mM phosphate, 25°C and pH 7.5
60
-
pH 7.0, 37°C, mutant enzyme A184C/T239C/A407C/A465C, cholesterol solubilized in detergent micelles as a substrate
63
-
product formation followed at 240 nm in the presence of 0.02 ml H2O2, substrate dissolved in Triton X-100, 100 mM phosphate buffer
63
-
substrate cholesterol, detection of product formation (cholest-4-en-3-one) at 240 nm. 0.1 M potassium phosphate, 1% Triton X-100, 1.25% propan-2-ol, 25°C and pH 7.5
67
-
pH 7.0, 37°C, wild-type enzyme, cholesterol solubilized in detergent micelles as a substrate
67
-
substrate cholesterol, detection of product formation (cholest-4-en-3-one) at 240 nm. 0.5 M potassium phosphate, 1% thesit (polyoxyethylene(9)-lauryl-ether), 1.25% propan-2-ol, 25°C and pH 7.5
68
-
pH 7.0, 37°C, mutant enzyme S153C/A205C/S312C/T435C, cholesterol solubilized in detergent micelles as a substrate
75
-
pH 7.0, 37°C, mutant enzyme L274C, cholesterol solubilized in detergent micelles as a substrate
89
-
pH 7.0, 37°C, mutant enzyme L80C, cholesterol solubilized in detergent micelles as a substrate
KM Value (141 results)
EC NUMBER
KM VALUE [MM]
KM VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
0.0027
-
apparent value, wild type enzyme, pH 7.0, temperature not specified in the publication
0.0046
-
apparent value, mutant enzyme N485L, pH 7.0, temperature not specified in the publication
0.0062
-
apparent value, mutant enzyme N485L, pH 5.1, temperature not specified in the publication
0.0063
-
apparent value, mutant enzyme N485D, pH 5.1, temperature not specified in the publication
0.0066
-
apparent value, mutant enzyme N485D, pH 7.0, temperature not specified in the publication
0.0067
-
apparent value, wild type enzyme, pH 5.1, temperature not specified in the publication
0.01
-
pH 7.0, 37°C, mutant enzyme S153C/A205C/S312C/T435C, cholesterol solubilized in detergent micelles as a substrate
0.011
-
pH 7.0, 37°C, mutant enzyme A184C/A301C/T394C, cholesterol solubilized in detergent micelles as a substrate
0.011
-
pH 7.0, 37°C, mutant enzyme A32C/S129C/T371C/A423C, cholesterol solubilized in detergent micelles as a substrate
0.011
-
pH 7.0, 37°C, mutant enzyme L80C, cholesterol solubilized in detergent micelles as a substrate
0.012
-
pH 7.0, 37°C, mutant enzyme A32C/T168C/S312C/A465C, cholesterol solubilized in detergent micelles as a substrate
0.013
-
Km increases when enzyme is entrapped in reverse micelles of the synthetic surfactant aerosol-OT-isooctane
0.013
-
pH 7.0, 37°C, mutant enzyme A184C/T239C/A407C/A465C, cholesterol solubilized in detergent micelles as a substrate
0.013
-
pH 7.0, 37°C, wild-type enzyme, cholesterol solubilized in detergent micelles as a substrate
0.014
-
pH 7.0, 37°C, mutant enzyme T168C/A276C, cholesterol solubilized in detergent micelles as a substrate
0.017
-
pH 7.0, 37°C, mutant enzyme L274C, cholesterol solubilized in detergent micelles as a substrate
0.04
-
substrate cholesterol, rate of H2O2 formation detected with o-dianisidine and horseradish peroxidase. 0.1 M potassium phosphate, 1% Triton X-100, 1.25% propan-2-ol, 25°C and pH 7.5
0.07
-
substrate cholesterol, detection of product formation (cholest-4-en-3-one) at 240 nm. 0.1 M potassium phosphate, 1% Triton X-100, 1.25% propan-2-ol, 25°C and pH 7.5
0.0962
-
enzyme from cultured immobilized cells, pH and temperature not specified in the publication
0.1013
-
enzyme from cultured free cells, pH and temperature not specified in the publication
0.11
-
substrate cholesterol, polarographic determination of the rate of oxygen consumption. 0.5 M potassium phosphate, 1% thesit (polyoxyethylene(9)-lauryl-ether), 1.25% propan-2-ol, 25°C and pH 7.5
0.14
-
substrate cholesterol, detection of product formation (cholest-4-en-3-one) at 240 nm. 0.5 M potassium phosphate, 1% thesit (polyoxyethylene(9)-lauryl-ether), 1.25% propan-2-ol, 25°C and pH 7.5
0.17
-
substrate cholesterol, polarographic determination of the rate of oxygen consumption. 1% thesit (polyoxyethylene(9)-lauryl-ether), 10% propan-2-ol and 50 mM phosphate, 25°C and pH 7.5
0.2
-
substrate cholesterol, detection of product formation (cholest-4-en-3-one) at 240 nm. 0.5 M potassium phosphate, 1% thesit (polyoxyethylene(9)-lauryl-ether), 1.25% propan-2-ol, 25°C and pH 7.5
0.2
-
substrate cholesterol, polarographic determination of the rate of oxygen consumption. 1% thesit (polyoxyethylene(9)-lauryl-ether), 10% propan-2-ol and 50 mM phosphate, 25°C and pH 7.5
0.2123
-
apparent value, free enzyme, in 50 mM potassium phosphate buffer, pH 7.5, 30°C
0.25
-
substrate cholesterol, polarographic determination of the rate of oxygen consumption. 0.5 M potassium phosphate, 1% thesit (polyoxyethylene(9)-lauryl-ether), 1.25% propan-2-ol, 25°C and pH 7.5
0.25
-
substrate cholesterol, polarographic determination of the rate of oxygen consumption. 1% thesit (polyoxyethylene(9)-lauryl-ether), 10% propan-2-ol and 50 mM phosphate, 25°C and pH 7.5
0.2599
-
apparent value, silk mat-immobilized enzyme, in 50 mM potassium phosphate buffer, pH 7.5, 30°C
0.4
-
substrate cholesterol, rate of H2O2 formation detected with o-dianisidine and horseradish peroxidase. 0.1 M potassium phosphate, 1% Triton X-100, 1.25% propan-2-ol, 25°C and pH 7.5
0.8
-
substrate cholesterol, detection of product formation (cholest-4-en-3-one) at 240 nm. 0.1 M potassium phosphate, 1% Triton X-100, 1.25% propan-2-ol, 25°C and pH 7.5
Ki Value (1 result)
IC50 Value (2 results)
EC NUMBER
IC50 VALUE
IC50 VALUE MAXIMUM
COMMENTARY
LITERATURE
References & Links
Literature References (575)
Links to other databases for cholesterol
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