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Information on EC 1.1.3.6 - cholesterol oxidase
for references in articles please use BRENDA:EC1.1.3.6
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.3 With oxygen as acceptor
1.1.3.6 cholesterol oxidase
IUBMB 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 3β-hydroxyl group to a keto group, and the isomerization of the double bond in the oxidized steroid ring system from the Δ5 position to Δ6 position (cf. EC 5.3.3.1, steroid Δ-isomerase).
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
- 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
showSynonyms
cholesterol oxidase, coase, chom2, chori, cholox, chorii, cho-u, chom1, cod-b, cholesterol oxidase ii, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3beta-hydroxy steroid oxidoreductase
-
-
-
-
3beta-hydroxysteroid:oxygen oxidoreductase
-
-
-
-
3beta-hydroxysterol oxidase
CgChoA
CHO
ChoA
choBb
CHOD
ChoG
ChoL
cholesterol oxidase
cholesterol-O2 oxidoreductase
-
-
-
-
choM
ChoM1
ChoM2
choP
ChoRI
ChoRII
ChOx
CO1
COD
HCEO-forming enzyme
HMPREF0204_11499
oxidase, cholesterol
-
-
-
-
PimE
CHOD
-
-
-
-
ChoG
a class II cholesterol oxidase
ChoG
a class II cholesterol oxidase
-
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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
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
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
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
Nocardia rhodochrous
-
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
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
Nocardia erythropolis
-
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
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
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
Corynebacterium cholesterolicum
-
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
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
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
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
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
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
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
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
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
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
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
-
cholesterol + O2 = cholest-5-en-3-one + H2O2
isomerization is not the rate limiting step
-
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
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
redox reaction
-
-
radical or hydride transfer mechanism
-
reduction
-
-
-
-
oxidation
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
cholesterol degradation to androstenedione I (cholesterol oxidase)
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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).
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CAS REGISTRY NUMBER
COMMENTARY
9028-76-6
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
17beta-hydroxymethyl-5-androsten-3beta-ol + O2
17beta-hydroxymethyl-5-androsten-3-one + H2O2
Nocardia erythropolis
-
Substrates: -
Products: -
Products: -
?
20,22-dihydroxycholesterol + O2
20,22-dihydroxycholest-5-en-3-one + H2O2
Nocardia erythropolis
-
Substrates: -
Products: -
Products: -
?
20,25-diazacholesterol + O2
20,25-diazacholest-4-en-3-one + H2O2
Nocardia erythropolis
-
Substrates: -
Products: -
Products: -
?
20-hydroxycholesterol + O2
20-hydroxycholest-5-en-3-one + H2O2
Nocardia erythropolis
-
Substrates: -
Products: -
Products: -
?
22-hydroxycholesterol + O2
22-hydroxycholest-5-en-3-one + H2O2
Nocardia erythropolis
-
Substrates: -
Products: -
Products: -
?
23,24-dinor-5-cholen-3beta,22-diol + O2
23,24-dinor-5-cholen-22-ol-3-one + H2O2
Nocardia erythropolis
-
Substrates: -
Products: -
Products: -
?
23,24-dinor-5-cholene-3beta,22-diol + O2
23,24-dinor-5-cholen-22-ol-3-one + H2O2
Nocardia erythropolis
-
Substrates: -
Products: -
Products: -
r
24-hydroxycholesterol + O2
24-hydroxycholest-5-en-3-one + H2O2
Nocardia erythropolis
-
Substrates: -
Products: -
Products: -
?
24-oxocholesterol + O2
24-oxocholest-5-en-3-one + H2O2
Nocardia erythropolis
-
Substrates: -
Products: -
Products: -
?
25-hydroxycholesterol + O2
25-hydroxycholest-5-en-3-one + H2O2
Nocardia erythropolis
-
Substrates: -
Products: -
Products: -
?
26-hydroxycholesterol + O2
26-hydroxycholest-5-en-3-one + H2O2
Nocardia erythropolis
-
Substrates: -
Products: -
Products: -
?
3beta-hydroxyandrost-5-en-17-one + O2
androst-5-en-3,17-dione + H2O2
-
Substrates: 30% of the activity with cholesterol
Products: -
Products: -
?
4,4-dimethylcholesterol + O2
4,4-dimethylcholest-5-en-3-one
Nocardia erythropolis
-
Substrates: -
Products: -
Products: -
?
4alpha-methylcholesterol + O2
4alpha-methylcholest-5-en-3-one + H2O2
Nocardia erythropolis
-
Substrates: -
Products: -
Products: -
?
4beta-methylcholesterol + O2
4beta-methylcholest-5-en-3-one + H2O2
Nocardia erythropolis
-
Substrates: -
Products: -
Products: -
?
5,7-cholestadien-3beta-ol + O2
5,7-cholestadien-3-one + H2O2
Nocardia erythropolis
-
Substrates: -
Products: -
Products: -
?
5-androstene-3beta,17beta-diol + O2
5-androsten-17beta-ol-3-one + H2O2
Nocardia erythropolis
-
Substrates: -
Products: -
Products: -
?
5-cholene-3beta,24-diol + O2
5-cholen-24-ol-3-one + H2O2
Nocardia erythropolis
-
Substrates: -
Products: -
Products: -
?
5-pregnen-3,20-dione + O2
pregnenolone + H2O2
Nocardia erythropolis
-
Substrates: -
Products: -
Products: -
r
5-pregnen-3beta,20beta-diol + O2
5-pregnen-20beta-ol-3-one + H2O2
Nocardia erythropolis
-
Substrates: -
Products: -
Products: -
?
5alpha-androstan-3-ol-17-one + O2
5alpha-androstan-3,17-dione + H2O2
-
Substrates: 15% of the activity with cholesterol
Products: -
Products: -
?
5alpha-cholest-8(14)-en-3beta-ol + O2
5alpha-cholest-8(14)-en-3-one + H2O2
Nocardia erythropolis
-
Substrates: -
Products: -
Products: -
?
androst-4-ene-3,17-dione + O2
? + H2O2
Substrates: -
Products: -
Products: -
?
beta-stigmasterol + O2
?
-
Substrates: 36% of the activity with cholesterol
Products: -
Products: -
?
cholest-4-en-3-one + O2
? + H2O2
Substrates: -
Products: -
Products: -
?
cholest-5-en-3beta-ol 7-one + O2
cholest-5-en-3,17-dione + H2O2
-
Substrates: low activity with wild-type and mutant enzymes L119A, L119F, V145Q, P357N, Q286R and S379T
Products: -
Products: -
?
cyclohexanol + O2
cyclohexanal + H2O2
-
Substrates: -
Products: -
Products: -
?
dehydroandrosterone + O2
? + H2O2
Substrates: -
Products: -
Products: -
?
dehydroepiandrosterone + O2
?
-
Substrates: 27% of the activity with cholesterol
Products: -
Products: -
?
dehydroepiandrosterone + O2
? + H2O2
-
Substrates: 30% activity compared to cholesterol
Products: -
Products: -
?
epiandrosterone + O2
? + H2O2
-
Substrates: 15% activity compared to cholesterol
Products: -
Products: -
?
ergosta-5,7,22-trien-3beta-ol + O2
ergostan-5,7,22-trien-3-one + H2O2
-
Substrates: 18% of the activity with cholesterol
Products: -
Products: -
?
estrone + O2
estra-1,5(10)-dien-3,17-dione + H2O2
-
Substrates: low activity with wild-type enzyme, no activity with mutant enzymes L119A, L119F, V145Q, P357N, Q286R and S379T
Products: -
Products: -
?
lanosterol + O2
lanosta-8,24-dien-3-one + H2O2
-
Substrates: slow rate
Products: -
Products: -
?
1,4-androstadiene-3,17-dione + H2O
?
-
Substrates: 11% of the activity with cholesterol, enzyme CO1
Products: -
Products: -
?
1,4-androstadiene-3,17-dione + H2O
?
-
Substrates: 11% of the activity with cholesterol, enzyme CO1
Products: -
Products: -
?
3-betacholestanol + O2
? + H2O2
Substrates: -
Products: -
Products: -
?
3beta-chlorocholest-5-ene + O2
? + H2O2
Substrates: low activity
Products: -
Products: -
?
