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Information on EC 5.3.3.5 - cholestenol DELTA-isomerase and Organism(s) Homo sapiens and UniProt Accession Q15125
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5.3.3.5 cholestenol DELTA-isomeraseSpecify your search results
Word Map
- 5.3.3.5
- ebp
-
x-linked
-
chondrodysplasia
- punctata
-
stipple
-
sigma1
-
epiphyseal
-
x-inactivation
- 8-dehydrocholesterol
- nsdhl
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
emopamil binding protein, emopamil-binding protein, delta8-delta7 sterol isomerase, c-8,7 sterol isomerase, erg2p, delta8-delta7 isomerase, d8d7i, 8,7si, cholestenol delta-isomerase, d8-d7 sterol isomerase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Cholestenol delta-isomerase
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D8-D7 sterol isomerase
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DELTA8-Cholestenol-DELTA7-cholestenol isomerase
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Delta8-delta7 sterol isomerase
Emopamil binding protein
Isomerase, cholestenol DELTA-
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Delta8-delta7 sterol isomerase
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Emopamil binding protein
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
isomerization
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intramolecular oxidoreduction
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PATHWAY SOURCE
PATHWAYS
BRENDA
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-, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
DELTA7-Cholestenol DELTA7-DELTA8-isomerase
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CAS REGISTRY NUMBER
COMMENTARY
37318-47-1
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
26,27-dinorcholesta-8,24-dienol
26,27-dinorcholesta-7,24-dienol
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?
26-homo-cholesta-8(9),23(24) E26(26')-trienol
26-homo-cholesta-7(8),23(24)E26(26')trienol
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?
5alpha-cholesta-8,24-dien-3beta-ol
5alpha-cholesta-7,24-dien-3beta-ol
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?
zymosterol
cholesta-7,24-dienol
preferred substrate for DELTA7-sterol production, the reaction equilibrium for double-bond isomerization favours the forward direction, DELTA8 to DELTA7
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r
additional information
?
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3-desoxyzymosterol is not an active substrate
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?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1'R,3a'R,7a'R,1''R)-5-(N-benzylpiperidin-4-yl)-aminomethyl-7a'-methyl-1'-(1,5-dimethylhexyl)-5-nitrospiro[1,3-dioxane-2,4'-octahydroindene]
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(1'R,3a'R,7a'R,1''R)-5-(N-benzylpiperidin-4-yl)-N-methylaminomethyl-7a'-methyl-1'-(1,5-dimethylhexyl)-5-nitrospiro[1,3-dioxane-2,4'-octahydroindene]
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(1'R,3a'R,7a'R,1''R)-7a'-methyl-1'-(1,5-dimethylhexyl)-5-nitro-5-[[2-(pyrrolidin-1yl)ethyl]aminomethyl]spiro[1,3-dioxane-2,4'-octahydroindene]
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(1'R,3a'R,7a'R,1''R)-7a'-methyl-5-[N-(N,N-dimethylaminoeth-2-yl-aminomethyl)-1'-(1,5-dimethylhexyl)-5-nitrospiro[1,3-dioxane-2,4'-octahydroindene]]
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(1R,3aR,4R,5S,7aR)-3a,7a-dimethyl-1-(6-methylheptan-2-yl)-5-(pent-4-en-1-ylamino)octahydro-1H-inden-4-ol
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(1R,3aR,4R,5S,7aR)-3a,7a-dimethyl-1-(6-methylheptan-2-yl)-5-[methyl(pent-4-en-1-yl)amino]octahydro-1H-inden-4-ol
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(1R,3aR,4R,5S,7aR)-5-(benzylamino)-3a,7a-dimethyl-1-(6-methylheptan-2-yl)octahydro-1H-inden-4-ol
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(1R,3aR,4R,5S,7aR)-5-(dibenzylamino)-3a,7a-dimethyl-1-(6-methylheptan-2-yl)octahydro-1H-inden-4-ol
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(1R,3aR,4R,5S,7aR)-5-amino-3a,7a-dimethyl-1-(6-methylheptan-2-yl)octahydro-1H-inden-4-ol
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(1R,3aR,4R,5S,7aR)-5-[benzyl(methyl)amino]-3a,7a-dimethyl-1-(6-methylheptan-2-yl)octahydro-1H-inden-4-ol
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(1R,3aR,4R,5S,7aR)-5-[benzyl(pent-4-en-1-yl)amino]-3a,7a-dimethyl-1-(6-methylheptan-2-yl)octahydro-1H-inden-4-ol
