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Information on EC 5.3.3.5 - cholestenol DELTA-isomerase
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EC Tree
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 enzyme appears in 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, d8-d7 sterol isomerase, cholestenol delta-isomerase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
8,7SI
Cholestenol delta-isomerase
-
-
-
-
D8-D7 sterol isomerase
-
-
-
-
DELTA8,7-sterol isomerase
DELTA8-Cholestenol-DELTA7-cholestenol isomerase
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-
-
-
DELTA8-DELTA7 isomerase
Delta8-delta7 sterol isomerase
EBP
Emopamil binding protein
emopamil-binding protein
Isomerase, cholestenol DELTA-
-
-
-
-
sterol 8,7-isomerase
Delta8-delta7 sterol isomerase
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-
-
-
Emopamil binding protein
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
5alpha-Cholest-7-en-3beta-ol = 5alpha-cholest-8-en-3beta-ol
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
intramolecular oxidoreduction
-
-
-
-
isomerization
-
-
-
-
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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
-
-
?
26-homo-cholesta-8(9),23(24) E26(26')-trienol
26-homo-cholesta-7(8),23(24)E26(26')trienol
-
-
?
4alpha-methyl-5alpha-ergosta-8,24-dien-3beta-ol
24-methylenelophenol
-
-
i.e. 4alpha-methyl-5alpha-ergosta-7,24-dien-3beta-ol
-
?
5alpha-cholest-7-en-3beta-ol
?
enzyme of the cholesterol biosynthetic pathway, mutations are associated with Conradi-Huenermann syndrome. The enzyme may be involved in liver function, since the mRNA is only detected in hepatocytes not in connective tissue or blood vessels. The expression of the SI gene is regulated transcriptionally in vitro and in vivo by widely known regulatory agents ranging from tamoxifen, an oestrogen receptor antagonist and SI-specific inhibitor, to cholesterol-lowering drugs
-
?
5alpha-cholesta-8,24-dien-3beta-ol
5alpha-cholesta-7,24-dien-3beta-ol
-
-
-
?
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
-
r
additional information
?
-
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
5alpha-cholest-7-en-3beta-ol
?
enzyme of the cholesterol biosynthetic pathway, mutations are associated with Conradi-Huenermann syndrome. The enzyme may be involved in liver function, since the mRNA is only detected in hepatocytes not in connective tissue or blood vessels. The expression of the SI gene is regulated transcriptionally in vitro and in vivo by widely known regulatory agents ranging from tamoxifen, an oestrogen receptor antagonist and SI-specific inhibitor, to cholesterol-lowering drugs
-
?
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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]
-
-
(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]
-
-
(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]
-
-
(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]]
-
-
(1R,3aR,4R,5S,7aR)-3a,7a-dimethyl-1-(6-methylheptan-2-yl)-5-(pent-4-en-1-ylamino)octahydro-1H-inden-4-ol
(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
(1R,3aR,4R,5S,7aR)-5-(benzylamino)-3a,7a-dimethyl-1-(6-methylheptan-2-yl)octahydro-1H-inden-4-ol
(1R,3aR,4R,5S,7aR)-5-(dibenzylamino)-3a,7a-dimethyl-1-(6-methylheptan-2-yl)octahydro-1H-inden-4-ol
(1R,3aR,4R,5S,7aR)-5-[benzyl(methyl)amino]-3a,7a-dimethyl-1-(6-methylheptan-2-yl)octahydro-1H-inden-4-ol
(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
(1R,3aR,5S,7aR)-5-(dimethylamino)-3a,7a-dimethyl-1-(6-methylheptan-2-yl)octahydro-1H-inden-4-ol