3beta-chlorocholest-5-ene + O2
? + H2O2
Substrates: -
Products: -
Products: -
?
3beta-hydroxypregn-5-en-20-one + O2
pregn-5-en-3,20-dione + H2O2
-
Substrates: 42% of the activity with cholesterol
Products: -
Products: -
?
3beta-hydroxypregn-5-en-20-one + O2
pregn-5-en-3,20-dione + H2O2
-
Substrates: 42% of the activity with cholesterol
Products: -
Products: -
?
5alpha-cholestan-3beta-ol + O2
5alpha-cholestan-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
5alpha-cholestan-3beta-ol + O2
5alpha-cholestan-3-one + H2O2
-
Substrates: 13.2% of activity with cholesterol
Products: -
Products: -
?
5alpha-cholestan-3beta-ol + O2
5alpha-cholestan-3-one + H2O2
Nocardia erythropolis
-
Substrates: -
Products: -
Products: -
?
5alpha-cholestan-3beta-ol + O2
5alpha-cholestan-3-one + H2O2
Nocardia erythropolis
-
Substrates: 87% of activity
Products: -
Products: -
?
5alpha-cholestan-3beta-ol + O2
5alpha-cholestan-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
5alpha-cholestan-3beta-ol + O2
5alpha-cholestan-3-one + H2O2
-
Substrates: equally active as cholesterol
Products: -
Products: -
?
5alpha-cholestan-3beta-ol + O2
5alpha-cholestan-3-one + H2O2
-
Substrates: equally active as cholesterol
Products: -
Products: -
?
5alpha-cholestan-3beta-ol + O2
5alpha-cholestan-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
5alpha-cholestane + O2
?
-
Substrates: 72% of the activity with cholesterol, enzyme CO1
Products: -
Products: -
?
5alpha-cholestane + O2
?
-
Substrates: 90% of the activity with cholesterol, enzyme CO2
Products: -
Products: -
?
5alpha-cholestane + O2
?
-
Substrates: 72% of the activity with cholesterol, enzyme CO1
Products: -
Products: -
?
5alpha-cholestane-3beta-ol-7-one + O2
5alpha-cholestane-3,7,dione
-
Substrates: 74% of the activity with cholesterol, enzyme CO1
Products: -
Products: -
?
5alpha-cholestane-3beta-ol-7-one + O2
5alpha-cholestane-3,7,dione
-
Substrates: 84% of the activity with cholesterol, enzyme CO2
Products: -
Products: -
?
7-dehydrocholesterol + O2
cholest-4,7-dien-3-one + H2O2
-
Substrates: 26% of the activity with cholesterol
Products: -
Products: -
?
7-dehydrocholesterol + O2
cholest-4,7-dien-3-one + H2O2
-
Substrates: 14% of the activity with cholesterol
Products: -
Products: -
?
7-keto-cholesterol + O2
?
-
Substrates: -
Products: -
Products: -
?
7-keto-cholesterol + O2
?
-
Substrates: -
Products: -
Products: -
?
7alpha-hydroxy-cholesterol + O2
7alpha-hydroxy-cholest-4-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
7alpha-hydroxy-cholesterol + O2
7alpha-hydroxy-cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
7alpha-hydroxy-cholesterol + O2
7alpha-hydroxy-cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
7alpha-hydroxy-cholesterol + O2
7alpha-hydroxy-cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
7beta-hydroxy-cholesterol + O2
7beta-hydroxy-cholest-4-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
7beta-hydroxy-cholesterol + O2
7beta-hydroxy-cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
7beta-hydroxy-cholesterol + O2
7beta-hydroxy-cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
7beta-hydroxy-cholesterol + O2
7beta-hydroxy-cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
7E,22-ergostadien-3beta-ol + O2
7E,22-ergostadien-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
7E,22-ergostadien-3beta-ol + O2
7E,22-ergostadien-3-one + H2O2
Nocardia erythropolis
-
Substrates: -
Products: -
Products: -
?
7E,22-ergostadien-3beta-ol + O2
7E,22-ergostadien-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
beta-cholestanol + O2
?
Substrates: 13% activity compared to cholesterol
Products: -
Products: -
?
beta-cholestanol + O2
?
Substrates: 69% activity compared to cholesterol
Products: -
Products: -
?
beta-cholestanol + O2
?
Substrates: 69% activity compared to cholesterol
Products: -
Products: -
?
beta-cholestanol + O2
?
Substrates: 95% activity compared to cholesterol
Products: -
Products: -
?
beta-cholestanol + O2
?
-
Substrates: 95% of the activity with cholesterol
Products: -
Products: -
?
beta-cholestanol + O2
?
-
Substrates: 78% activity compared to cholesterol
Products: -
Products: -
?
beta-cholestanol + O2
?
-
Substrates: 78% activity compared to cholesterol
Products: -
Products: -
?
beta-cholestanol + O2
?
P12676, Q55020
Substrates: 75% activity compared to cholesterol
Products: -
Products: -
?
beta-cholestanol + O2
?
-
Substrates: 101% activity compared to cholesterol
Products: -
Products: -
?
beta-cholestanol + O2
?
Streptoverticillium cholesterolieum
-
Substrates: 96% activity compared to cholesterol
Products: -
Products: -
?
beta-cholestanol + O2
?
-
Substrates: 79% activity compared to cholesterol
Products: -
Products: -
?
beta-cholestanol + O2
?
-
Substrates: 79% activity compared to cholesterol
Products: -
Products: -
?
beta-cholestanol + O2
? + H2O2
-
Substrates: 96% activity compared to cholesterol
Products: -
Products: -
?
beta-cholestanol + O2
? + H2O2
Streptomyces rimosus MTCC 10792
-
Substrates: 96% activity compared to cholesterol
Products: -
Products: -
?
beta-sitosterol + O2
?
-
Substrates: about 55% of the activity with cholesterol, cholesterol oxidase II
Products: -
Products: -
?
beta-sitosterol + O2
?
-
Substrates: 80% of the activity with cholesterol
Products: -
Products: -
?
beta-sitosterol + O2
?
-
Substrates: -
Products: -
Products: -
?
beta-sitosterol + O2
? + H2O2
Substrates: -
Products: -
Products: -
?
beta-sitosterol + O2
? + H2O2
-
Substrates: 88% activity compared to cholesterol
Products: -
Products: -
?
beta-sitosterol + O2
? + H2O2
Streptomyces rimosus MTCC 10792
-
Substrates: 88% activity compared to cholesterol
Products: -
Products: -
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
-
Substrates: 57% of the activity with cholesterol, enzyme CO1
Products: -
Products: -
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
-
Substrates: 79% of the activity with cholesterol, enzyme CO2
Products: -
Products: -
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
-
Substrates: 19.7% of activity with cholesterol
Products: -
Products: -
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
-
Substrates: about 30% of the activity with cholesterol, cholesterol oxidase I
Products: -
Products: -
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
Substrates: 20% activity compared to cholesterol
Products: -
Products: -
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
Substrates: 84% activity compared to cholesterol
Products: -
Products: -
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
Substrates: 84% activity compared to cholesterol
Products: -
Products: -
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
Substrates: 80% activity compared to cholesterol
Products: -
Products: -
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
Corynebacterium cholesterolicum
-
Substrates: 50% activity compared to cholesterol
Products: -
Products: -
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
-
Substrates: 19% of the activity with cholesterol
Products: -
Products: -
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
-
Substrates: 29% of the activity with cholesterol
Products: -
Products: -
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
Nocardia erythropolis
-
Substrates: -
Products: -
Products: -
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
Substrates: 64% activity compared to cholesterol
Products: -
Products: -
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
-
Substrates: 85% activity compared to cholesterol
Products: -
Products: -
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
-
Substrates: 85% activity compared to cholesterol
Products: -
Products: -
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
Substrates: 64% activity compared to cholesterol
Products: -
Products: -
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
P12676, Q55020
Substrates: 72% activity compared to cholesterol
Products: -
Products: -
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
-
Substrates: 64% activity compared to cholesterol
Products: -
Products: -
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
Streptoverticillium cholesterolieum
-
Substrates: 39% activity compared to cholesterol
Products: -
Products: -
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
-
Substrates: 29% activity compared to cholesterol
Products: -
Products: -
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
-
Substrates: 29% activity compared to cholesterol
Products: -
Products: -
?
