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Information on EC 3.3.2.11 - cholesterol-5,6-oxide hydrolase
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EC Tree
3.3.2.11 cholesterol-5,6-oxide hydrolaseIUBMB Comments
The enzyme appears to work equally well with either epoxide as substrate . The product is a competitive inhibitor of the reaction. In vertebrates, five epoxide-hydrolase enzymes have been identified to date: EC 3.3.2.6 (leukotriene-A4 hydrolase), EC 3.3.2.7 (hepoxilin-epoxide hydrolase), EC 3.3.2.9 (microsomal epoxide hydrolase), EC 3.3.2.10 (soluble epoxide hydrolase) and EC 3.3.2.11 (cholesterol 5,6-oxide hydrolase) .
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Word Map
- 3.3.2.11
-
anti-estrogenic
- oxysterols
- diphenylmethane
-
hetero-oligomeric
-
hormonotherapy
- medicine
- drug development
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
cholesterol epoxide hydrolase, anti-estrogen binding site, cehase, cholesterol-5,6-epoxide hydrolase, cholesterol-epoxide hydrolase, cholesterol oxide hydrolase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
anti-estrogen binding site
-
cholesterol epoxide hydrolase is a heterooligomeric complex called the anti-estrogen binding site comprising 3beta-hydroxysterol-DELTA8-DELTA7-isomerase and 3beta-hydroxysterol-DELTA7-reductase
ChEH
cholesterol 5alpha,6alpha-oxide hydrolase
cholesterol epoxide hydrolase
cholesterol-5,6-epoxide hydrolase
EH_CH
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
5,6alpha-epoxy-5alpha-cholestan-3beta-ol + H2O = 5alpha-cholestane-3beta,5alpha,6beta-triol
5,6alpha-epoxy-5alpha-cholestan-3beta-ol + H2O = 5alpha-cholestane-3beta,5alpha,6beta-triol
-
-
-
-
5,6alpha-epoxy-5alpha-cholestan-3beta-ol + H2O = 5alpha-cholestane-3beta,5alpha,6beta-triol
positively charged transition state
-
5,6beta-epoxy-5beta-cholestan-3beta-ol + H2O = 5alpha-cholestane-3beta,5alpha,6beta-triol
-
-
-
-
5,6beta-epoxy-5beta-cholestan-3beta-ol + H2O = 5alpha-cholestane-3beta,5alpha,6beta-triol
positively charged transition state
-
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SYSTEMATIC NAME
IUBMB Comments
5,6alpha-epoxy-5alpha-cholestan-3beta-ol hydrolase
The enzyme appears to work equally well with either epoxide as substrate [3]. The product is a competitive inhibitor of the reaction. In vertebrates, five epoxide-hydrolase enzymes have been identified to date: EC 3.3.2.6 (leukotriene-A4 hydrolase), EC 3.3.2.7 (hepoxilin-epoxide hydrolase), EC 3.3.2.9 (microsomal epoxide hydrolase), EC 3.3.2.10 (soluble epoxide hydrolase) and EC 3.3.2.11 (cholesterol 5,6-oxide hydrolase) [3].
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CAS REGISTRY NUMBER
COMMENTARY
55467-47-5
-
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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
5,6-epoxy-5alpha-cholestan-3beta-ol + H2O
cholestane-3beta,5alpha,6beta-triol
-
-
-
-
?
5,6alpha-epoxy-5alpha-cholestan-3beta-ol + H2O
5alpha-cholestane-3beta,5alpha,6beta-triol
-
-
-
-
?
5,6alpha-epoxy-5alpha-cholestan-3beta-ol + H2O
5alpha-cholestane-3beta,5alpha,6beta-triol
-
-
-
-
?
5,6alpha-epoxy-5alpha-cholestan-3beta-ol + H2O
cholestane-3beta,5alpha,6beta-triol
-
-
-
-
?
5,6alpha-epoxy-5alpha-cholestan-3beta-ol + H2O
cholestane-3beta,5alpha,6beta-triol
-
the enzyme is equally active with both stereoisomers
-
-
?
5,6alpha-epoxy-5alpha-cholestan-3beta-ol + H2O
cholestane-3beta,5alpha,6beta-triol
-
-
-
-
?
5,6alpha-epoxy-5alpha-cholestan-3beta-ol + H2O
cholestane-3beta,5alpha,6beta-triol
-
the enzyme is equally active with both stereoisomers
-
-
?
5,6alpha-epoxy-5alpha-cholestan-3beta-ol + H2O
cholestane-3beta,5alpha,6beta-triol
-
-
-
-
?