(R,S)-1-cyclohexyl-4-[3-(5-methoxy-1,2,3,4-tetrahydronaphthalen-1-yl)-n-propyl]piperazine
-
-
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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-
2-[4-[(1Z)-1,2-diphenylbut-1-en-1-yl]phenoxy]-N,N-dimethylethanamine
-
noncompetitive, IC50: 0.00025 mM
trans-2-[4-(1,2-diphenylbuten-1-yl)phenoxy]-N,N-dimethylethylamine
IC50: 0.0112 mM
(+)-pentazocine
-
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
(-)-emopamil
IC50: 28 nM for the liver enzyme, IC50: 34 nM for the brain enzyme
(1R,3aR,4R,5S,7aR)-3a,7a-dimethyl-1-(6-methylheptan-2-yl)-5-(pent-4-en-1-ylamino)octahydro-1H-inden-4-ol
-
-
(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-(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-(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)-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)-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)-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-(benzylamino)-3a,7a-dimethyl-1-(6-methylheptan-2-yl)octahydro-1H-inden-4-ol
-
-
(1R,3aR,4R,5S,7aR)-5-(benzylamino)-3a,7a-dimethyl-1-(6-methylheptan-2-yl)octahydro-1H-inden-4-ol
-
-
(1R,3aR,4R,5S,7aR)-5-(benzylamino)-3a,7a-dimethyl-1-(6-methylheptan-2-yl)octahydro-1H-inden-4-ol
-
-
(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-(dibenzylamino)-3a,7a-dimethyl-1-(6-methylheptan-2-yl)octahydro-1H-inden-4-ol
-
-
(1R,3aR,4R,5S,7aR)-5-(dibenzylamino)-3a,7a-dimethyl-1-(6-methylheptan-2-yl)octahydro-1H-inden-4-ol
-
-
(1R,3aR,4R,5S,7aR)-5-(dibenzylamino)-3a,7a-dimethyl-1-(6-methylheptan-2-yl)octahydro-1H-inden-4-ol
-
-
(1R,3aR,4R,5S,7aR)-5-amino-3a,7a-dimethyl-1-(6-methylheptan-2-yl)octahydro-1H-inden-4-ol
-
-
(1R,3aR,4R,5S,7aR)-5-amino-3a,7a-dimethyl-1-(6-methylheptan-2-yl)octahydro-1H-inden-4-ol
-
-
(1R,3aR,4R,5S,7aR)-5-amino-3a,7a-dimethyl-1-(6-methylheptan-2-yl)octahydro-1H-inden-4-ol
-
-
(1R,3aR,4R,5S,7aR)-5-amino-3a,7a-dimethyl-1-(6-methylheptan-2-yl)octahydro-1H-inden-4-ol
-
-
(1R,3aR,4R,5S,7aR)-5-[benzyl(methyl)amino]-3a,7a-dimethyl-1-(6-methylheptan-2-yl)octahydro-1H-inden-4-ol
-
-
(1R,3aR,4R,5S,7aR)-5-[benzyl(methyl)amino]-3a,7a-dimethyl-1-(6-methylheptan-2-yl)octahydro-1H-inden-4-ol
-
-
(1R,3aR,4R,5S,7aR)-5-[benzyl(methyl)amino]-3a,7a-dimethyl-1-(6-methylheptan-2-yl)octahydro-1H-inden-4-ol
-
-
(1R,3aR,4R,5S,7aR)-5-[benzyl(methyl)amino]-3a,7a-dimethyl-1-(6-methylheptan-2-yl)octahydro-1H-inden-4-ol
-
-
(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
-
-
(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
-
-
(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
-
-
(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
-
-
(1R,3aR,5S,7aR)-5-(dimethylamino)-3a,7a-dimethyl-1-(6-methylheptan-2-yl)octahydro-1H-inden-4-ol
-
-
(1R,3aR,5S,7aR)-5-(dimethylamino)-3a,7a-dimethyl-1-(6-methylheptan-2-yl)octahydro-1H-inden-4-ol
-
-
(1R,3aR,5S,7aR)-5-(dimethylamino)-3a,7a-dimethyl-1-(6-methylheptan-2-yl)octahydro-1H-inden-4-ol
-
-
(1R,3aR,5S,7aR)-5-(dimethylamino)-3a,7a-dimethyl-1-(6-methylheptan-2-yl)octahydro-1H-inden-4-ol
-
-
ditolylguanidine
IC50: 122 nM for the liver enzyme, IC50: 36 nM for the brain enzyme
haloperidol
IC50: 6.8 nM for the liver enzyme, 23 nM for the brain enzyme
ifenprodil
IC50: 2.4 nM for the liver enzyme, 1.7 nM for the brain enzyme
Trifluoperazine
IC50: 11 nM for the liver enzyme, IC50: 13 nM for the brain enzyme
additional information
-
not inhibited by N-benzamido-decalin, tamoxifen, N-benzyl-8-azadecalin, and AY9944
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Antley-Bixler Syndrome Phenotype
Radiographic features of the skeleton in disorders of post-squalene cholesterol biosynthesis.