beta-stigmasterol + O2
? + H2O2
-
Substrates: 68% activity compared to cholesterol
Products: -
Products: -
?
beta-stigmasterol + O2
? + H2O2
Streptomyces rimosus MTCC 10792
-
Substrates: 68% activity compared to cholesterol
Products: -
Products: -
?
beta-stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
Substrates: 10% activity compared to cholesterol
Products: -
Products: -
?
beta-stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
Substrates: 59% activity compared to cholesterol
Products: -
Products: -
?
beta-stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
Substrates: 59% activity compared to cholesterol
Products: -
Products: -
?
beta-stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
Substrates: 36% activity compared to cholesterol
Products: -
Products: -
?
beta-stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
Corynebacterium cholesterolicum
-
Substrates: 12% activity compared to cholesterol
Products: -
Products: -
?
beta-stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
-
Substrates: 47% activity compared to cholesterol
Products: -
Products: -
?
beta-stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
Substrates: -
Products: -
Products: -
?
beta-stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
Substrates: -
Products: -
Products: -
?
beta-stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
-
Substrates: 40% activity compared to cholesterol
Products: -
Products: -
?
beta-stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
-
Substrates: 40% activity compared to cholesterol
Products: -
Products: -
?
beta-stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
Substrates: 33% activity compared to cholesterol
Products: -
Products: -
?
beta-stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
-
Substrates: 83% activity compared to cholesterol
Products: -
Products: -
?
beta-stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
-
Substrates: 83% activity compared to cholesterol
Products: -
Products: -
?
beta-stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
Substrates: 33% activity compared to cholesterol
Products: -
Products: -
?
beta-stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
P12676, Q55020
Substrates: 37% activity compared to cholesterol
Products: -
Products: -
?
beta-stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
-
Substrates: 50% activity compared to cholesterol
Products: -
Products: -
?
beta-stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
Streptoverticillium cholesterolieum
-
Substrates: 17% activity compared to cholesterol
Products: -
Products: -
?
beta-stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
-
Substrates: 32% activity compared to cholesterol
Products: -
Products: -
?
beta-stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
-
Substrates: 32% activity compared to cholesterol
Products: -
Products: -
?
campesterol + O2
(24R)-ergost-5-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
campesterol + O2
(24R)-ergost-5-en-3-one + H2O2
Nocardia erythropolis
-
Substrates: 67% of activity with cholesterol
Products: -
Products: -
?
campesterol + O2
(24R)-ergost-5-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholestenol + O2
5alpha-cholest-8-en-3-one + H2O2
-
Substrates: 43% activity compared to cholesterol
Products: -
Products: -
?
cholestenol + O2
5alpha-cholest-8-en-3-one + H2O2
-
Substrates: 43% activity compared to cholesterol
Products: -
Products: -
?
cholestenone + O2
?
Substrates: -
Products: -
Products: -
?
cholestenone + O2
?
Substrates: -
Products: -
Products: -
?
cholesterol + O2
6beta-hydroxycholest-4-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
6beta-hydroxycholest-4-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: overview: substrate specificity
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: specific for steroid substrates with an OH group in position 3, preference for steroids with at least a C2 chain at position C17
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: 100% activity
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: 100% activity
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: 100% activity
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: 100% activity
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Corynebacterium cholesterolicum
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Corynebacterium cholesterolicum
-
Substrates: 100% activity
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Nocardia erythropolis
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Nocardia erythropolis
-
Substrates: -
Products: the assumed intermediate 5-cholesten-3-one is rapidly isomerized by the enzyme to cholest-4-en-3-one
Products: the assumed intermediate 5-cholesten-3-one is rapidly isomerized by the enzyme to cholest-4-en-3-one
r
cholesterol + O2
cholest-4-en-3-one + H2O2
Nocardia erythropolis
-
Substrates: overview: substrate specificity
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Nocardia erythropolis
-
Substrates: relatively unreactive 17keto-DELTA5-3beta-hydroxysteroids are converted to satisfactory substrates by formation of isopentyloximes or benzyloximes
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Nocardia erythropolis
-
Substrates: size and shape of steroid 17beta-side-chain and oxygenation of nucleus
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Nocardia erythropolis
-
Substrates: enzyme specifically oxidizes 3beta-hydroxy groups in steroids
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Nocardia erythropolis
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Nocardia rhodochrous
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: 100% activity
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: 100% activity
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
ir
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: enzyme specifically oxidizes 3beta-hydroxy groups in steroids
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: 100% activity
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: 100% activity
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: highest activity
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: 100% activity
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: best substrate
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: highest activity
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: best substrate
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: 100% activity
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: 100% activity
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: specific for steroid substrates with an OH group in position 3, preference for steroids with at least a C2 chain at position C17
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: cholesterol oxidase is required for the biosynthesis of the antifungal polyene pimaricin
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: cholesterol oxidase is required for the biosynthesis of the antifungal polyene pimaricin, apparently acting as an antifungal sensor
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: via cholest-5-en-3-one
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: via cholest-5-en-3-one
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: overview: substrate specificity
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: 100% activity
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Streptoverticillium cholesterolieum
-
Substrates: 100% activity
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Streptoverticillum cholesterolicum
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: 100% activity
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: 100% activity
Products: -
Products: -
?
cholesterol + O2
cholest-5-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-5-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-5-en-3-one + H2O2
-
Substrates: first step in cholesterol degradation
Products: -
Products: -
?
cholesterol + O2
cholest-5-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-5-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-5-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-5-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-5-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-5-en-3-one + H2O2
Corynebacterium cholesterolicum
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-5-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-5-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-5-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-5-en-3-one + H2O2
Nocardia erythropolis
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-5-en-3-one + H2O2
Nocardia erythropolis
-
Substrates: first step in cholesterol degradation
Products: -
Products: -
?
cholesterol + O2
cholest-5-en-3-one + H2O2
Nocardia rhodochrous
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-5-en-3-one + H2O2
Nocardia rhodochrous
-
Substrates: first step in cholesterol degradation
Products: -
Products: -
?
cholesterol + O2
cholest-5-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-5-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-5-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-5-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-5-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-5-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-5-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-5-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-5-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-5-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-5-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-5-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-5-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-5-en-3-one + H2O2
Streptomyces aegyptia NEAE 102
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-5-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-5-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-5-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-5-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-5-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-5-en-3-one + H2O2
Streptomyces rimosus MTCC 10792
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-5-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-5-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-5-en-3-one + H2O2
-
Substrates: -
Products: subsequent isomerization to cholest-4-en-3-one
Products: subsequent isomerization to cholest-4-en-3-one
?
cholesterol + O2
cholest-5-en-3-one + H2O2
-
Substrates: assay with phenazine sulfate and dichlorophenylindophenol as electron acceptors
Products: -
Products: -
?
cholesterol + O2
cholest-5-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-5-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-5-en-3-one + H2O2
Substrates: a combination of molecular docking and molecular dynamics simulations is used to predict the binding interactions of CHL in the active site of ChOx. The hydrophobic triad residues (Y107A, F444 and Y446A) are observed to change conformation upon CHL binding in the wild-type form of the enzyme, leading to an optimal binding mode for catalytic efficiency
Products: -
Products: -
?
cholesterol + O2
cholest-5-en-3-one + H2O2
Substrates: the enzyme catalyzes the oxidation of the substrate via a hydride transfer mechanism and concomitant reduction of the FAD cofactor. The Glu361 residue acts as a catalytic base facilitating the hydride transfer from the substrate to the cofactor
Products: -
Products: -
?
cholesterol + O2
cholest-5-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-5-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-5-en-3-one + H2O2
-
Substrates: first step in cholesterol degradation
Products: -
Products: -
?
cholesterol-5alpha,6beta-epoxide + O2
?
-
Substrates: 9% of the activity with cholesterol, enzyme CO1
Products: -
Products: -
?
cholesterol-5alpha,6beta-epoxide + O2
?
-
Substrates: 10% of the activity with cholesterol, enzyme CO2
Products: -
Products: -
?
coprostane + O2
?
-
Substrates: 63% of the activity with cholesterol, enzyme CO1
Products: -
Products: -
?
coprostane + O2
?