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(1R,3aR,5S,7aR)-5-(dimethylamino)-3a,7a-dimethyl-1-(6-methylheptan-2-yl)octahydro-1H-inden-4-ol
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(R,S)-1-cyclohexyl-4-[3-(5-methoxy-1,2,3,4-tetrahydronaphthalen-1-yl)-n-propyl]piperazine
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1',2',3',4'-tetrahydro-5-(N-benzylpiperidin-4-yl)-aminomethyl-5-nitro-6'-(4-methylpentyloxy)-spiro[1,3-dioxane-2,1'-naphthaline]
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1',2',3',4'-tetrahydro-5-(N-benzylpiperidin-4-yl)-aminomethyl-6'-methoxy-5-nitrospiro[1,3-dioxane-2,1'-naphthaline]
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1-[(6-methoxy-1,2,3,4-tetrahydronaphthalen-2-yl)methyl]-4-pyridin-2-ylpiperazine
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(+)-pentazocine
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i.e. (+)-[2S-(2R,6R,11R)]-1,2,3,4,5,6-hexahydro-6,11-dimethyl-3-(3-methyl-2-butenyl)-2,6-methano-3-benzazocine-8-ol
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000016
1-cyclohexyl-4-[cis-4-(2,6-difluorophenyl)cyclohexyl]piperazine
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pH and temperature not specified in the publication
0.0000076
1-cyclohexyl-4-[cis-4-(2,6-dimethoxyphenyl)cyclohexyl]piperazine
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pH and temperature not specified in the publication
0.0000041
1-cyclohexyl-4-[cis-4-(2-methoxyphenyl)cyclohexyl]piperazine
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pH and temperature not specified in the publication
0.000009
1-cyclohexyl-4-[cis-4-(2-methylphenyl)cyclohexyl]piperazine
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pH and temperature not specified in the publication
0.00000651
1-cyclohexyl-4-[cis-4-(4-methoxyphenyl)cyclohexyl]piperazine
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pH and temperature not specified in the publication
0.000018
1-cyclohexyl-4-[trans-4-(2,6-difluorophenyl)cyclohexyl]piperazine
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pH and temperature not specified in the publication
0.000011
1-cyclohexyl-4-[trans-4-(2,6-dimethoxyphenyl)cyclohexyl]piperazine
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pH and temperature not specified in the publication
0.0000107
1-cyclohexyl-4-[trans-4-(2-methoxyphenyl)cyclohexyl]piperazine
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pH and temperature not specified in the publication
0.00000973
1-cyclohexyl-4-[trans-4-(2-methylphenyl)cyclohexyl]piperazine
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pH and temperature not specified in the publication
0.0000136
1-cyclohexyl-4-[trans-4-(4-methoxyphenyl)cyclohexyl]piperazine
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pH and temperature not specified in the publication
0.0000321
1-[(6-methoxy-1,2,3,4-tetrahydronaphthalen-2-yl)methyl]-4-pyridin-2-ylpiperazine
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0.0000169
1-[cis-4-(2-chlorophenyl)cyclohexyl]-4-cyclohexylpiperazine
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pH and temperature not specified in the publication
0.0000206
1-[trans-4-(2-chlorophenyl)cyclohexyl]-4-cyclohexylpiperazine
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pH and temperature not specified in the publication
0.0000167
3-[4-(4-naphthalen-1-ylpiperazin-1-yl)cyclohexyl]phenyl hydroperoxide
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0.0000467
4-[1-(2,6-dimethylphenyl)-3-cyclohexen-4-yl]-1-(2-pyridinyl)piperazine
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0.0000123
cis-1-cyclohexyl-4-(4-phenylcyclohexyl)piperazine
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pH and temperature not specified in the publication
0.0000126
cis-1-cyclohexyl-4-[(3-methoxyphenyl)cyclohexyl]piperazine
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pH and temperature not specified in the publication
0.0000331
cis-4-[4-(2,6-dimethylyphenyl)cyclohexyl]-1-(2-pyridinyl)piperazine
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0.0000142
trans-1-cyclohexyl-4-(4-phenylcyclohexyl)piperazine
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pH and temperature not specified in the publication
0.0000004
trans-1-cyclohexyl-4-[(3-methoxyphenyl)cyclohexyl]piperazine