Candidiasis
ERG2 and ERG24 Are Required for Normal Vacuolar Physiology as Well as Candida albicans Pathogenicity in a Murine Model of Disseminated but Not Vaginal Candidiasis.
cholestenol delta-isomerase deficiency
Radiographic features of the skeleton in disorders of post-squalene cholesterol biosynthesis.
Chondrodysplasia Punctata
A novel EBP c.224T>A mutation supports the existence of a male-specific disorder independent of CDPX2.
Chondrodysplasia Punctata
A novel X-linked multiple congenital anomaly syndrome associated with an EBP mutation.
Chondrodysplasia Punctata
Characterization of mutations in 22 females with X-linked dominant chondrodysplasia punctata (Happle syndrome).
Chondrodysplasia Punctata
Cloning of an emopamil-binding protein (EBP)-like protein that lacks sterol delta8-delta7 isomerase activity.
Chondrodysplasia Punctata
Conradi-Hünermann-Happle syndrome (X-linked dominant chondrodysplasia punctata) confirmed by plasma sterol and mutation analysis.
Chondrodysplasia Punctata
Gas chromatography-mass spectrometry and molecular genetic studies in families with the Conradi-Hünermann-Happle syndrome.
Chondrodysplasia Punctata
Male CDPX2 patient with EBP mosaicism and asymmetrically lateralized skin lesions with strict midline demarcation.
Chondrodysplasia Punctata
Prenatal testing for a novel EBP missense mutation causing X-linked dominant chondrodysplasia punctata.
Chondrodysplasia Punctata
Pustular Skin Lesions in an Adult Female Patient with X-linked Dominant Chondrodysplasia Punctata with a Novel Emopamil Binding Protein Mutation: A Rare Skin Manifestation.
Chondrodysplasia Punctata
Radiographic features of the skeleton in disorders of post-squalene cholesterol biosynthesis.
Chondrodysplasia Punctata
The Conradi-Hünermann-Happle syndrome (CDPX2) and emopamil binding protein: novel mutations, and somatic and gonadal mosaicism.
Chondrodysplasia Punctata
X-linked dominant chondrodysplasia punctata with severe phenotype in a female fetus: A case report.
Colorectal Neoplasms
A perspective on medicinal chemistry approaches towards adenomatous polyposis coli and Wnt signal based colorectal cancer inhibitors.
Demyelinating Diseases
[Mechanisms underlying remyelination with special focus on demyelination models of multiple sclerosis].
Foot-and-Mouth Disease
Single-cell analysis reveals the relevance of foot-and-mouth disease virus persistence to emopamil-binding protein gene expression in host cells.
Infections
ERG2 and ERG24 Are Required for Normal Vacuolar Physiology as Well as Candida albicans Pathogenicity in a Murine Model of Disseminated but Not Vaginal Candidiasis.
Neoplasms
Isolation of differentially expressed genes in NPM-ALK-positive anaplastic large cell lymphoma.
Neoplasms
Prenatal diagnosis of fetal skeletal dysplasia using targeted next-generation sequencing: an analysis of 30 cases.
Nevus
Male CDPX2 patient with EBP mosaicism and asymmetrically lateralized skin lesions with strict midline demarcation.
Protein Deficiency
Radiographic features of the skeleton in disorders of post-squalene cholesterol biosynthesis.