-
Substrates: 67% of the activity with cholesterol, enzyme CO2
Products: -
Products: -
?
dehydro-epi-androsterone + O2
?
-
Substrates: about 5% of the activity with cholesterol, cholesterol oxidase II
Products: -
Products: -
?
dehydro-epi-androsterone + O2
?
-
Substrates: about 35% of the activity with cholesterol, cholesterol oxidase I
Products: -
Products: -
?
dehydroepiandrosterone + O2
androst-5-en-3,17-dione + H2O2
-
Substrates: 41.4% of the activity with cholesterol
Products: -
Products: -
?
dehydroepiandrosterone + O2
androst-5-en-3,17-dione + H2O2
Substrates: 41% activity compared to cholesterol
Products: -
Products: -
?
dehydroepiandrosterone + O2
androst-5-en-3,17-dione + H2O2
Substrates: 16% activity compared to cholesterol
Products: -
Products: -
?
dehydroepiandrosterone + O2
androst-5-en-3,17-dione + H2O2
Substrates: 27% activity compared to cholesterol
Products: -
Products: -
?
dehydroepiandrosterone + O2
androst-5-en-3,17-dione + H2O2
Corynebacterium cholesterolicum
-
Substrates: 5% activity compared to cholesterol
Products: -
Products: -
?
dehydroepiandrosterone + O2
androst-5-en-3,17-dione + H2O2
Nocardia erythropolis
-
Substrates: -
Products: -
Products: -
r
dehydroepiandrosterone + O2
androst-5-en-3,17-dione + H2O2
-
Substrates: -
Products: -
Products: -
?
dehydroepiandrosterone + O2
androst-5-en-3,17-dione + H2O2
-
Substrates: -
Products: -
Products: -
?
dehydroepiandrosterone + O2
androst-5-en-3,17-dione + H2O2
-
Substrates: 28% activity compared to cholesterol
Products: -
Products: -
?
dehydroepiandrosterone + O2
androst-5-en-3,17-dione + H2O2
P12676, Q55020
Substrates: 24% activity compared to cholesterol
Products: -
Products: -
?
dehydroepiandrosterone + O2
androst-5-en-3,17-dione + H2O2
-
Substrates: -
Products: -
Products: -
?
dehydroepiandrosterone + O2
androst-5-en-3,17-dione + H2O2
-
Substrates: 37% activity compared to cholesterol
Products: -
Products: -
?
dehydroepiandrosterone + O2
androst-5-en-3,17-dione + H2O2
Substrates: -
Products: -
Products: -
?
dehydroepiandrosterone + O2
androst-5-en-3,17-dione + H2O2
Substrates: -
Products: -
Products: -
?
dehydroepiandrosterone + O2
androst-5-en-3,17-dione + H2O2
Streptoverticillium cholesterolieum
-
Substrates: 48% activity compared to cholesterol
Products: -
Products: -
?
dehydroisoandrosterone + O2
androst-5-en-3,17-dione + H2O
-
Substrates: low activity with wild-type and mutant enzymes L119A, L119F, V145Q, P357N, Q286R and S379T
Products: -
Products: -
?
dehydroisoandrosterone + O2
androst-5-en-3,17-dione + H2O
Substrates: -
Products: -
Products: -
?
desmosterol + O2
cholesta-5,24-dien-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
desmosterol + O2
cholesta-5,24-dien-3-one + H2O2
Nocardia erythropolis
-
Substrates: 98% of activity with cholesteol
Products: -
Products: -
?
desmosterol + O2
cholesta-5,24-dien-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
dihydrocholesterol + O2
5alpha-cholestan-3-one + H2O2
-
Substrates: 58% of the activity with cholesterol, enzyme CO1
Products: -
Products: -
?
dihydrocholesterol + O2
5alpha-cholestan-3-one + H2O2
-
Substrates: 70% of the activity with cholesterol, enzyme CO2
Products: -
Products: -
?
dihydrocholesterol + O2
5alpha-cholestan-3-one + H2O2
-
Substrates: 22% of the activity with cholesterol
Products: -
Products: -
?
dihydrocholesterol + O2
5alpha-cholestan-3-one + H2O2
-
Substrates: 79% of the activity with cholesterol
Products: -
Products: -
?
dihydrocholesterol + O2
5alpha-cholestan-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
dihydrocholesterol + O2
5alpha-cholestan-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
diosgenin + O2
diosgenone + H2O2
Substrates: i.e. (25R)-spirost-5-en-3beta-ol
Products: -
Products: -
?
diosgenin + O2
diosgenone + H2O2
Substrates: i.e. (25R)-spirost-5-en-3beta-ol
Products: -
Products: -
?
epiandrosterone + O2
?
Substrates: 10% activity compared to cholesterol
Products: -
Products: -
?
epiandrosterone + O2
?
Substrates: 15% activity compared to cholesterol
Products: -
Products: -
?
epiandrosterone + O2
?
-
Substrates: 15% of the activity with cholesterol
Products: -
Products: -
?
epiandrosterone + O2
?
-
Substrates: 1% activity compared to cholesterol
Products: -
Products: -
?
ergosterol + O2
?
-
Substrates: 12% of the activity with cholesterol
Products: -
Products: -
?
ergosterol + O2
?
-
Substrates: 22% of the activity with cholesterol
Products: -
Products: -
?
ergosterol + O2
?
-
Substrates: -
Products: -
Products: -
?
ergosterol + O2
? + H2O2
-
Substrates: 22% activity compared to cholesterol
Products: -
Products: -
?
ergosterol + O2
? + H2O2
-
Substrates: 12% activity compared to cholesterol
Products: -
Products: -
?
ergosterol + O2
dehydroergosterol + H2O2
-
Substrates: -
Products: -
Products: -
?
ergosterol + O2
dehydroergosterol + H2O2
Substrates: 20% activity compared to cholesterol
Products: -
Products: -
?
ergosterol + O2
dehydroergosterol + H2O2
Substrates: 20% activity compared to cholesterol
Products: -
Products: -
?
ergosterol + O2
dehydroergosterol + H2O2
Substrates: 12% activity compared to cholesterol
Products: -
Products: -
?
ergosterol + O2
dehydroergosterol + H2O2
Corynebacterium cholesterolicum
-
Substrates: 4% activity compared to cholesterol
Products: -
Products: -
?
ergosterol + O2
dehydroergosterol + H2O2
-
Substrates: low activity
Products: -
Products: -
?
ergosterol + O2
dehydroergosterol + H2O2
-
Substrates: 17% activity compared to cholesterol
Products: -
Products: -
?
ergosterol + O2
dehydroergosterol + H2O2
-
Substrates: 51% activity compared to cholesterol
Products: -
Products: -
?
ergosterol + O2
dehydroergosterol + H2O2
-
Substrates: 51% activity compared to cholesterol
Products: -
Products: -
?
ergosterol + O2
dehydroergosterol + H2O2
P12676, Q55020
Substrates: 12% activity compared to cholesterol
Products: -
Products: -
?
ergosterol + O2
dehydroergosterol + H2O2
-
Substrates: -
Products: -
Products: -
?
ergosterol + O2
dehydroergosterol + H2O2
-
Substrates: 14% activity compared to cholesterol
Products: -
Products: -
?
ergosterol + O2
dehydroergosterol + H2O2
Streptoverticillium cholesterolieum
-
Substrates: 5% activity compared to cholesterol
Products: -
Products: -
?
fucosterol + O2
stigmasta-5,24(28)-dien-3-one + H2O2
Nocardia erythropolis
-
Substrates: -
Products: -
Products: -
?
fucosterol + O2
stigmasta-5,24(28)-dien-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
hecogenin + O2
5alpha-(25R)-spirostan-3,12-dione + H2O2
-
Substrates: 66% of the activity with cholesterol, enzyme CO1
Products: -
Products: -
?
hecogenin + O2
5alpha-(25R)-spirostan-3,12-dione + H2O2
-
Substrates: 80% of the activity with cholesterol, enzyme CO2
Products: -
Products: -
?
lanosterol + O2
5alpha-lanosta-8,24-dien-3-one + H2O2
-
Substrates: 4% of the activity with cholesterol, enzyme CO1
Products: -
Products: -
?
