Any feedback?
Information on EC 1.1.3.6 - cholesterol oxidase and Organism(s) Brevibacterium sterolicum and UniProt Accession P22637
for references in articles please use BRENDA:EC1.1.3.6Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.1.3.6 cholesterol oxidaseIUBMB Comments
Contains FAD. Cholesterol oxidases are secreted bacterial bifunctional enzymes that catalyse the first two steps in the degradation of cholesterol. The enzyme catalyses the oxidation of the 3beta-hydroxyl group to a keto group, and the isomerization of the double bond in the oxidized steroid ring system from the Delta5 position to Delta6 position (cf. EC 5.3.3.1, steroid Delta-isomerase).
Specify your search results
Word Map
- 1.1.3.6
-
biosensors
-
electrode
- esterase
-
electrochemical
- brevibacterium
-
fabric
- oxidases
-
amperometric
-
film
- rhodococcus
-
raft
- cholestenone
-
voltammetry
- cholest-4-en-3-one
-
flavoenzyme
-
cholesteryl
-
nanocomposite
-
biosensing
- erythropolis
- filipin
- 4-cholesten-3-one
- nocardia
- medicine
-
3hcholesterol
-
electropolymerization
- lavendulae
- biotechnology
- agriculture
-
co-immobilized
- methyl-beta-cyclodextrin
- diagnostics
-
bioelectrode
- luminol
-
screen-printed
-
electrocatalytic
- analysis
-
3.1.1.13
-
polypyrrole
-
multiwalled
- beta-ol
- synthesis
- drug development
The taxonomic range for the selected organisms is: Brevibacterium sterolicum
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
cholesterol oxidase, coase, chori, chom2, chorii, cholox, cho-u, chom1, cod-b, cholesterol oxidase ii, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3beta-hydroxy steroid oxidoreductase
-
-
-
-
3beta-hydroxysteroid:oxygen oxidoreductase
-
-
-
-
CHOD
-
-
-
-
cholesterol-O2 oxidoreductase
-
-
-
-
oxidase, cholesterol
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cholesterol + O2 = cholest-5-en-3-one + H2O2
bifunctional enzyme, catalyzes both the oxidation of DELTA5-ene-3beta hydroxysteroids with a trans A-B ring junction to the corresponding DELTA5-3-ketosteroid with the reduction of oxygen to hydrogen peroxide, and the isomerization to the DELTA4-3-ketosteroid
-
cholesterol + O2 = cholest-5-en-3-one + H2O2
isomerization is not the rate limiting step
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
cholesterol:oxygen oxidoreductase
Contains FAD. Cholesterol oxidases are secreted bacterial bifunctional enzymes that catalyse the first two steps in the degradation of cholesterol. The enzyme catalyses the oxidation of the 3beta-hydroxyl group to a keto group, and the isomerization of the double bond in the oxidized steroid ring system from the Delta5 position to Delta6 position (cf. EC 5.3.3.1, steroid Delta-isomerase).
CAS REGISTRY NUMBER
COMMENTARY
9028-76-6
-
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
7alpha-hydroxy-cholesterol + O2
7alpha-hydroxy-cholest-4-en-3-one + H2O2
-
-
-
?
7beta-hydroxy-cholesterol + O2
7beta-hydroxy-cholest-4-en-3-one + H2O2
-
-
-
?
beta-cholestanol + O2
?
13% activity compared to cholesterol
-
-
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
20% activity compared to cholesterol
-
-
?
beta-stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
10% activity compared to cholesterol
-
-
?
dehydroepiandrosterone + O2
androst-5-en-3,17-dione + H2O2
41% activity compared to cholesterol
-
-
?
pregnenolone + O2
5-pregnen-3,20-dione + H2O2
22% activity compared to cholesterol
-
-
?
7E,22-ergostadien-3beta-ol + O2
7E,22-ergostadien-3-one + H2O2
-
-
-
?
beta-sitosterol + O2
?
-
about 55% of the activity with cholesterol, cholesterol oxidase II
-
-
?
dehydroepiandrosterone + O2
androst-5-en-3,17-dione + H2O2
-
41.4% of the activity with cholesterol
-
?
pregnenolone + O2
5-pregnen-3,20-dione + H2O2
-
22.4% of activity with chelesterol
-
?
additional information
?