Psoriasis
Emopamil binding protein mutation in conradi-hünermann-happle syndrome representing plaque-type psoriasis.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000016
1-cyclohexyl-4-[cis-4-(2,6-difluorophenyl)cyclohexyl]piperazine
-
pH and temperature not specified in the publication
0.0000076
1-cyclohexyl-4-[cis-4-(2,6-dimethoxyphenyl)cyclohexyl]piperazine
-
pH and temperature not specified in the publication
0.0000041
1-cyclohexyl-4-[cis-4-(2-methoxyphenyl)cyclohexyl]piperazine
-
pH and temperature not specified in the publication
0.000009
1-cyclohexyl-4-[cis-4-(2-methylphenyl)cyclohexyl]piperazine
-
pH and temperature not specified in the publication
0.00000651
1-cyclohexyl-4-[cis-4-(4-methoxyphenyl)cyclohexyl]piperazine
-
pH and temperature not specified in the publication
0.000018
1-cyclohexyl-4-[trans-4-(2,6-difluorophenyl)cyclohexyl]piperazine
-
pH and temperature not specified in the publication
0.000011
1-cyclohexyl-4-[trans-4-(2,6-dimethoxyphenyl)cyclohexyl]piperazine
-
pH and temperature not specified in the publication
0.0000107
1-cyclohexyl-4-[trans-4-(2-methoxyphenyl)cyclohexyl]piperazine
-
pH and temperature not specified in the publication
0.00000973
1-cyclohexyl-4-[trans-4-(2-methylphenyl)cyclohexyl]piperazine
-
pH and temperature not specified in the publication
0.0000136
1-cyclohexyl-4-[trans-4-(4-methoxyphenyl)cyclohexyl]piperazine
-
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
-
-
0.0000169
1-[cis-4-(2-chlorophenyl)cyclohexyl]-4-cyclohexylpiperazine
-
pH and temperature not specified in the publication
0.0000206
1-[trans-4-(2-chlorophenyl)cyclohexyl]-4-cyclohexylpiperazine
-
pH and temperature not specified in the publication
0.0000167
3-[4-(4-naphthalen-1-ylpiperazin-1-yl)cyclohexyl]phenyl hydroperoxide
-
-
0.0000467
4-[1-(2,6-dimethylphenyl)-3-cyclohexen-4-yl]-1-(2-pyridinyl)piperazine
-
-
0.0000123
cis-1-cyclohexyl-4-(4-phenylcyclohexyl)piperazine
-
pH and temperature not specified in the publication
0.0000126
cis-1-cyclohexyl-4-[(3-methoxyphenyl)cyclohexyl]piperazine
-
pH and temperature not specified in the publication
0.0000331
cis-4-[4-(2,6-dimethylyphenyl)cyclohexyl]-1-(2-pyridinyl)piperazine
-
-
0.0000142
trans-1-cyclohexyl-4-(4-phenylcyclohexyl)piperazine
-
pH and temperature not specified in the publication
0.0000004
trans-1-cyclohexyl-4-[(3-methoxyphenyl)cyclohexyl]piperazine
-
pH and temperature not specified in the publication
0.000106
trans-4-[4-(2,6-difluorophenyl)cyclohexyl]-1-(2-pyridinyl)piperazine
-
-
0.000007
trans-4-[4-(2,6-dimethoxyphenyl)cyclohexyl]-1-(2-pyridinyl)piperazine
-
-
0.0000147
(+/-)-ifenprodil
-
pH and temperature not specified in the publication
0.00000495
cis-4-[4-(2,6-dimethoxyphenyl)cyclohexyl]-1-(2-pyridinyl)piperazine
-
-
0.00000495
cis-4-[4-(2,6-dimethoxyphenyl)cyclohexyl]-1-(2-pyridinyl)piperazine
-
pH and temperature not specified in the publication
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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
-
pH and temperature not specified in the publication
0.00025
2-[4-[(1Z)-1,2-diphenylbut-1-en-1-yl]phenoxy]-N,N-dimethylethanamine
Rattus norvegicus
-
noncompetitive, IC50: 0.00025 mM
0.0042
3beta-[2-(diethylamino)ethoxy]androst-5-en-17-one
Rattus norvegicus
IC50: 0.0042 mM
0.0112
trans-2-[4-(1,2-diphenylbuten-1-yl)phenoxy]-N,N-dimethylethylamine
Rattus norvegicus
IC50: 0.0112 mM
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
the enzyme is involved in the ergosterol production. Pharmacological relationship between sigma ligand-binding and C-8,7 sterol isomerase activity, the C-8,7 sterol isomerase that contains a sigma ligand binding site
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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_ARATH