lanosterol + O2
5alpha-lanosta-8,24-dien-3-one + H2O2
-
Substrates: 5% of the activity with cholesterol, enzyme CO2
Products: -
Products: -
?
pregnenolone + O2
5-pregnen-3,20-dione + H2O2
-
Substrates: 22.4% of activity with chelesterol
Products: -
Products: -
?
pregnenolone + O2
5-pregnen-3,20-dione + H2O2
Substrates: 22% activity compared to cholesterol
Products: -
Products: -
?
pregnenolone + O2
5-pregnen-3,20-dione + H2O2
Substrates: 32% activity compared to cholesterol
Products: -
Products: -
?
pregnenolone + O2
5-pregnen-3,20-dione + H2O2
Substrates: 95% activity compared to cholesterol
Products: -
Products: -
?
pregnenolone + O2
5-pregnen-3,20-dione + H2O2
Corynebacterium cholesterolicum
-
Substrates: 38% activity compared to cholesterol
Products: -
Products: -
?
pregnenolone + O2
5-pregnen-3,20-dione + H2O2
Nocardia erythropolis
-
Substrates: -
Products: -
Products: -
r
pregnenolone + O2
5-pregnen-3,20-dione + H2O2
-
Substrates: 6% activity compared to cholesterol
Products: -
Products: -
?
pregnenolone + O2
5-pregnen-3,20-dione + H2O2
-
Substrates: -
Products: -
Products: -
?
pregnenolone + O2
5-pregnen-3,20-dione + H2O2
-
Substrates: -
Products: -
Products: -
?
pregnenolone + O2
5-pregnen-3,20-dione + H2O2
-
Substrates: 20% activity compared to cholesterol
Products: -
Products: -
?
pregnenolone + O2
5-pregnen-3,20-dione + H2O2
P12676, Q55020
Substrates: 99% activity compared to cholesterol
Products: -
Products: -
?
pregnenolone + O2
5-pregnen-3,20-dione + H2O2
-
Substrates: -
Products: -
Products: -
?
pregnenolone + O2
5-pregnen-3,20-dione + H2O2
-
Substrates: 42% activity compared to cholesterol
Products: -
Products: -
?
pregnenolone + O2
5-pregnen-3,20-dione + H2O2
Streptoverticillium cholesterolieum
-
Substrates: 37% activity compared to cholesterol
Products: -
Products: -
?
pregnenolone + O2
?
-
Substrates: about 60% of the activity with cholesterol, cholesterol oxidase II
Products: -
Products: -
?
pregnenolone + O2
?
-
Substrates: about 60% of the activity with cholesterol, cholesterol oxidase I
Products: -
Products: -
?
pregnenolone + O2
?
-
Substrates: 95% of the activity with cholesterol
Products: -
Products: -
?
pregnenolone + O2
? + H2O2
Substrates: -
Products: -
Products: -
?
pregnenolone + O2
? + H2O2
-
Substrates: 46% activity compared to cholesterol
Products: -
Products: -
?
pregnenolone + O2
? + H2O2
Streptomyces rimosus MTCC 10792
-
Substrates: 46% activity compared to cholesterol
Products: -
Products: -
?
pregnenolone + O2
pregn-5-ene-3,20-dione + H2O2
Substrates: low activity
Products: -
Products: -
?
pregnenolone + O2
pregn-5-ene-3,20-dione + H2O2
Substrates: low activity
Products: -
Products: -
?
sitost-5-en-3beta-ol + O2
sitost-5-en-3-one + H2O2
-
Substrates: 88% of the activity with cholesterol
Products: -
Products: -
?
sitost-5-en-3beta-ol + O2
sitost-5-en-3-one + H2O2
-
Substrates: 88% of the activity with cholesterol
Products: -
Products: -
?
stigmast-5-en-3beta-ol + O2
stigmast-5-en-3-one + H2O2
-
Substrates: 68% of the activity with cholesterol
Products: -
Products: -
?
stigmast-5-en-3beta-ol + O2
stigmast-5-en-3-one + H2O2
-
Substrates: 68% of the activity with cholesterol
Products: -
Products: -
?
stigmastanol + O2
stigmastanone + H2O2
-
Substrates: 7% of the activity with cholesterol
Products: -
Products: -
?
stigmastanol + O2
stigmastanone + H2O2
-
Substrates: 15% of the activity with cholesterol
Products: -
Products: -
?
stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
-
Substrates: 86% of the activity with cholesterol, enzyme CO1
Products: -
Products: -
?
stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
-
Substrates: 102% of the activity with cholesterol, enzyme CO2
Products: -
Products: -
?
stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
-
Substrates: 86% of the activity with cholesterol, enzyme CO1
Products: -
Products: -
?
stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
-
Substrates: 10% of activity with cholesterol
Products: -
Products: -
?
stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
-
Substrates: about 10% of the activity with cholesterol, cholesterol oxidase II
Products: -
Products: -
?
stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
-
Substrates: about 10% of the activity with cholesterol, cholesterol oxidase I
Products: -
Products: -
?
stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
-
Substrates: 15% of the activity with cholesterol
Products: -
Products: -
?
stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
-
Substrates: 32% of the activity with cholesterol
Products: -
Products: -
?
stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
Nocardia erythropolis
-
Substrates: -
Products: -
Products: -
?
stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
taurocholate + O2
? + H2O2
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: optimization of assay conditions, concerning buffer type and molarity, temperature, pH, deergent addition, ionogenic state etc.
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with ergosterol
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with epicholesterol
Products: -
Products: -
?
additional information
?
-
Substrates: cholesterol oxidase is a bifunctional enzyme that catalyzes the oxidation and isomerization of cholesterol to cholest-4-en-3-one while dioxygen is finally reduced to H2O2 as by-product. The enzymatic overall cholesterol oxidation comprises three steps. In the first one the 3beta-OH group of cholesterol is oxidized to the corresponding ketone with the concomitant reduction of the FAD cofactor. In a second step an isomerization of the double bond from the DELTA5-6 position to the DELTA4-5 position takes place. The FAD is recycled in a redox reaction with dioxygen, yielding hydrogen peroxide
Products: -
Products: -
?
additional information
?
-
-
Substrates: cholesterol oxidase is a bifunctional enzyme that catalyzes the oxidation and isomerization of cholesterol to cholest-4-en-3-one while dioxygen is finally reduced to H2O2 as by-product. The enzymatic overall cholesterol oxidation comprises three steps. In the first one the 3beta-OH group of cholesterol is oxidized to the corresponding ketone with the concomitant reduction of the FAD cofactor. In a second step an isomerization of the double bond from the DELTA5-6 position to the DELTA4-5 position takes place. The FAD is recycled in a redox reaction with dioxygen, yielding hydrogen peroxide
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme also acts as a DELTA5-ketosteroid isomerase, EC 5.3.3.1, converting a 3-oxo-DELTA5-steroid to a 3-oxo-DELTA4-steroid
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme also acts as a DELTA5-ketosteroid isomerase, EC 5.3.3.1, converting a 3-oxo-DELTA5-steroid to a 3-oxo-DELTA4-steroid
Products: -
Products: -
?
additional information
?
-
Substrates: cholesterol oxidase is a bifunctional enzyme that catalyzes the oxidation and isomerization of cholesterol to cholest-4-en-3-one while dioxygen is finally reduced to H2O2 as by-product. The enzymatic overall cholesterol oxidation comprises three steps. In the first one the 3beta-OH group of cholesterol is oxidized to the corresponding ketone with the concomitant reduction of the FAD cofactor. In a second step an isomerization of the double bond from the DELTA5-6 position to the DELTA4-5 position takes place. The FAD is recycled in a redox reaction with dioxygen, yielding hydrogen peroxide
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme also acts as a DELTA5-ketosteroid isomerase, EC 5.3.3.1, converting a 3-oxo-DELTA5-steroid to a 3-oxo-DELTA4-steroid
Products: -
Products: -
?
additional information
?
-
-
Substrates: less than 3% of the activity with cholesterol: ergosterol and epiandrosterone. No activity: dehydroepiandrosterone, pregnenolone
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with: ergosterol, dehydroepiandrosterone, epiandrosterone, pregnenolone
Products: -
Products: -
?
additional information
?