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pH and temperature not specified in the publication
0.000106
trans-4-[4-(2,6-difluorophenyl)cyclohexyl]-1-(2-pyridinyl)piperazine
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0.000007
trans-4-[4-(2,6-dimethoxyphenyl)cyclohexyl]-1-(2-pyridinyl)piperazine
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0.0000147
(+/-)-ifenprodil
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pH and temperature not specified in the publication
0.00000495
cis-4-[4-(2,6-dimethoxyphenyl)cyclohexyl]-1-(2-pyridinyl)piperazine
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0.00000495
cis-4-[4-(2,6-dimethoxyphenyl)cyclohexyl]-1-(2-pyridinyl)piperazine
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pH and temperature not specified in the publication
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0017
(1'R,3a'R,7a'R,1''R)-5-(N-benzylpiperidin-4-yl)-aminomethyl-7a'-methyl-1'-(1,5-dimethylhexyl)-5-nitrospiro[1,3-dioxane-2,4'-octahydroindene]
Homo sapiens
-
pH and temperature not specified in the publication
0.0047
(1'R,3a'R,7a'R,1''R)-5-(N-benzylpiperidin-4-yl)-N-methylaminomethyl-7a'-methyl-1'-(1,5-dimethylhexyl)-5-nitrospiro[1,3-dioxane-2,4'-octahydroindene]
Homo sapiens
-
pH and temperature not specified in the publication
0.0045
1',2',3',4'-tetrahydro-5-(N-benzylpiperidin-4-yl)-aminomethyl-5-nitro-6'-(4-methylpentyloxy)-spiro[1,3-dioxane-2,1'-naphthaline]
Homo sapiens
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pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). EBP_HUMAN
230
5
26353
Swiss-Prot
other Location (Reliability: 5)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C121A
mutant enzyme with 95% of the in vivo activity of the wild-type enzyme
C128A
mutant enzyme with 81% of the in vivo activity of the wild-type enzyme
C68A
mutant enzyme with 94% of the in vivo activity of the wild-type enzyme
C73A
mutant enzyme with 83% of the in vivo activity of the wild-type enzyme
E123A
mutant enzyme with 10% of the in vivo activity of the wild-type enzyme
E81A
mutant enzyme with 5% of the in vivo activity of the wild-type enzyme
F186A
mutant enzyme with 56% of the in vivo activity of the wild-type enzyme
F188A
mutant enzyme with 94% of the in vivo activity of the wild-type enzyme
F190A
mutant enzyme with 21% of the in vivo activity of the wild-type enzyme
F192A
mutant enzyme with 92% of the in vivo activity of the wild-type enzyme
F37A
mutant enzyme with 74% of the in vivo activity of the wild-type enzyme
F70A
mutant enzyme with 95% of the in vivo activity of the wild-type enzyme
F75A
mutant enzyme with 88% of the in vivo activity of the wild-type enzyme
F84A
mutant enzyme with 72% of the in vivo activity of the wild-type enzyme
G131A
mutant enzyme with 69% of the in vivo activity of the wild-type enzyme
G41A
mutant enzyme with 94% of the in vivo activity of the wild-type enzyme
G82A/F84V
mutant enzyme with 56% of the in vivo activity of the wild-type enzyme
H31A
mutant enzyme with 69% of the in vivo activity of the wild-type enzyme
H77A
mutant enzyme with 9% of the in vivo activity of the wild-type enzyme
I125A
mutant enzyme with 78% of the in vivo activity of the wild-type enzyme
I139A
mutant enzyme with 90% of the in vivo activity of the wild-type enzyme
I32A
mutant enzyme with 73% of the in vivo activity of the wild-type enzyme
I76A
mutant enzyme with 33% of the in vivo activity of the wild-type enzyme
I76L/L78A
mutant enzyme with 74% of the in vivo activity of the wild-type enzyme
L129A
mutant enzyme with 81% of the in vivo activity of the wild-type enzyme
L133A
mutant enzyme with 77% of the in vivo activity of the wild-type enzyme
L135A
mutant enzyme with 92% of the in vivo activity of the wild-type enzyme
L196A
mutant enzyme with 62% of the in vivo activity of the wild-type enzyme
L198A
mutant enzyme with 50% of the in vivo activity of the wild-type enzyme
L204A
mutant enzyme with 77% of the in vivo activity of the wild-type enzyme
L33A
mutant enzyme with 47% of the in vivo activity of the wild-type enzyme
L35A
mutant enzyme with 62% of the in vivo activity of the wild-type enzyme
L43A
mutant enzyme with 103% of the in vivo activity of the wild-type enzyme
L49A
mutant enzyme with 108% of the in vivo activity of the wild-type enzyme
L50A
mutant enzyme with 96% of the in vivo activity of the wild-type enzyme
L65A
mutant enzyme with 82% of the in vivo activity of the wild-type enzyme