223
5
25146
Swiss-Prot
other Location (Reliability: 2)
EBP_CAVPO
229
5
26679
Swiss-Prot
Secretory Pathway (Reliability: 3)
EBP_DICDI
219
5
25195
Swiss-Prot
Secretory Pathway (Reliability: 1)
EBP_HUMAN
230
5
26353
Swiss-Prot
other Location (Reliability: 5)
EBP_MOUSE
230
5
26215
Swiss-Prot
other Location (Reliability: 5)
EBP_ORYSJ
219
5
24758
Swiss-Prot
other Location (Reliability: 2)
EBP_RAT
230
5
26738
Swiss-Prot
Secretory Pathway (Reliability: 4)
A0A2I0AA87_9ASPA
218
5
24570
TrEMBL
other Location (Reliability: 3)
A0A072UB85_MEDTR
228
5
25816
TrEMBL
other Location (Reliability: 1)
B9RG26_RICCO
220
5
24610
TrEMBL
other Location (Reliability: 1)
A0A8J8WCZ3_9EURO
168
3
20040
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8B6C903_MYTGA
228
5
26424
TrEMBL
Secretory Pathway (Reliability: 5)
Q6DG98_DANRE
232
5
27031
TrEMBL
other Location (Reliability: 5)
A0A5B7BX71_DAVIN
225
5
25638
TrEMBL
other Location (Reliability: 3)
A0A0F8CSD3_CERFI
230
5
26369
TrEMBL
other Location (Reliability: 5)
A0A0B2RJ74_GLYSO
260
5
29219
TrEMBL
other Location (Reliability: 5)
A0A3R7MCA0_TRYRA
260
6
29437
TrEMBL
Secretory Pathway (Reliability: 1)
A0A6J7ZW50_MYTCO
427
2
48904
TrEMBL
Secretory Pathway (Reliability: 5)
A0A3S7WTZ6_LEIDO
285
6
32719
TrEMBL
Secretory Pathway (Reliability: 1)
B5DEE7_XENTR
229
5
26427
TrEMBL
Secretory Pathway (Reliability: 4)
A0A364MU95_9PLEO
280
5
31656
TrEMBL
Secretory Pathway (Reliability: 2)
A0A061HYV7_CRIGR
228
3
26142
TrEMBL
Secretory Pathway (Reliability: 4)
Q4QEY6_LEIMA
169
3
19307
TrEMBL
other Location (Reliability: 2)
A0A396HHN6_MEDTR
86
2
9880
TrEMBL
Secretory Pathway (Reliability: 2)
A0A151RJC2_CAJCA
219
5
24783
TrEMBL
other Location (Reliability: 4)
A0A1S7UNN2_ROSNE
244
5
27318
TrEMBL
Secretory Pathway (Reliability: 4)
A0A0B2RI71_GLYSO
214
5
24114
TrEMBL
other Location (Reliability: 2)
A0A364MYC5_9PLEO
283
4
30681
TrEMBL
other Location (Reliability: 4)
A0A422P324_9TRYP
250
6
27997
TrEMBL
Secretory Pathway (Reliability: 1)
A0A422NRW0_9TRYP
179
4
19746
TrEMBL
Secretory Pathway (Reliability: 1)
B0EL12_ENTDS
Entamoeba dispar (strain ATCC PRA-260 / SAW760)
319
7
36987
TrEMBL
other Location (Reliability: 4)
A0A1L8F5H7_XENLA
229
5
26754
TrEMBL
Secretory Pathway (Reliability: 4)
A0A0B2RFD1_GLYSO
197
5
22133
TrEMBL
Secretory Pathway (Reliability: 2)
A4HWT3_LEIIN
169
3
19202
TrEMBL
other Location (Reliability: 3)
Q4WFW3_ASPFU
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)
225
5
26507
TrEMBL
Secretory Pathway (Reliability: 4)
A0A1G4I5V5_TRYEQ
221
1
24573
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2P6QZX5_ROSCH
224
5
24938
TrEMBL
other Location (Reliability: 2)
A0A364MZY4_9PLEO
240
5
27415
TrEMBL
other Location (Reliability: 4)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
26737
27000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
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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
additional information
-
functional complementation by C-8,7 sterol isomerase of the corresponding sterol mutant in yeast and its characterization by exposure to sigma ligands. The full-length Arabidosis thaliana cDNA encoding C-8,7 sterol isomerase complements the erg2 mutation
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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
-
the full-length cDNA that complements the erg2 mutation contains an open reading frame encoding a 21000 Da protein that shares 68% similarity and 35% amino acid identity to the recently isolated mouse C8,7 sterol isomerase
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lee, W.H.; Kammereck, R.; Lutsky, B.N.; McCloskey, J.A.; Schroepfer, G.J.Jr.