-
no activity with ergosterol
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
100% activity
-
-
?
5alpha-cholestan-3beta-ol + O2
5alpha-cholestan-3-one + H2O2
-
-
-
?
5alpha-cholestan-3beta-ol + O2
5alpha-cholestan-3-one + H2O2
-
13.2% of activity with cholesterol
-
-
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
-
19.7% of activity with cholesterol
-
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
-
about 30% of the activity with cholesterol, cholesterol oxidase I
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
overview: substrate specificity
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
specific for steroid substrates with an OH group in position 3, preference for steroids with at least a C2 chain at position C17
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
-
first step in cholesterol degradation
-
?
dehydro-epi-androsterone + O2
?
-
about 35% of the activity with cholesterol, cholesterol oxidase I
-
-
?
dehydro-epi-androsterone + O2
?
-
about 5% of the activity with cholesterol, cholesterol oxidase II
-
-
?
pregnenolone + O2
?
-
about 60% of the activity with cholesterol, cholesterol oxidase I
-
-
?
pregnenolone + O2
?
-
about 60% of the activity with cholesterol, cholesterol oxidase II
-
-
?
stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
-
10% of activity with cholesterol
-
-
?
stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
-
about 10% of the activity with cholesterol, cholesterol oxidase I
-
-
?
stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
-
about 10% of the activity with cholesterol, cholesterol oxidase II
-
-
?
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
beta-cholestanol + O2
?
13% activity compared to cholesterol
-
-
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
20% activity compared to cholesterol
-
-
?
beta-stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
10% activity compared to cholesterol
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
100% activity
-
-
?
dehydroepiandrosterone + O2
androst-5-en-3,17-dione + H2O2
41% activity compared to cholesterol
-
-
?
pregnenolone + O2
5-pregnen-3,20-dione + H2O2
22% activity compared to cholesterol
-
-
?
additional information
?
-
no activity with ergosterol
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
-
first step in cholesterol degradation
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
the type II cholesterol oxidase fully active enzyme contains covalently bound FAD
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
p-chloromercuribenzoate
-
1 mM, 20% inhibition, 0.1 mM, 14% inhibition
Triton X-100
-
strong decrease in enzyme activity at concentration of 0.2% Triton X-100 or higher
additional information
-
not inhibited by 1% Triton X-100, 1% Tween 20, 1% sodium cholate and 1% CHAPS
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cholic acid
-
stimulates without a significant change in Km in the presence of low Triton X-100 concentrations, changes the sigmoidal kinetic into normal Michaelis-Menten kinetic with reduced Km in the presence of high Triton X-100 concentrations
dodecylpoly(ethylene glycol ether)9-10
-
trivial name thesit, 0.1 mM cholesterol: increase in enzyme activity in the presence of 0.1% to 2% thesit, 0.34 mM cholesterol: sharp decrease with increasing thesit concentrations
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.27
5-Cholesten-3-one
-
assay relies on spectroscopic detection of 4-cholesten-3-one formation
0.8
trans-androsterone
-
substrate trans-androsterone, 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
3beta-hydroxy-androst-5-en-17-one
-
assay relies on detection of H2O2 formation
1.2
3beta-hydroxy-androst-5-en-17-one
-
assay relies on spectroscopic detection of 4-cholesten-3-one formation
0.2
cholestanol
-
substrate cholestanol, 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
0.04
cholesterol
-
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
cholesterol
-
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
0.11
cholesterol
-
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
cholesterol
-
assay relies on spectroscopic detection of 4-cholesten-3-one formation
0.14
cholesterol
-
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
cholesterol
-
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
0.25
cholesterol
-
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
0.47
cholesterol
-
H69A mutant enzyme, 50 mM phosphate buffer, pH 7.5, 1% thesit, 1% 2-propanol
0.45
O2
-
H69A mutant enzyme, 50 mM phosphate buffer, pH 7.5, 1% thesit, 1% 2-propanol
0.2
pregnenolone
-