5,6alpha-epoxy-5alpha-cholestan-3beta-ol + H2O
cholestane-3beta,5alpha,6beta-triol
-
the substrate is a product of lipid peroxidation in the liver
-
-
?
5,6alpha-epoxy-5alpha-cholestan-3beta-ol + H2O
cholestane-3beta,5alpha,6beta-triol
-
the enzyme is equally active with both stereoisomers
-
-
?
5,6alpha-epoxy-5alpha-cholestan-3beta-ol + H2O
cholestane-3beta,5alpha,6beta-triol
-
-
-
-
?
5,6alpha-epoxy-5alpha-cholestan-3beta-ol + H2O
cholestane-3beta,5alpha,6beta-triol
-
the enzyme is highly substrate-specific
-
-
?
5,6alpha-epoxy-5alpha-cholestan-3beta-ol + H2O
cholestane-3beta,5alpha,6beta-triol
-
the enzyme is equally active with both stereoisomers
-
-
?
5,6alpha-epoxy-5alpha-cholestan-3beta-ol + H2O
cholestane-3beta,5alpha,6beta-triol
-
-
-
-
?
5,6alpha-epoxy-5alpha-cholestan-3beta-ol + H2O
cholestane-3beta,5alpha,6beta-triol
-
regulation, the enzyme is highly substrate specific
-
-
?
5,6alpha-epoxy-5alpha-cholestan-3beta-ol + H2O
cholestane-3beta,5alpha,6beta-triol
-
the enzyme is highly substrate-specific
-
-
?
5,6alpha-epoxy-5alpha-cholestan-3beta-ol + H2O
cholestane-3beta,5alpha,6beta-triol
-
the enzyme is highly substrate-specific
i.e. 5,6-glycol
-
?
5,6alpha-epoxy-5alpha-cholestan-3beta-ol + H2O
cholestane-3beta,5alpha,6beta-triol
-
the enzyme is equally active with both stereoisomers
-
-
?
5,6alpha-epoxy-5alpha-cholestan-3beta-ol + H2O
cholestane-3beta,5alpha,6beta-triol
-
the enzyme is highly substrate specific
-
-
?
5,6beta-epoxy-5alpha-cholestan-3beta-ol + H2O
5alpha-cholestane-3beta,5alpha,6beta-triol
-
-
-
-
?
5,6beta-epoxy-5alpha-cholestan-3beta-ol + H2O
5alpha-cholestane-3beta,5alpha,6beta-triol
-
better substrate
-
-
?
5,6beta-epoxy-5alpha-cholestan-3beta-ol + H2O
5alpha-cholestane-3beta,5alpha,6beta-triol
-
best substrate
-
-
?
5,6beta-epoxy-5beta-cholestan-3beta-ol + H2O
5alpha-cholestane-3beta,5alpha,6beta-triol
-
-
-
-
?
5,6beta-epoxy-5beta-cholestan-3beta-ol + H2O
5alpha-cholestane-3beta,5alpha,6beta-triol
-
-
-
-
?
5,6beta-epoxy-5beta-cholestan-3beta-ol + H2O
cholestane-3beta,5alpha,6beta-triol
-
the enzyme is equally active with both stereoisomers
-
-
?
5,6beta-epoxy-5beta-cholestan-3beta-ol + H2O
cholestane-3beta,5alpha,6beta-triol
-
the enzyme is equally active with both stereoisomers
-
-
?
5,6beta-epoxy-5beta-cholestan-3beta-ol + H2O
cholestane-3beta,5alpha,6beta-triol
-
the enzyme is equally active with both stereoisomers
-
-
?
5,6beta-epoxy-5beta-cholestan-3beta-ol + H2O
cholestane-3beta,5alpha,6beta-triol
-
the enzyme is equally active with both stereoisomers
-
-
?
5,6beta-epoxy-5beta-cholestan-3beta-ol + H2O
cholestane-3beta,5alpha,6beta-triol
-
-
-
-
?
5,6beta-epoxy-5beta-cholestan-3beta-ol + H2O
cholestane-3beta,5alpha,6beta-triol
-
the enzyme is equally active with both stereoisomers
-
-
?
additional information
?
-
-
the enzyme is distinct from the microsomal epoxide hydrolase EC 3.3.2.9, which shows a wider substrate specificity
-
-
?
additional information
?
-
-
the enzyme is distinct from the microsomal epoxide hydrolase EC 3.3.2.9, which shows a wider substrate specificity
-
-
?
additional information
?
-
-
the enzyme is distinct from the microsomal epoxide hydrolase EC 3.3.2.9, which shows a wider substrate specificity
-
-
?
additional information
?
-
-
the enzyme is distinct from the microsomal epoxide hydrolase EC 3.3.2.9, which shows a wider xenobiotic substrate specificity
-
-
?
additional information
?