-
-
Substrates: intact ChoD is important for the growth of Mycobacterium tuberculosis in peritoneal macrophages and lungs of mice. Cholesterol oxidase is required for virulence of Mycobacterium tuberculosis
Products: -
Products: -
?
additional information
?
-
Substrates: the bifunctional FAD-dependent enzyme catalyzes the oxidation and isomerization of sterols to sterones, typically cholesterol (5-cholesten-3-beta-ol) to 4-cholesten-3-one (cholestenone) and H2O2. The enzyme shows higher activity towards the 3beta-hydroxy steroids with long alkyl chains at C17
Products: -
Products: -
?
additional information
?
-
Substrates: the bifunctional FAD-dependent enzyme catalyzes the oxidation and isomerization of sterols to sterones, typically cholesterol (5-cholesten-3-beta-ol) to 4-cholesten-3-one (cholestenone) and H2O2. The enzyme shows higher activity towards the 3beta-hydroxy steroids with long alkyl chains at C17
Products: -
Products: -
?
additional information
?
-
Substrates: the bifunctional FAD-dependent enzyme catalyzes the oxidation and isomerization of sterols to sterones, typically cholesterol (5-cholesten-3-beta-ol) to 4-cholesten-3-one (cholestenone) and H2O2. The enzyme shows higher activity towards the 3beta-hydroxy steroids with long alkyl chains at C17
Products: -
Products: -
?
additional information
?
-
Substrates: the bifunctional FAD-dependent enzyme catalyzes the oxidation and isomerization of sterols to sterones, typically cholesterol (5-cholesten-3-beta-ol) to 4-cholesten-3-one (cholestenone) and H2O2. The enzyme shows higher activity towards the 3beta-hydroxy steroids with long alkyl chains at C17
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme oxidizes 3beta-hydroxysteroids such as cholesterol, beta-cholestanol, and beta-sitosterol at high rates. No activity with 5alpha-androstan-3beta-ol-17-one, and 3beta-hydroxyandrost-5-en-17-one
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme oxidizes 3beta-hydroxysteroids such as cholesterol, beta-cholestanol, and beta-sitosterol at high rates. No activity with 5alpha-androstan-3beta-ol-17-one, and 3beta-hydroxyandrost-5-en-17-one
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with dehydroepiandrosterone
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with dehydroepiandrosterone
Products: -
Products: -
?
additional information
?
-
Substrates: the oxidation of the allylic alcohols by cholesterol oxidase from Rhodococcus erythropolis is stereo- and enantioselective. The enzyme oxidizes (S)-alcohol at a higher rate than (R)-alcohol
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme does not use glycerol as substrate
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with cholic acid, progesterone and 4-androsten-3,17-dione
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme shows substrate specificity for 3beta-hydroxysteroids. No activity with cholic acid and cholesteryl linoleate
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme does not use glycerol as substrate
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with cholic acid, progesterone and 4-androsten-3,17-dione
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with ergosterol
Products: -
Products: -
?
additional information
?
-
-
Substrates: cholesterol oxidase is involved in pimaricin biosynthesis
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with cholest-5-en-3alpha-ol
Products: -
Products: -
?
additional information
?
-
-
Substrates: the wild-type enzyme also shows cholesterol dehydrogenase activity with 0.001 U/mg
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme catalyzes the oxidation of steroid substrates which have a hydroxyl group at the 3beta-position of the steroid ring system
Products: -
Products: -
?
additional information
?
-
-
Substrates: cholesterol oxidase is a bifunctional FAD-containing oxidoreductase which catalyzes the oxidation and isomerization of cholesterol into 4-cholesten-3-one
Products: -
Products: -
?
additional information
?
-
Substrates: cholesterol oxidase is a bifunctional flavoenzyme that catalyzes the oxidation and isomerization of cholesterol to cholest-4-en-3-one
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme catalyzes the oxidation and isomerization of steroids containing a 3-hydroxyl group, with the cholestane group conferring binding specificity in the active site. The enzyme is also able to oxidize small-molecule alcohols such as 2-propanol and methanol, with a preference for those containing aromatic ring, but with lower activity. Substrate oxidation results in reduction of the cofactor during the reductive half reaction. An oxidative half reaction occurs with re-oxidation of the flavin cofactor by molecular oxygen to form hydrogen peroxide. Structure-function relationship and analysis overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with ergosterol, pregnenolone, dehydroepiandrosterone, and epiandosterone
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with ergosterol, pregnenolone, dehydroepiandrosterone, and epiandosterone
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3beta-chlorocholest-5-ene + O2
? + H2O2
Substrates: low activity
Products: -
Products: -
?
androst-4-ene-3,17-dione + O2
? + H2O2
Substrates: -
Products: -
Products: -
?
beta-sitosterol + O2
? + H2O2
Substrates: -
Products: -
Products: -
?
cholest-4-en-3-one + O2
? + H2O2
Substrates: -
Products: -
Products: -
?
dehydroandrosterone + O2
? + H2O2
Substrates: -
Products: -
Products: -
?
pregnenolone + O2
? + H2O2
Substrates: -
Products: -
Products: -
?
beta-cholestanol + O2
?
Substrates: 13% activity compared to cholesterol
Products: -
Products: -
?
beta-cholestanol + O2
?
Substrates: 69% activity compared to cholesterol
Products: -
Products: -
?
beta-cholestanol + O2
?
Substrates: 69% activity compared to cholesterol
Products: -
Products: -
?
beta-cholestanol + O2
?
Substrates: 95% activity compared to cholesterol
Products: -
Products: -
?
beta-cholestanol + O2
?
-
Substrates: 78% activity compared to cholesterol
Products: -
Products: -
?
beta-cholestanol + O2
?
-
Substrates: 78% activity compared to cholesterol
Products: -
Products: -
?
beta-cholestanol + O2
?
P12676, Q55020
Substrates: 75% activity compared to cholesterol
Products: -
Products: -
?
beta-cholestanol + O2
?
-
Substrates: 101% activity compared to cholesterol
Products: -
Products: -
?
beta-cholestanol + O2
?
Streptoverticillium cholesterolieum
-
Substrates: 96% activity compared to cholesterol
Products: -
Products: -
?
beta-cholestanol + O2
?
-
Substrates: 79% activity compared to cholesterol
Products: -
Products: -
?
beta-cholestanol + O2
?
-
Substrates: 79% activity compared to cholesterol
Products: -
Products: -
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
Substrates: 20% activity compared to cholesterol
Products: -
Products: -
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
Substrates: 84% activity compared to cholesterol
Products: -
Products: -
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
Substrates: 84% activity compared to cholesterol
Products: -
Products: -
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
Substrates: 80% activity compared to cholesterol
Products: -
Products: -
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
Corynebacterium cholesterolicum
-
Substrates: 50% activity compared to cholesterol
Products: -
Products: -
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
P12676, Q55020
Substrates: 72% activity compared to cholesterol
Products: -
Products: -
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
-
Substrates: 64% activity compared to cholesterol
Products: -
Products: -
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
Streptoverticillium cholesterolieum
-
Substrates: 39% activity compared to cholesterol
Products: -
Products: -
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
-
Substrates: 29% activity compared to cholesterol
Products: -
Products: -
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
-
Substrates: 29% activity compared to cholesterol
Products: -
Products: -
?
beta-stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
Substrates: 10% activity compared to cholesterol
Products: -
Products: -
?
beta-stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
Substrates: 59% activity compared to cholesterol
Products: -
Products: -
?
beta-stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
Substrates: 59% activity compared to cholesterol
Products: -
Products: -
?
beta-stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
Substrates: 36% activity compared to cholesterol
Products: -
Products: -
?
beta-stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
Corynebacterium cholesterolicum
-
Substrates: 12% activity compared to cholesterol
Products: -
Products: -
?
beta-stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
-
Substrates: 47% activity compared to cholesterol
Products: -
Products: -
?
beta-stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
-
Substrates: 40% activity compared to cholesterol
Products: -
Products: -
?
beta-stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
-
Substrates: 40% activity compared to cholesterol
Products: -
Products: -
?
beta-stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
P12676, Q55020
Substrates: 37% activity compared to cholesterol
Products: -
Products: -
?