substrate pregnenolone, 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
0.4
pregnenolone
-
assay relies on spectroscopic detection of 4-cholesten-3-one formation
0.4
pregnenolone
-
substrate pregnenolone, detection of product formation at 240 nm. 0.1 M potassium phosphate, 1% Triton X-100, 1.25% propan-2-ol, 25°C and pH 7.5
0.9
trans-dehydroandrosterone
-
substrate trans-dehydroandrosterone, 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
1.2
trans-dehydroandrosterone
-
substrate trans-dehydroandrosterone, detection of product formation at 240 nm. 0.1 M potassium phosphate, 1% Triton X-100, 1.25% propan-2-ol, 25°C and pH 7.5
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.8
3beta-hydroxy-androst-5-en-17-one
-
product formation followed at 240 nm in the presence of 0.02 ml H2O2, substrate dissolved in Triton X-100, 100 mM phosphate buffer
0.8
trans-androsterone
-
substrate trans-androsterone, 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
3beta-hydroxy-5-androsten-17-one
-
assay relies on detection of H2O2 formation
0.8
3beta-hydroxy-5-androsten-17-one
-
H2O2 production assayed, 100 mM phosphate buffer
28
5-Cholesten-3-one
-
H69A mutant enzyme, 5-cholesten-3-one isomerization, 50 mM phosphate buffer, 1% thesit, 1% 2-propanol
250
5-Cholesten-3-one
-
isomerization to 4-cholesten-3-one, rapid reaction, stopped-flow measurement, 500 mM phosphate buffer, pH 7.5, in the presence of 1% thesit and 1.25% 2-propanol
278
5-Cholesten-3-one
-
assay relies on spectroscopic detection of 4-cholesten-3-one formation
40
cholestanol
-
substrate cholestanol, 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
0.55
cholesterol
-
H69A mutant enzyme, steady state, 50 mM phosphate buffer, 1% thesit, 1% 2-propanol
0.8
cholesterol
-
assay relies on spectroscopic detection of 4-cholesten-3-one formation, decreasing length of C17 chain affects turnover negatively
1.6
cholesterol
-
H69A mutant enzyme, cholesterol oxidation, 50 mM phosphate buffer, 1% thesit, 1% 2-propanol
43
cholesterol
-
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
48
cholesterol
-
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
cholesterol
-
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
cholesterol
-
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
cholesterol
-
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
cholesterol
-
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
67
cholesterol
-
assay relies on spectroscopic detection of 4-cholesten-3-one formation
67
cholesterol
-
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
105
cholesterol
-
50 mM phosphate buffer, pH 7.5, 1% thesit, 10% 2-propanol
21
pregnenolone
-
assay relies on spectroscopic detection of 4-cholesten-3-one formation
21
pregnenolone
-
product formation followed at 240 nm in the presence of 0.02 ml H2O2, substrate dissolved in Triton X-100, 100 mM phosphate buffer
21
pregnenolone
-
substrate pregnenolone, detection of product formation at 240 nm. 0.1 M potassium phosphate, 1% Triton X-100, 1.25% propan-2-ol, 25°C and pH 7.5
35
pregnenolone
-
substrate pregnenolone, 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
trans-dehydroandrosterone
-
substrate trans-dehydroandrosterone, detection of product formation at 240 nm. 0.1 M potassium phosphate, 1% Triton X-100, 1.25% propan-2-ol, 25°C and pH 7.5
1
trans-dehydroandrosterone
-
substrate trans-dehydroandrosterone, 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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
comparison of relative activity of ChOx from different sources
additional information
comparison of the effect of detergents and solvents on ChOx activity and stability (from different sources)
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 8.5
-
pH 5.0: about 75% of maximalm acttivity, pH 8.5: about 60% of maximal activity, cholesterol oxidase II
5.5 - 8.5
-
pH 5.5: about 50% of maximal activity, pH 8.5: about 40% of maximal activity, cholesterol oxidase I
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.9
-
isoelectric focusing with carrier ampholites pH 4-6, cholesterol oxidase II
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
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). PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals of recombinant His-tagged enzyme, vapor diffusion by hanging drop, space group P21
-
structure of substrate-enzyme complex, 1.8 A resolution, substrate binds in internal cavity which is totally sealed from solvent
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E311D
-