-
-
the enzyme is distinct from the microsomal epoxide hydrolase EC 3.3.2.9, which shows a wider substrate specificity
-
-
?
additional information
?
-
-
the enzyme is distinct from the microsomal epoxide hydrolase EC 3.3.2.9, which shows a wider substrate specificity
-
-
?
additional information
?
-
-
the enzyme is distinct from the microsomal epoxide hydrolase EC 3.3.2.9
-
-
?
additional information
?
-
-
the enzyme is distinct from the microsomal epoxide hydrolase EC 3.3.2.9
-
-
?
additional information
?
-
-
the enzyme is distinct from the microsomal epoxide hydrolase EC 3.3.2.9, which shows a wider substrate specificity
-
-
?
additional information
?
-
-
the enzyme is distinct from the microsomal epoxide hydrolase EC 3.3.2.9, which shows a wider substrate specificity
-
-
?
additional information
?
-
-
the enzyme is distinct from the microsomal epoxide hydrolase EC 3.3.2.9, which shows a wider xenobiotic substrate specificity
-
-
?
additional information
?
-
-
no activity with xenobiotic alkene oxides and arene oxides, e.g. octene 1,2-oxide or benz[a]anthracene 5,6-oxide
-
-
?
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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
5,6beta-epoxy-5beta-cholestan-3beta-ol + H2O
cholestane-3beta,5alpha,6beta-triol
-
-
-
-
?
5,6alpha-epoxy-5alpha-cholestan-3beta-ol + H2O
5alpha-cholestane-3beta,5alpha,6beta-triol
-
-
-
-
?
5,6alpha-epoxy-5alpha-cholestan-3beta-ol + H2O
5alpha-cholestane-3beta,5alpha,6beta-triol
-
-
-
-
?
5,6alpha-epoxy-5alpha-cholestan-3beta-ol + H2O
cholestane-3beta,5alpha,6beta-triol
-
-
-
-
?
5,6alpha-epoxy-5alpha-cholestan-3beta-ol + H2O
cholestane-3beta,5alpha,6beta-triol
-
-
-
-
?
5,6alpha-epoxy-5alpha-cholestan-3beta-ol + H2O
cholestane-3beta,5alpha,6beta-triol
-
-
-
-
?
5,6alpha-epoxy-5alpha-cholestan-3beta-ol + H2O
cholestane-3beta,5alpha,6beta-triol
-
the substrate is a product of lipid peroxidation in the liver
-
-
?
5,6alpha-epoxy-5alpha-cholestan-3beta-ol + H2O
cholestane-3beta,5alpha,6beta-triol
-
-
-
-
?
5,6alpha-epoxy-5alpha-cholestan-3beta-ol + H2O
cholestane-3beta,5alpha,6beta-triol
-
the enzyme is highly substrate-specific
-
-
?
5,6alpha-epoxy-5alpha-cholestan-3beta-ol + H2O
cholestane-3beta,5alpha,6beta-triol
-
-
-
-
?
5,6alpha-epoxy-5alpha-cholestan-3beta-ol + H2O
cholestane-3beta,5alpha,6beta-triol
-
regulation, the enzyme is highly substrate specific
-
-
?
5,6alpha-epoxy-5alpha-cholestan-3beta-ol + H2O
cholestane-3beta,5alpha,6beta-triol
-
the enzyme is highly substrate-specific
-
-
?
5,6beta-epoxy-5alpha-cholestan-3beta-ol + H2O
5alpha-cholestane-3beta,5alpha,6beta-triol
-
-
-
-
?
5,6beta-epoxy-5alpha-cholestan-3beta-ol + H2O
5alpha-cholestane-3beta,5alpha,6beta-triol
-
better substrate
-
-
?
5,6beta-epoxy-5alpha-cholestan-3beta-ol + H2O
5alpha-cholestane-3beta,5alpha,6beta-triol
-
best substrate
-
-
?
additional information
?
-
-
the enzyme is distinct from the microsomal epoxide hydrolase EC 3.3.2.9, which shows a wider substrate specificity
-
-
?
additional information
?
-
-
the enzyme is distinct from the microsomal epoxide hydrolase EC 3.3.2.9, which shows a wider substrate specificity
-
-
?
additional information
?
-
-
the enzyme is distinct from the microsomal epoxide hydrolase EC 3.3.2.9, which shows a wider substrate specificity
-
-
?
additional information
?
-
-
the enzyme is distinct from the microsomal epoxide hydrolase EC 3.3.2.9, which shows a wider xenobiotic substrate specificity
-
-
?
additional information
?