beta-stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
-
Substrates: 50% activity compared to cholesterol
Products: -
Products: -
?
beta-stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
Streptoverticillium cholesterolieum
-
Substrates: 17% activity compared to cholesterol
Products: -
Products: -
?
beta-stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
-
Substrates: 32% activity compared to cholesterol
Products: -
Products: -
?
beta-stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
-
Substrates: 32% activity compared to cholesterol
Products: -
Products: -
?
cholesterol + O2
6beta-hydroxycholest-4-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
6beta-hydroxycholest-4-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: 100% activity
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: 100% activity
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: 100% activity
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: 100% activity
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Corynebacterium cholesterolicum
-
Substrates: 100% activity
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Nocardia rhodochrous
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: 100% activity
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: 100% activity
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: 100% activity
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: 100% activity
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: 100% activity
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: cholesterol oxidase is required for the biosynthesis of the antifungal polyene pimaricin
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: cholesterol oxidase is required for the biosynthesis of the antifungal polyene pimaricin, apparently acting as an antifungal sensor
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: via cholest-5-en-3-one
Products: -
Products: -
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: -
Products: -
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cholesterol + O2
cholest-4-en-3-one + H2O2
Substrates: via cholest-5-en-3-one
Products: -
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cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: 100% activity
Products: -
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?
cholesterol + O2
cholest-4-en-3-one + H2O2
Streptoverticillium cholesterolieum
-
Substrates: 100% activity
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cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: 100% activity
Products: -
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?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
Substrates: 100% activity
Products: -
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?
cholesterol + O2
cholest-5-en-3-one + H2O2
-
Substrates: -
Products: -
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?
cholesterol + O2
cholest-5-en-3-one + H2O2
-
Substrates: first step in cholesterol degradation
Products: -
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?
cholesterol + O2
cholest-5-en-3-one + H2O2
-
Substrates: -
Products: -
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?
cholesterol + O2
cholest-5-en-3-one + H2O2
-
Substrates: -
Products: -
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?
cholesterol + O2
cholest-5-en-3-one + H2O2
-
Substrates: -
Products: -
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?
cholesterol + O2
cholest-5-en-3-one + H2O2
Corynebacterium cholesterolicum
-
Substrates: -
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cholesterol + O2
cholest-5-en-3-one + H2O2
-
Substrates: -
Products: -
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?
cholesterol + O2
cholest-5-en-3-one + H2O2
Substrates: -
Products: -
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?
cholesterol + O2
cholest-5-en-3-one + H2O2
Nocardia erythropolis
-
Substrates: -
Products: -
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cholesterol + O2
cholest-5-en-3-one + H2O2
Nocardia erythropolis
-
Substrates: first step in cholesterol degradation
Products: -
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?
cholesterol + O2
cholest-5-en-3-one + H2O2
Nocardia rhodochrous
-
Substrates: -
Products: -
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cholesterol + O2
cholest-5-en-3-one + H2O2
Nocardia rhodochrous
-
Substrates: first step in cholesterol degradation
Products: -
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?
cholesterol + O2
cholest-5-en-3-one + H2O2
-
Substrates: -
Products: -
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?
cholesterol + O2
cholest-5-en-3-one + H2O2
-
Substrates: -
Products: -
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?
cholesterol + O2
cholest-5-en-3-one + H2O2
-
Substrates: -
Products: -
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?
cholesterol + O2
cholest-5-en-3-one + H2O2
-
Substrates: -
Products: -
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?
cholesterol + O2
cholest-5-en-3-one + H2O2
-
Substrates: -
Products: -
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?
cholesterol + O2
cholest-5-en-3-one + H2O2
-
Substrates: -
Products: -
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?
cholesterol + O2
cholest-5-en-3-one + H2O2
-
Substrates: -
Products: -
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?
cholesterol + O2
cholest-5-en-3-one + H2O2
-
Substrates: -
Products: -
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?
cholesterol + O2
cholest-5-en-3-one + H2O2
-
Substrates: -
Products: -
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?
cholesterol + O2
cholest-5-en-3-one + H2O2
-
Substrates: -
Products: -
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?
cholesterol + O2
cholest-5-en-3-one + H2O2
-
Substrates: -
Products: -
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?
cholesterol + O2
cholest-5-en-3-one + H2O2
-
Substrates: -
Products: -
Products: -
?
cholesterol + O2
cholest-5-en-3-one + H2O2
Substrates: -
Products: -
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?
cholesterol + O2
cholest-5-en-3-one + H2O2
-
Substrates: -
Products: -
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?
cholesterol + O2
cholest-5-en-3-one + H2O2
-
Substrates: -
Products: -
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cholesterol + O2
cholest-5-en-3-one + H2O2
Substrates: -
Products: -
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?
cholesterol + O2
cholest-5-en-3-one + H2O2
-
Substrates: -
Products: -
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cholesterol + O2
cholest-5-en-3-one + H2O2
-
Substrates: first step in cholesterol degradation
Products: -
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?
dehydroepiandrosterone + O2
androst-5-en-3,17-dione + H2O2
Substrates: 41% activity compared to cholesterol
Products: -
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?
dehydroepiandrosterone + O2
androst-5-en-3,17-dione + H2O2
Substrates: 16% activity compared to cholesterol
Products: -
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?
dehydroepiandrosterone + O2
androst-5-en-3,17-dione + H2O2
Substrates: 27% activity compared to cholesterol
Products: -
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?
dehydroepiandrosterone + O2
androst-5-en-3,17-dione + H2O2
Corynebacterium cholesterolicum
-
Substrates: 5% activity compared to cholesterol
Products: -
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dehydroepiandrosterone + O2
androst-5-en-3,17-dione + H2O2
-
Substrates: 28% activity compared to cholesterol
Products: -
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?
dehydroepiandrosterone + O2
androst-5-en-3,17-dione + H2O2
P12676, Q55020
Substrates: 24% activity compared to cholesterol
Products: -
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?
dehydroepiandrosterone + O2
androst-5-en-3,17-dione + H2O2
-
Substrates: 37% activity compared to cholesterol
Products: -
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?
dehydroepiandrosterone + O2
androst-5-en-3,17-dione + H2O2
Streptoverticillium cholesterolieum
-
Substrates: 48% activity compared to cholesterol
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?
epiandrosterone + O2
?
Substrates: 10% activity compared to cholesterol
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?
epiandrosterone + O2
?
Substrates: 15% activity compared to cholesterol
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?
epiandrosterone + O2
?
-
Substrates: 1% activity compared to cholesterol
Products: -
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?
ergosterol + O2
dehydroergosterol + H2O2
Substrates: 20% activity compared to cholesterol
Products: -
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?
ergosterol + O2
dehydroergosterol + H2O2
Substrates: 20% activity compared to cholesterol
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?
ergosterol + O2
dehydroergosterol + H2O2
Substrates: 12% activity compared to cholesterol
Products: -
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?
ergosterol + O2
dehydroergosterol + H2O2
Corynebacterium cholesterolicum
-
Substrates: 4% activity compared to cholesterol
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?
ergosterol + O2
dehydroergosterol + H2O2
-
Substrates: 17% activity compared to cholesterol
Products: -
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?
ergosterol + O2
dehydroergosterol + H2O2
-
Substrates: 51% activity compared to cholesterol
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?
ergosterol + O2
dehydroergosterol + H2O2
-
Substrates: 51% activity compared to cholesterol
Products: -
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?
ergosterol + O2
dehydroergosterol + H2O2
P12676, Q55020
Substrates: 12% activity compared to cholesterol
Products: -
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?
ergosterol + O2
dehydroergosterol + H2O2
-
Substrates: 14% activity compared to cholesterol
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?
ergosterol + O2
dehydroergosterol + H2O2
Streptoverticillium cholesterolieum
-
Substrates: 5% activity compared to cholesterol
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pregnenolone + O2
5-pregnen-3,20-dione + H2O2
Substrates: 22% activity compared to cholesterol
Products: -
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?
pregnenolone + O2
5-pregnen-3,20-dione + H2O2
Substrates: 32% activity compared to cholesterol
Products: -
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?
pregnenolone + O2
5-pregnen-3,20-dione + H2O2
Substrates: 95% activity compared to cholesterol
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?
pregnenolone + O2
5-pregnen-3,20-dione + H2O2
Corynebacterium cholesterolicum
-
Substrates: 38% activity compared to cholesterol
Products: -
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?
pregnenolone + O2
5-pregnen-3,20-dione + H2O2
-
Substrates: 6% activity compared to cholesterol
Products: -
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?
pregnenolone + O2
5-pregnen-3,20-dione + H2O2
-
Substrates: 20% activity compared to cholesterol
Products: -
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?
pregnenolone + O2
5-pregnen-3,20-dione + H2O2
P12676, Q55020
Substrates: 99% activity compared to cholesterol
Products: -
Products: -
?
pregnenolone + O2
5-pregnen-3,20-dione + H2O2
-
Substrates: 42% activity compared to cholesterol
Products: -
Products: -
?
pregnenolone + O2
5-pregnen-3,20-dione + H2O2
Streptoverticillium cholesterolieum
-
Substrates: 37% activity compared to cholesterol
Products: -
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?
additional information
?