L67A
mutant enzyme with 63% of the in vivo activity of the wild-type enzyme
M122A
mutant enzyme with 28% of the in vivo activity of the wild-type enzyme
M193A
mutant enzyme with 53% of the in vivo activity of the wild-type enzyme
S134A
mutant enzyme with 101% of the in vivo activity of the wild-type enzyme
S38A
mutant enzyme with 74% of the in vivo activity of the wild-type enzyme
T124A
mutant enzyme with 91% of the in vivo activity of the wild-type enzyme
T126A
mutant enzyme with 4% of the in vivo activity of the wild-type enzyme
V120A
mutant enzyme with 62% of the in vivo activity of the wild-type enzyme
V138A
mutant enzyme with 94% of the in vivo activity of the wild-type enzyme
V191A
mutant enzyme with 91% of the in vivo activity of the wild-type enzyme
V199A
mutant enzyme with 76% of the in vivo activity of the wild-type enzyme
V203A
mutant enzyme with 71% of the in vivo activity of the wild-type enzyme
V39A
mutant enzyme with 80% of the in vivo activity of the wild-type enzyme
V44A
mutant enzyme with 76% of the in vivo activity of the wild-type enzyme
V45A
mutant enzyme with 79% of the in vivo activity of the wild-type enzyme
V72A
mutant enzyme with 93% of the in vivo activity of the wild-type enzyme
V79A
mutant enzyme with 75% of the in vivo activity of the wild-type enzyme
V85A
mutant enzyme with 68% of the in vivo activity of the wild-type enzyme
W130A
mutant enzyme with 70% of the in vivo activity of the wild-type enzyme
W136A
mutant enzyme with 104% of the in vivo activity of the wild-type enzyme
W187A
mutant enzyme with 56% of the in vivo activity of the wild-type enzyme
W197A
mutant enzyme with 5% of the in vivo activity of the wild-type enzyme
W48A
mutant enzyme with 87% of the in vivo activity of the wild-type enzyme
W69A
mutant enzyme with 17% of the in vivo activity of the wild-type enzyme
W83A
mutant enzyme with 97% of the in vivo activity of the wild-type enzyme
Y185A
mutant enzyme with 64% of the in vivo activity of the wild-type enzyme
Y189A
mutant enzyme with 32% of the in vivo activity of the wild-type enzyme
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
coexpression of D8D7I and DHCR7 in COS-7 cells produces a high affinity binding site for tritiated tamoxifen that displays the pharmacological profile of the antiestrogen binding site found in tumor cells
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nes, W.D.; Zhou, W.; Dennis, A.L.; Li, H.; Jia, Z.; Keith, R.A.; Piser, T.M.; Furlong, S.T.
Purification, characterization and catalytic properties of human sterol 8-isomerase
Biochem. J.
367
587-599
2002
Homo sapiens (Q15125)
Moebius, F.F.; Soellner, K.E.M.; Fiechtner, B.; Huck, C.W.; Bonn, G.; Glossmann, H.
Histidine77, glutamic acid81, glutamic acid123, threonine126, asparagine194, and tryptophan197 of the human emopamil binding protein are required for in vivo sterol DELTA8-DELTA7 isomerization
Biochemistry
38
1119-1127
1999
Homo sapiens (Q15125), Homo sapiens
Moebius, F.F.; Reiter, R.J.; Bermoser, K.; Glossmann, H.; Cho, S.Y.; Paik, Y.K.
Pharmacological analysis of sterol DELTA8-DELTA7-isomerase proteins with [3H]ifenprodil
Mol. Pharmacol.
54
591-598
1998
Cavia porcellus (Q60490), Homo sapiens (Q15125), Homo sapiens, Mus musculus (P70245), Saccharomyces cerevisiae
Kedjouar, B.; de Medina, P.; Oulad-Abdelghani, M.; Payre, B.; Silvente-Poirot, S.; Favre, G.; Faye, J.C.; Poirot, M.
Molecular characterization of the microsomal tamoxifen binding site
J. Biol. Chem.
279
34048-34061
2004
Homo sapiens
Berardi, F.; Abate, C.; Ferorelli, S.; de Robertis, A.F.; Leopoldo, M.; Colabufo, N.A.; Niso, M.; Perrone, R.
Novel 4-(4-aryl)cyclohexyl-1-(2-pyridyl)piperazines as DELTA8-DELTA7 sterol isomerase (emopamil binding protein) selective ligands with antiproliferative activity
J. Med. Chem.
51
7523-7531
2008
Homo sapiens
Abate, C.; Niso, M.; Contino, M.; Colabufo, N.A.; Ferorelli, S.; Perrone, R.; Berardi, F.
1-Cyclohexyl-4-(4-arylcyclohexyl)piperazines: Mixed sigma and human DELTA8-DELTA7 sterol isomerase ligands with antiproliferative and P-glycoprotein inhibitory activity
ChemMedChem
6
73-80
2011
Homo sapiens
Krojer, M.; Mueller, C.; Bracher, F.
Steroidomimetic aminomethyl spiroacetals as novel inhibitors of the enzyme DELTA8,7-sterol isomerase in cholesterol biosynthesis
Arch. Pharm.
347
108-122
2014
Homo sapiens
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