-
-
the enzyme is distinct from the microsomal epoxide hydrolase EC 3.3.2.9, which shows a wider substrate specificity
-
-
?
additional information
?
-
-
the enzyme is distinct from the microsomal epoxide hydrolase EC 3.3.2.9, which shows a wider substrate specificity
-
-
?
additional information
?
-
-
the enzyme is distinct from the microsomal epoxide hydrolase EC 3.3.2.9
-
-
?
additional information
?
-
-
the enzyme is distinct from the microsomal epoxide hydrolase EC 3.3.2.9
-
-
?
additional information
?
-
-
the enzyme is distinct from the microsomal epoxide hydrolase EC 3.3.2.9, which shows a wider substrate specificity
-
-
?
additional information
?
-
-
the enzyme is distinct from the microsomal epoxide hydrolase EC 3.3.2.9, which shows a wider substrate specificity
-
-
?
additional information
?
-
-
the enzyme is distinct from the microsomal epoxide hydrolase EC 3.3.2.9, which shows a wider xenobiotic substrate specificity
-
-
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(11beta,17beta)-11-{4-[2-(Dimethylamino)ethoxy]phenyl}estra-1,3,5(10)-triene-3,17-diol
-
-
(E)-N,3,6,6-tetra methyl-N-(naphthalene-1-ylmethyl)hept-2-en-4-yn-1-amine
-
-
(E)-N-(4-(3-chloro-4-cyclohexylphenyl)but-3-enyl)-N-ethylcyclohexanamine
-
-
1-[2-[4-[(Z)-1-(4-methoxyphenyl)-2-nitro-2-phenylethenyl]phenoxy]ethyl]pyrrolidine
-
-
2-(4-chlorophenyl)-1-(4-(2-(diethylamino)ethoxy)phenyl)-1-p-tolyl ethanol
-
-
2-[4-[(Z)-2-chloro-1,2-di (phenyl)ethenyl]phenoxy]-N,N-diethylethanamine
-
-
4-(4-(4-chloro phenyl)-4-hydroxypiperidin-1-yl)-1-(4-fluorophenyl)butan-1-one
-
-
4-[(Z)-1-[4-(2-dimethylaminoethyloxy)phenyl]-2-phenyl but-1-enyl]phenol
-
-
5,6alpha-epoxy-5alpha-cholestan-3beta-ol
-
competitive to 5,6beta-epoxy-5alpha-cholestan-3beta-ol
5,6beta-epoxy-5beta-cholestan-3beta-ol
-
competitive to 5,6alpha-epoxy-5alpha-cholestan-3beta-ol
6-oxo-cholestan-3beta,5alpha-diol
-
OCDO, inhibition of the ChEH activity by OCDO, at higher concentration OCDO is reported to inhibit cholesterol biosynthesis from mevalonate but not from acetate at the D8D7I step (the catalytic subunit of ChEH), leading to the accumulation of Delta-8 sterols. Identification of OCDO as an oncometabolite in humans
acetone
-
reduces the activity by 85% at 1.25% v/v, by 50% at 3.75% v/v, and by 56% at 6.25% v/v
[6-hydroxy-2-(4-hydroxyphenyl)-1-benzothiophen-3-yl]-[4-(2-piperidin-1-ylethoxy)phenyl]methanone
-
-
5,6alpha-imino-5alpha-cholestan-3beta-ol
-
strong, specific, competitive inhibition
5,6alpha-imino-5alpha-cholestane-3beta-ol
-
specific inhibition of cholesterol-5,6-epoxide hydrolase
5,6alpha-imino-5alpha-cholestane-3beta-ol
-
specific inhibition of cholesterol-5,6-epoxide hydrolase
additional information
-
no inhibition by 1,1,1-trichloropropene oxide
-
additional information
-
no effect by 5,6alpha-epoxy-5alpha-cholestan-3beta-ol in vivo, and by EDTA and 2,2-dipyridyl, preferred buffer is 300 mM potassium phosphate at pH 7.4 and 37°C, low activity in Tris and HEPES buffers
-
additional information
-
comparison of inhibition level in microsomes of normal liver tissue and liver hyperplastic nodules, remaining activities, overview
-
additional information
-
no inhibition by isoquinoline, styrene oxide, cyclohexane oxide, benzil, cholesterol, and cholic acid
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
acetonitrile
-
maximal enzyme activity at 6.25% v/v, 19% of maximal activity at 1.25% v/v, 50% of maximal activity at 12.5% v/v, no activity at 18.8% v/v
additional information
-
no effect by 5,6alpha-epoxy-5alpha-cholestan-3beta-ol in vivo, and by EDTA and 2,2-dipyridyl, preferred buffer is 300 mM potassium phosphate at pH 7.4 and 37°C, low activity in Tris and HEPES buffers
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Breast Neoplasms
A diphenylmethane derivative selective for the anti-estrogen binding site may help define its biological role.