mutations of Glu311 cause a switch in the basic kinetic mechanism of the reaction of reduced cholesterol oxidase with dioxygen: wild-type cholesterol oxidase shows a saturation behavior with increasing oxygen concentration, while for Glu311 mutants a linear dependence is found that is assumed to reflect a simple second order process
E311L
-
mutations of Glu311 cause a switch in the basic kinetic mechanism of the reaction of reduced cholesterol oxidase with dioxygen: wild-type cholesterol oxidase shows a saturation behavior with increasing oxygen concentration, while for Glu311 mutants a linear dependence is found that is assumed to reflect a simple second order process
E311Q
-
mutations of Glu311 cause a switch in the basic kinetic mechanism of the reaction of reduced cholesterol oxidase with dioxygen: wild-type cholesterol oxidase shows a saturation behavior with increasing oxygen concentration, while for Glu311 mutants a linear dependence is found that is assumed to reflect a simple second order process
H69A
additional information
-
development and evaluation of a cholesterol biosensor based on immobilized cholesterol esterase and cholesterol oxidase on oxygen electrode for the determination of total cholesterol in food samples
H69A
-
site-directed mutagenesis, the mutant does not bind FAD, the mutant is more sensitive to urea and unfolds at lower urea concentrations of 3 M compared to the wild-type enzyme at 5 M, the mutant also has a lower melting temperature
H69A
-
mutation results in a significant decrease in activity, in the midpoint redox potential of the flavin, and in stability with respect to the wild-type enzyme, but does not modify the overall structure of the enzyme
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
60
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
65% activity remains after 24 h at 25°C in 50 mM potassium phosphate, pH 7.5, enzyme is completely stable for 300 min in the presence of 1% propan-2-ol and 1% thesit as well as in the presence of 10% propan-2-ol and 8% thesit
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
propan-2-ol
the activity of the enzyme is rapidly inactivated in the presence of 30% (v/v) propan-2-ol at 25°C
urea
-
the apoprotein of the mutant H69A lacks the characteristic tertiary structure of the holoprotein and displays larger hydrophobic surfaces. Its urea-induced unfolding does not occur by a simple two-state mechanism and is largely nonreversible. Minor alterations in the flavin binding region are evident between the native and the refolded proteins, and are likely responsible for the low refolding yield observed
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0-5°C, crystallized enzyme in lyophilized state, in the dark, stable for at least 10 months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cholesterol oxidase II, expression in Escherichia coli MM294/pnH10
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
unfolding and folding after urea treatment of wild-type enzyme and mutant H69A, equilibrium unfolding study, kinetics
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
recombinant expression in plants gives insect resistance
biotechnology
biocatalysis, industrial steroid drug production, steroid production as diagnostic tool
diagnostics
analytic tool for determining cholesterol in various samples
analysis
-
the enzyme can be used as cholesterol biosensor co-immobilized with cholesterol esterase on oxygen electrodes, determination of total cholesterol in food samples
biotechnology
-
Cholesterol oxidase has two major biotechnological applications, i.e. in the determination of serum (and food) cholesterol levels and as biocatalyst providing valuable intermediates for industrial steroid drug production
medicine
-
determination of cholesterol in various sample types, determination of cholesterol in gall stones, determination of cholesterol on the cell membrane of erythrocytes, other cells and cellular compartments
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Uwajima, T.; Yagi, H.; Terado, O.
Properties of crystalline 3beta-hydroxysteroid oxidase of Brevibacterium sterolicum
Agric. Biol. Chem.
38
1149-1156
1974
Brevibacterium sterolicum
-
Uwajima, T.; Terada, O.
On the kinetics of cholesterol oxidase from Brevibacterium sterolicum in the presence of detergents
Agric. Biol. Chem.
42
1453-1454
1978
Brevibacterium sterolicum
-
Uwajima, T.; Yagi, H.; Nakamura, S.; Terada, O.
Isolation and crystallization of extracellular 3beta-hydroxysteroid oxidase of Brevibacterium sterolicum nov. Sp.
Agric. Biol. Chem.
37
2345-2350
1973
Brevibacterium sterolicum
-
Smith, A.G.; Brooks, C.J.W.