Studies on the mechanism of the enzymatic conversion of DELTA8-cholesten-3beta-ol to DELTA7-cholesten-3beta-ol
J. Biol. Chem.
244
2033-2040
1969
Rattus norvegicus
brenda
Wilton, D.C.; Rahimtula, A.D.; Akhtar, M.
The reversibility of the DELTA8-cholestenol-DELTA7-cholestenol isomerase reaction in cholesterol biosynthesis
Biochem. J.
114
71-73
1969
Rattus norvegicus
brenda
Scala, A.; Galli-Kienle, M.; Anastasia, M.; Galli, G.
The reversibility of the isomerization of the DELTA8 to DELTA7 bond in cholesterol biosynthesis
Eur. J. Biochem.
48
263-269
1974
Rattus norvegicus
brenda
Bae, S.H.; Seong, J.; Paik, Y.K.
Cholesterol biosynthesis from lanosterol: molecular cloning, chromosomal localization, functional expression and liver-specific gene regulation of rat sterol DELTA8-isomerase, a cholesterogenic enzyme with multiple functions
Biochem. J.
353
689-699
2001
Rattus norvegicus (Q9JJ46)
brenda
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)
brenda
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
brenda
Cho, S.Y.; Kim, J.H.; Paik, Y.K.
Cholesterol biosynthesis from lanosterol: differential inhibition of sterol DELTA8-isomerase and other lanosterol-converting enzymes by tamoxifen
Mol. Cells
8
233-239
1998
Rattus norvegicus
brenda
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
Saccharomyces cerevisiae, Mus musculus (P70245), Homo sapiens (Q15125), Homo sapiens, Cavia porcellus (Q60490)
brenda
Grebenok, R.J.; Ohnmeiss, T.E.; Yamamoto, A.; Huntley, E.D.; Galbraith, D.W.; Della Penna, D.
Isolation and characterization of an Arabidopsis thaliana C-8,7 sterol isomerase: functional and structural similarities to mammalian C-8,7 sterol isomerase/emopamil-binding protein
Plant Mol. Biol.
38
807-815
1998
Arabidopsis thaliana
brenda
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
brenda
Rahier, A.; Pierre, S.; Riveill, G.; Karst, F.
Identification of essential amino acid residues in a sterol 8,7-isomerase from Zea mays reveals functional homology and diversity with the isomerases of animal and fungal origin
Biochem. J.
414
247-259
2008
Saccharomyces cerevisiae, Zea mays
brenda
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
brenda
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
brenda
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
brenda
Koenig, M.; Mueller, C.; Bracher, F.
Stereoselective synthesis of a new class of potent and selective inhibitors of human DELTA8,7-sterol isomerase
Bioorg. Med. Chem.
21
1925-1943
2013
Saccharomyces cerevisiae, [Candida] glabrata, Yarrowia lipolytica, Homo sapiens
brenda
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