Breast Neoplasms
A potent and selective photoaffinity probe for the anti-estrogen binding site of rat liver.
Neoplasms
Dendrogenin A arises from cholesterol and histamine metabolism and shows cell differentiation and anti-tumour properties.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00091
5,6-epoxy-5alpha-cholestan-3beta-ol
-
pH 7.4, 37°C, normal liver tissue microsomes
0.0044
5,6beta-epoxy-5beta-cholestan-3beta-ol
-
pH 7.4, 37°C, versus 5,6alpha-epoxy-5alpha-cholestan-3beta-ol
0.0037
5,6alpha-epoxy-5alpha-cholestan-3beta-ol
-
pH 7.4, 37°C, versus 5,6beta-epoxy-5alpha-cholestan-3beta-ol
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000155
(11beta,17beta)-11-{4-[2-(Dimethylamino)ethoxy]phenyl}estra-1,3,5(10)-triene-3,17-diol
-
pH 7.4, 37°C
0.000089
(4-(6-(allyl (methyl)amino)hexyloxy)phenyl)(4-bromophenyl)methanone
-
pH 7.4, 37°C
0.0091
(E)-N,3,6,6-tetra methyl-N-(naphthalene-1-ylmethyl)hept-2-en-4-yn-1-amine
-
pH 7.4, 37°C
0.000006
(E)-N-(4-(3-chloro-4-cyclohexylphenyl)but-3-enyl)-N-ethylcyclohexanamine
-
pH 7.4, 37°C
0.000035
1-(2-(4-(2-phenylpropan-2-yl) phenoxy)ethyl)pyrrolidine
-
pH 7.4, 37°C
0.000018
1-[2-[4-[(Z)-1-(4-methoxyphenyl)-2-nitro-2-phenylethenyl]phenoxy]ethyl]pyrrolidine
-
pH 7.4, 37°C
0.000039
2-(4-chlorophenyl)-1-(4-(2-(diethylamino)ethoxy)phenyl)-1-p-tolyl ethanol
-
pH 7.4, 37°C
0.000009
2-[4-[(Z)-2-chloro-1,2-di (phenyl)ethenyl]phenoxy]-N,N-diethylethanamine
-
pH 7.4, 37°C
0.000057
4-(2-(4-(2-phenylpropan-2-yl)phenoxy)ethyl)morpholine
-
pH 7.4, 37°C
0.018
4-(4-(4-chloro phenyl)-4-hydroxypiperidin-1-yl)-1-(4-fluorophenyl)butan-1-one
-
pH 7.4, 37°C
0.000145
4-hydroxy-tamoxifen
-
pH and temperature not specified in the publication
0.000145
4-[(Z)-1-[4-(2-dimethylaminoethyloxy)phenyl]-2-phenyl but-1-enyl]phenol
-
pH 7.4, 37°C
0.0044
5,6alpha-epoxy-5alpha-cholestan-3beta-ol
-
pH 7.4, 37°C, versus 5,6beta-epoxy-5alpha-cholestan-3beta-ol
0.000085
5,6alpha-imino-5alpha-cholestan-3beta-ol
-
pH 7.4, 37°C, versus 5,6alpha-epoxy-5alpha-cholestan-3beta-ol
0.0037
5,6beta-epoxy-5beta-cholestan-3beta-ol
-
pH 7.4, 37°C, versus 5,6alpha-epoxy-5alpha-cholestan-3beta-ol
0.126
9,10-iminophenanthrene
-
pH 7.4, 37°C, versus 5,6alpha-epoxy-5alpha-cholestan-3beta-ol
0.0366
Iminosqualene
-
pH 7.4, 37°C, versus 5,6alpha-epoxy-5alpha-cholestan-3beta-ol
0.000099
N-(3,4-dichlorophenethyl)-N-methyl-2-(pyrrolidin-1-yl)ethanemine
-
pH 7.4, 37°C
0.000027
N-pyrrolidino-2-[4-(benzyl)-phenoxy]-ethanamine
-
pH and temperature not specified in the publication
0.000203
phenyl{4-[2-(pyrrolidin-1-yl)ethoxy]phenyl}methanone
-
pH 7.4, 37°C
0.000036
[6-hydroxy-2-(4-hydroxyphenyl)-1-benzothiophen-3-yl]-[4-(2-piperidin-1-ylethoxy)phenyl]methanone
-
pH 7.4, 37°C
additional information
additional information
-
inhibition kinetics at pH 8.0, 37°C, 6.5% v/v acetonitrile
-
0.036
alpha-linolenic acid
-
pH and temperature not specified in the publication
0.0097
cholestane-3beta,5alpha,6beta-triol
-
pH and temperature not specified in the publication
0.012
docosahexaenoic acid
-
pH and temperature not specified in the publication
0.000135
trifluoroperazine
-
pH and temperature not specified in the publication
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000765
1-(2-(4-benzylphenoxy)ethyl)pyrrolidin hydrochloride
Homo sapiens
-
pH and temperature not specified in the publication
0.000231
1-[2-[4-(phenylmethyl)phenoxy]ethyl]-pyrrolidine
Homo sapiens
-
MDA-MB231 cells, pH not specified in the publication, temperature not specified in the publication
0.00025
1-[2-[4-(phenylmethyl)phenoxy]ethyl]-pyrrolidine
Homo sapiens
-
MCF-7 cells, pH not specified in the publication, temperature not specified in the publication
0.000065
4-hydroxytamoxifen
Homo sapiens
-
MDA-MB231 cells, pH not specified in the publication, temperature not specified in the publication
0.000095
4-hydroxytamoxifen
Homo sapiens
-
MCF-7 cells, pH not specified in the publication, temperature not specified in the publication