Cholesterol oxidases: properties and applications
J. Steroid Biochem.
7
705-713
1976
Streptomyces violascens, Brevibacterium sterolicum, Nocardia erythropolis
Li, J.; Vrielink, A.; Brick, P.; Blow, D.M.
Crystal structure of cholesterol oxidase complexed with a steroid substrate: implications for flavin adenine dinucleotide dependent alcohol oxidases
Biochemistry
32
11507-11515
1993
Brevibacterium sterolicum
Croteau, N.; Vrielink, A.
Crystallization and preliminary x-ray analysis of cholesterol oxidase from Brevibacterium sterolicum containing covalently bound FAD
J. Struct. Biol.
116
317-319
1996
Brevibacterium sterolicum
Gadda, G.; Wels, G.; Pollegioni, L.; Zucchelli, S.; Amrosius, D.; Pilone, M.S.; Ghisla, S.
Characterization of cholesterol oxidase from Streptomyces hygroscopicus and Brevibacterium sterolicum
Eur. J. Biochem.
250
369-376
1997
Brevibacterium sterolicum, Streptomyces hygroscopicus
Pollegioni, L.; Gadda, G.; Ambrosius, D.; Ghisla, S.; Pilone, M.S.
Cholesterol oxidase from Streptomyces hycroscopicus and Brevibacterium sterolicum: effect of surfactants and organic solvents on activity
Biotechnol. Appl. Biochem.
30
27-33
1999
Brevibacterium sterolicum, Streptomyces hygroscopicus
Pollegioni, L.; Wels, G.; Pilone, M.S.; Ghisla, S.
Kinetic mechanisms of cholesterol oxidase from Streptomyces hygroscopicus and Brevibacterium sterolicum
Eur. J. Biochem.
264
140-151
1999
Brevibacterium sterolicum, Streptomyces hygroscopicus
MacLachlan, J.; Wotherspoon, A.T.L.; Ansell, R.O.; Brooks, C.J.W.
Cholesterol oxidase: sources, physical properties and analytical applications
J. Steroid Biochem. Mol. Biol.
72
169-195
2000
Streptomyces lavendulae, Streptomyces violascens, Pimelobacter simplex, Brevibacterium sterolicum, Streptomyces sp., Comamonas testosteroni, Rhodococcus equi, Corynebacterium cholesterolicum, Mycobacterium sp., Nocardia erythropolis, Nocardia rhodochrous, Nocardia sp., Pseudomonas sp., Rhodococcus erythropolis, Rhodococcus sp., Schizophyllum commune, Streptomyces griseocarneus, Streptomyces hygroscopicus, Streptomyces lividans, Rhodococcus sp. GK1
Motteront, L.; Pilonet, M.S.; Molla, G.; Ghisla, S.; Pollegioni, L.
Cholesterol oxidase from Brevibacterium sterolicum
J. Biol. Chem.
276
18024-18030
2001
Brevibacterium sterolicum
Doukyu, N.; Aono, R.
Cloning, sequence analysis and expression of a gene encoding an organic solvent- and detergent-tolerant cholesterol oxidase of Burkholderia cepacia strain ST-200
Appl. Microbiol. Biotechnol.
57
146-152
2001
Brevibacterium sterolicum, Burkholderia cepacia, Streptomyces sp., Nocardia erythropolis, Pseudomonas sp., Burkholderia cepacia ST-200
Fujishiro, K.; Uchida, H.; Shimokawa, K.; Nakano, M.; Sano, F.; Ohta, T.; Kayahara, N.; Aisaka, K.; Uwajima, T.
Purification and properties of a new Brevibacterium sterolicum cholesterol oxidase produced by E. coli MM294/pnH10
FEMS Microbiol. Lett.
215
243-248
2002
Brevibacterium sterolicum
Basu, A.K.; Chattopadhyay, P.; Roychoudhuri, U.; Chakraborty, R.
Development of cholesterol biosensor based on immobilized cholesterol esterase and cholesterol oxidase on oxygen electrode for the determination of total cholesterol in food samples
Bioelectrochemistry
70
375-379
2006
Brevibacterium sterolicum
Caldinelli, L.; Iametti, S.; Barbiroli, A.; Bonomi, F.; Fessas, D.; Molla, G.; Pilone, M.S.; Pollegioni, L.