0.00006
clomiphene
Homo sapiens
-
MDA-MB231 cells, pH not specified in the publication, temperature not specified in the publication
0.000064
clomiphene
Homo sapiens
-
MCF-7 cells, pH not specified in the publication, temperature not specified in the publication
0.000313
dendrogenin A
Homo sapiens
-
MDA-MB231 cells, pH not specified in the publication, temperature not specified in the publication
0.00035
dendrogenin A
Homo sapiens
-
MCF-7 cells, pH not specified in the publication, temperature not specified in the publication
0.000069
raloxifene
Homo sapiens
-
MDA-MB231 cells, pH not specified in the publication, temperature not specified in the publication
0.0001
raloxifene
Homo sapiens
-
MCF-7 cells, pH not specified in the publication, temperature not specified in the publication
0.003
rimcazole
Homo sapiens
-
MCF-7 cells, pH not specified in the publication, temperature not specified in the publication
0.0035
rimcazole
Homo sapiens
-
MDA-MB231 cells, pH not specified in the publication, temperature not specified in the publication
0.00007
tamoxifen
Homo sapiens
-
MDA-MB231 cells, pH not specified in the publication, temperature not specified in the publication
0.00011
tamoxifen
Homo sapiens
-
MCF-7 cells, pH not specified in the publication, temperature not specified in the publication
0.000172
tesmilifene
Homo sapiens
-
MDA-MB231 cells, pH not specified in the publication, temperature not specified in the publication
0.00021
tesmilifene
Homo sapiens
-
MCF-7 cells, pH not specified in the publication, temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00004
-
liver microsomes, substrate 5,6beta-epoxy-5alpha-cholestan-3beta-ol
0.0001
-
liver microsomes, substrate 5,6beta-epoxy-5alpha-cholestan-3beta-ol
0.00014
-
liver microsomes, substrate 5,6alpha-epoxy-5alpha-cholestan-3beta-ol
0.00018
0.0002
-
liver microsomes, substrate 5,6alpha-epoxy-5alpha-cholestan-3beta-ol
0.00045
-
liver microsomes, substrate 5,6beta-epoxy-5alpha-cholestan-3beta-ol
0.00048
-
liver microsomes, substrate 5,6alpha-epoxy-5alpha-cholestan-3beta-ol
0.00052
-
liver microsomes, substrate 5,6beta-epoxy-5alpha-cholestan-3beta-ol
0.00108
additional information
0.00108
-
liver microsomes, substrate 5,6alpha-epoxy-5alpha-cholestan-3beta-ol
additional information
-
evaluation of substrate solubilization solvents for enzyme assay, preferred buffer is 300 mM potassium phosphate at pH 7.4 and 37°C
additional information
-
specific activity in different tissues and subcellular fractions
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
-
tissue distribution analysis, no or poor activity in lung and spleen
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
subcellular distribution analysis, no or low activity in cytosol, plasma membrane, Golgi apparatus II, and nucleus, overview
-
brenda
-
similar enzyme activity in smooth and rough microsomes
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
-
knockdown of D8D7I (3beta-hydroxysterol-DELTA8-DELTA7-isomerase) and DHCR7 (3beta-hydroxysterol-DELTA7-reductase) abolishes ChEH activity. D8D7I and DHCR7 cooperate in the ChEH activity
malfunction
-
patients suffering the lysosomal storage diseases Niemann-Pick types A, B, C1 and C2 (NPA, NPB, NPC) show elevated 5alpha-cholestane-3beta,5alpha,6beta-triol in plasma, presumably derived from free radical oxidation of cholesterol to 5,6-epoxycholesterol followed by hydrolysis to the triol by enzyme cholesterol epoxide hydrolase, ChEH
metabolism
-
cholesterol-5,6-epoxide pathway in normal breast and breast cancers, overview
metabolism
-
the enzymes ChEH, HSD11B1 and HSD11B2, and CYP27A1 sit at a fulcrum balancing the formation from 5alpha,6-epoxycholesterol of the tumour suppressor DDA and from 5,6-epoxycholesterol, through 5alpha-cholestane-3beta,5alpha,6beta-triol, the oncometabolite 3beta,5alpha-diHC-6O or the bile acid 3beta,5alpha,6beta-trihydroxycholanoic acid. 26-hydroxy-7-oxocholesterol activates the Hedgehog signalling pathway, constitutive activation of which is linked to tumorigenesis further connecting the HSD11B and CYP27A1 enzymes to oncology
physiological function
-
the existence of ChEH activity in MCF-7 cells, and thus ChEH inhibition and accumulation are likely to play a role in the mechanism of induction of breast cancer cell differentiation and apoptosis by antiestrogen binding site (AEBS) ligands that require sterol autoxidation products
physiological function
-
primary and secondary products of the enzyme's activity have tumor promoting and carcinogenic activity
physiological function
-
the enzyme plays a potential role in cancer progression and resistance
physiological function
-
5,6-epoxycholesterol is hydrolysed by the enzyme cholesterol epoxide hydrolase (ChEH) to 3beta,5alpha,6beta-triol which itself is oxidised by hydroxysteroid dehydrogenase (HSD), steps leading to the acidic pathway of bile acid biosynthesis
physiological function
-
in breast tumors from patients, OCDO production as well as the expression of the enzymes involved in the pathway producing 6-oxo-cholestan-3beta,5alpha-diol (OCDO), namely ChEH subunits and 11beta-hydroxysteroid dehydrogenase of type 2 (HSD2), are higher compared to normal tissues, and overexpression of these enzymes correlates with a higher risk of patient death, indicating that this onco-metabolism is of major importance to breast cancer pathology. The ChEH product 5alpha-cholestane-3beta,5alpha,6beta-triol is metabolized into OCDO
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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). EPHG_MYCTU
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
149
0
16593
Swiss-Prot
-
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
acetone reduces the activity by 85% at 1.25% v/v, by 50% at 3.75% v/v, and by 56% at 6.25% v/v
-
660782
acetonitrile activates the enzyme at moderate concentration, maximal enzyme activity at 6.25% v/v, 19% of maximal activity at 1.25% v/v, 50% of maximal activity at 12.5% v/v, no activity at 18.8% v/v
-
660782
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-90°C, liver microsomes, enzyme is stable during repeated freezing and thawing
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
from microsomes, separation from EC 3.3.2.9 by immunoprecipitation
liver microsome preparation
partially from liver by micosome preparation and immunoprecipitation, separation from the xenobiotic epoxide hydrolase, EC 3.3.2.9
-
partially from liver by micosome preparation, two steps of gel filtration, separation from the xenobiotic epoxide hydrolase, EC 3.3.2.9
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
-
the enzyme is a target for inhibition of the 6-oxo-cholestan-3beta,5alpha-diol (OCDO) biosynthesis in cancer therapy
medicine
-
in breast cancer tissue, cholesterol epoxide hydrolase ChEH metabolizes cholesterol-5,6-epoxide into cholestane-3beta,5alpha,6beta-triol, which is transformed into the oncometabolite 6-oxo-cholestan-3beta,5alpha-diol by 11beta-hydroxysteroid-dehydrogenase 11betaHSD2. ChEH inhibition and 11betaHSD2 silencing inhibit 6-oxo-cholestan-3beta,5alpha-diol production and tumor growth. Patient breast cancer samples show significantly increased 6-oxocholestan-3beta,5alpha-diol levels and greater ChEH and 11betaHSD2 protein expression compared with normal tissues, and 11betaHSD2 and ChEH overexpression correlate with a higher risk of patient death
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Levin, W.; Michaud, D.P.; Thomas, P.E.; Jerina, D.M.
Distinct rat hepatic microsomal epoxide hydrolases catalyze the hydration of cholesterol 5,6alpha-oxide and certain xenobiotic alkene and arene oxides
Arch. Biochem. Biophys.
220
485-494
1983
Rattus norvegicus
brenda
Nashed, N.T.; Michaud, D.P.; Levin, W.; Jerina, D.M.