Dissecting the structural determinants of the stability of cholesterol oxidase containing covalently bound flavin
J. Biol. Chem.
280
22572-22581
2005
Brevibacterium sterolicum
Piubelli, L.; Pedotti, M.; Molla, G.; Feindler-Boeckh, S.; Ghisla, S.; Pilone, M.S.; Pollegioni, L.
On the oxygen reactivity of flavoprotein oxidases: An oxygen access tunnel and gate in Brevibacterium sterolicum cholesterol oxidase
J. Biol. Chem.
283
24738-24747
2008
Brevibacterium sterolicum
Aparicio, J.F.; Martin, J.F.
Microbial cholesterol oxidases: bioconversion enzymes or signal proteins?
Mol. Biosyst.
4
804-809
2008
Arthrobacter sp., Streptomyces sp., Rhodococcus equi, Rhodococcus erythropolis, Rhodococcus rhodochrous, Schizophyllum commune, Brevibacterium sterolicum (P22637)
Caldinelli, L.; Iametti, S.; Barbiroli, A.; Fessas, D.; Bonomi, F.; Piubelli, L.; Molla, G.; Pollegioni, L.
Relevance of the flavin binding to the stability and folding of engineered cholesterol oxidase containing noncovalently bound FAD
Protein Sci.
17
409-419
2008
Brevibacterium sterolicum
Vrielink, A.; Ghisla, S.
Cholesterol oxidase: biochemistry and structural features
FEBS J.
276
6826-6843
2009
Brevibacterium sterolicum, Streptomyces hygroscopicus
Pollegioni, L.; Piubelli, L.; Molla, G.
Cholesterol oxidase: biotechnological applications
FEBS J.
276
6857-6870
2009
Streptomyces violascens, Arthrobacter sp., Rhodococcus equi, Mycobacterium sp., Nocardia erythropolis, Nocardia rhodochrous, Pseudomonas spp., Schizophyllum commune, uncultured Gammaproteobacteria bacterium, Streptoverticillum cholesterolicum, Brevibacterium sterolicum (P22637), uncultured Gammaproteobacteria bacterium Y-134
Doukyu, N.
Characteristics and biotechnological applications of microbial cholesterol oxidases
Appl. Microbiol. Biotechnol.
83
825-837
2009
Arthrobacter sp., Arthrobacter sp. (Q56DL0), Arthrobacter sp. IM79, Brevibacterium sterolicum (P22637), Burkholderia cepacia (Q93RE1), Burkholderia cepacia ST-200 (Q93RE1), Burkholderia pseudomallei, Burkholderia thailandensis (Q2T0X3), Chromobacterium sp. (B5MGF8), Corynebacterium cholesterolicum, Corynebacterium urealyticum (B1VGH1), Corynebacterium urealyticum DSM 7109 (B1VGH1), Mycobacterium leprae (Q59530), Mycobacterium tuberculosis (P9WMV9), Mycobacterium tuberculosis H37Rv (P9WMV9), Nocardia farcinica (Q5YRJ2), Nocardia farcinica IFM 10152 (Q5YRJ2), Nocardia rhodochrous, Nocardia sp., Paraburkholderia xenovorans (Q13UN0), Pimelobacter simplex, Pseudomonas aeruginosa, Pseudomonas sp., Pseudomonas sp. COX629, Rhodococcus equi (A0A3S5YA89), Rhodococcus equi 103S (A0A3S5YA89), Rhodococcus erythropolis (A9QAE7), Schizophyllum commune, Streptomyces avermitilis (Q93H76), Streptomyces coelicolor (Q9L0H6), Streptomyces fradiae, Streptomyces griseus (A7RA76), Streptomyces natalensis (Q9EW96), Streptomyces sp. (P12676), Streptomyces sp. (Q55020), Streptomyces violascens, Streptoverticillium cholesterolieum, uncultured Gammaproteobacteria bacterium, uncultured Gammaproteobacteria bacterium Y-134
EXTERNAL LINKS (specific for EC-Number 1.1.3.6)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