Properties of liver microsomal cholesterol 5,6-oxide hydrolase
Arch. Biochem. Biophys.
241
149-162
1985
Oryctolagus cuniculus, Homo sapiens, Mesocricetus auratus, Mus musculus, Rattus norvegicus
brenda
Watabe, T.; Ozawa, N.; Ishii, H.; Chiba, K.; Hiratsuka, A.
Hepatic microsomal cholesterol epoxide hydrolase: selective inhibition by detergents and separation from xenobiotic epoxide hydrolase
Biochem. Biophys. Res. Commun.
140
632-637
1986
Mus musculus
brenda
Palakodety, R.B.; Vaz, A.D.; Griffin, M.J.
Microsomal cholesterol epoxide hydrolase activity in 2-acetylaminofluorene-induced rat liver hyperplastic nodules
Biochem. Pharmacol.
36
2424-2427
1987
Rattus norvegicus
brenda
Astroem, A.; Eriksson, M.; Eriksson, L.C.; Birberg, W.; Pilotti, A.; DePierre, J.W.
Subcellular and organ distribution of cholesterol epoxide hydrolase in the rat
Biochim. Biophys. Acta
882
359-366
1986
Rattus norvegicus
brenda
Oesch, F.; Timms, C.W.; Walker, C.H.; Guenthner, T.M.; Sparrow, A.; Watabe, T.; Wolf, C.R.
Existence of multiple forms of microsomal epoxide hydrolases with radically different substrate specificities
Carcinogenesis
5
7-9
1984
Oryctolagus cuniculus, Rattus norvegicus
brenda
Nashed, N.T.; Michaud, D.P.; Levin, W.; Jerina, D.M.
7-Dehydrocholesterol 5,6 beta-oxide as a mechanism-based inhibitor of microsomal cholesterol oxide hydrolase
J. Biol. Chem.
261
2510-2513
1986
Rattus norvegicus
brenda
Sevanian, A.; McLeod, L.L.
Catalytic properties and inhibition of hepatic cholesterol-epoxide hydrolase
J. Biol. Chem.
261
54-59
1986
Rattus norvegicus
brenda
de Medina, P.; Paillasse, M.R.; Segala, G.; Poirot, M.; Silvente-Poirot, S.
Identification and pharmacological characterization of cholesterol-5,6-epoxide hydrolase as a target for tamoxifen and AEBS ligands
Proc. Natl. Acad. Sci. USA
107
13520-13525
2010
Homo sapiens, Rattus norvegicus
brenda
Segala, G.; de Medina, P.; Iuliano, L.; Zerbinati, C.; Paillasse, M.R.; Noguer, E.; Dalenc, F.; Payre, B.; Jordan, V.C.; Record, M.; Silvente-Poirot, S.; Poirot, M.
5,6-Epoxy-cholesterols contribute to the anticancer pharmacology of tamoxifen in breast cancer cells
Biochem. Pharmacol.
86
175-189
2013
Homo sapiens
brenda
Poirot, M.; Silvente-Poirot, S.
Cholesterol-5,6-epoxides: chemistry, biochemistry, metabolic fate and cancer
Biochimie
95
622-631
2013
Rattus norvegicus
brenda
Silvente-Poirot, S.; Poirot, M.
Cholesterol epoxide hydrolase and cancer
Curr. Opin. Pharmacol.
12
696-703
2012
Homo sapiens
brenda
Voisin, M.; de Medina, P.; Mallinger, A.; Dalenc, F.; Huc-Claustre, E.; et, al.
Identification of a tumor-promoter cholesterol metabolite in human breast cancers acting through the glucocorticoid receptor
Proc. Natl. Acad. Sci. USA
114
E9346-E9355
2017
Homo sapiens
brenda
Poirot, M.; Soules, R.; Mallinger, A.; Dalenc, F.; Silvente-Poirot, S.
Chemistry, biochemistry, metabolic fate and mechanism of action of 6-oxo-cholestan-3beta,5alpha-diol (OCDO), a tumor promoter and cholesterol metabolite
Biochimie
153
139-149
2018
Homo sapiens
brenda
Griffiths, W.J.; Yutuc, E.; Abdel-Khalik, J.; Crick, P.J.; Hearn, T.; Dickson, A.; Bigger, B.W.; Hoi-Yee Wu, T.; Goenka, A.; Ghosh, A.; Jones, S.A.; Covey, D.F.; Ory, D.S.; Wang, Y.
Metabolism of non-enzymatically derived oxysterols clues from sterol metabolic disorders
Free Radic. Biol. Med.
144
124-133
2019
Homo sapiens
brenda
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