-
Substrates: no activity with ergosterol
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?
additional information
?
-
Substrates: cholesterol oxidase is a bifunctional enzyme that catalyzes the oxidation and isomerization of cholesterol to cholest-4-en-3-one while dioxygen is finally reduced to H2O2 as by-product. The enzymatic overall cholesterol oxidation comprises three steps. In the first one the 3beta-OH group of cholesterol is oxidized to the corresponding ketone with the concomitant reduction of the FAD cofactor. In a second step an isomerization of the double bond from the DELTA5-6 position to the DELTA4-5 position takes place. The FAD is recycled in a redox reaction with dioxygen, yielding hydrogen peroxide
Products: -
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?
additional information
?
-
-
Substrates: cholesterol oxidase is a bifunctional enzyme that catalyzes the oxidation and isomerization of cholesterol to cholest-4-en-3-one while dioxygen is finally reduced to H2O2 as by-product. The enzymatic overall cholesterol oxidation comprises three steps. In the first one the 3beta-OH group of cholesterol is oxidized to the corresponding ketone with the concomitant reduction of the FAD cofactor. In a second step an isomerization of the double bond from the DELTA5-6 position to the DELTA4-5 position takes place. The FAD is recycled in a redox reaction with dioxygen, yielding hydrogen peroxide
Products: -
Products: -
?
additional information
?
-
Substrates: cholesterol oxidase is a bifunctional enzyme that catalyzes the oxidation and isomerization of cholesterol to cholest-4-en-3-one while dioxygen is finally reduced to H2O2 as by-product. The enzymatic overall cholesterol oxidation comprises three steps. In the first one the 3beta-OH group of cholesterol is oxidized to the corresponding ketone with the concomitant reduction of the FAD cofactor. In a second step an isomerization of the double bond from the DELTA5-6 position to the DELTA4-5 position takes place. The FAD is recycled in a redox reaction with dioxygen, yielding hydrogen peroxide
Products: -
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additional information
?
-
-
Substrates: intact ChoD is important for the growth of Mycobacterium tuberculosis in peritoneal macrophages and lungs of mice. Cholesterol oxidase is required for virulence of Mycobacterium tuberculosis
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additional information
?
-
-
Substrates: no activity with dehydroepiandrosterone
Products: -
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?
additional information
?
-
-
Substrates: no activity with dehydroepiandrosterone
Products: -
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?
additional information
?
-
Substrates: the oxidation of the allylic alcohols by cholesterol oxidase from Rhodococcus erythropolis is stereo- and enantioselective. The enzyme oxidizes (S)-alcohol at a higher rate than (R)-alcohol
Products: -
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?
additional information
?
-
-
Substrates: no activity with ergosterol
Products: -
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?
additional information
?
-
-
Substrates: cholesterol oxidase is involved in pimaricin biosynthesis
Products: -
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?
additional information
?
-
-
Substrates: cholesterol oxidase is a bifunctional FAD-containing oxidoreductase which catalyzes the oxidation and isomerization of cholesterol into 4-cholesten-3-one
Products: -
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?
additional information
?
-
Substrates: cholesterol oxidase is a bifunctional flavoenzyme that catalyzes the oxidation and isomerization of cholesterol to cholest-4-en-3-one
Products: -
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additional information
?
-
-
Substrates: no activity with ergosterol, pregnenolone, dehydroepiandrosterone, and epiandosterone
Products: -
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?
additional information
?
-
-
Substrates: no activity with ergosterol, pregnenolone, dehydroepiandrosterone, and epiandosterone
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
combined quantum mechanical and molecular mechanical simulations of one- and two-electron reduction potentials of flavin cofactor
FAD
-
distortion of flavin geometry is linked to ligand binding in cholesterol oxidase
FAD
Streptoverticillum cholesterolicum
-
both as a covalently or noncovalently bound cofactor
FAD
-
the type II cholesterol oxidase fully active enzyme contains covalently bound FAD
FAD
isozyme ChoM1 contains a typical consensus sequence (GXGXXGXXXAXXXXXXG) in the FAD-binding site, which is located near the N-terminal end at amino acids 11-27
FAD
isozyme ChoM2 contains a typical consensus sequence (GXGXXGXXXAXXXXXXG) in the FAD-binding site, which is located near the N-terminal end at amino acids 45-61
FAD
dependent on, the enzyme contains a Rossmann fold (xh)2GxGxxGx(xxh)2(x) FAD binding site, where x is any amino acid and h an hydrophobic one, between V44 and E70 in the N-terminal region. CgChoA belongs to the non-covalent FAD-dependent enzymes belonging to the class I family. Residues N503 and Y464 are required for stabilization of the reduced form cofactor-enzyme binding
FAD
the structure of the dithionite-reduced enzyme reveals a sulfite molecule covalently bound to the FAD cofactor. The hydride transfer generates a tetrahedral geometry about the flavin N5 atom
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ag+
1 mM, 1 h 30°C, partially reduced the activity to 88%
Co2+
Cu2+
Mg2+
Mn2+
Zn2+
additional information
Cu2+
1 mM, 1 h 30°C, partially reduced the activity to 88%
Cu2+
1 mM, 1 h 30°C, partially reduced the activity to 62%
Mn2+
1 mM, 1 h 30°C, partially reduced the activity to 63%
Zn2+
1 mM, 1 h 30°C, partially reduced the activity to 73%
Zn2+
1 mM, 1 h 30°C, partially reduced the activity to 79%
additional information
Ag+ scarcely influences the activity of the enzyme
additional information
no or poor effects by Na+, K+, Ni2+, and Ca2+, and EDTA
additional information
no or poor effects by Na+, K+, Ni2+, and Ca2+, and EDTA
additional information
1 mM of Ca2+, Mg2+, Mn2+, Ni2+, Fe2+, and Zn2+ have no obvious effect on the enzyme activity.No effect by EDTA
additional information
-
1 mM of Ca2+, Mg2+, Mn2+, Ni2+, Fe2+, and Zn2+ have no obvious effect on the enzyme activity.No effect by EDTA
additional information
-
the enzyme activity is unaffected or poorly affected by Ca2+, Mg2+, Mn2+, and EDTA
additional information
-
no or poor effects at 5 mM by Ca2+, Zn2+, Mg2+, and Fe2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4-chloromercuribenzoate
-
85% inhibition at 0.1 mM
laurylbenzenesulfonate
0.5% (w/v), complete inactivation; 0.5% (w/v), complete inactivation
NaCl
-
80% residual activity with 20% NaCl (3.42 M) and 83% relative activity with 12% NaCl (2.05 M) concentration
p-chloromercuribenzoic acid
-
the addition of p-chloromercuribenzoic acid partially reduces the activity of the enzyme
propan-2-ol
-
at 10% propan-2-ol kcat reaches 65% of that at 1.25% propan-2-ol
2-pyridylhydroxymethane sulfate
-
1 mM, 30 min at 4°C, 34% inhibition
2-pyridylhydroxymethane sulfate
-
1 mM, 30 min at 4°C, 32% inhibition
acetone
-
85% inhibition at a ratio of 1:2 with enzyme solution
butanol
-
the enzyme is inactivated by the addition of 50% (v/v) after incubation for 24 h at 37°C
butanol
the enzyme is inactivated by the addition of 50% (v/v) of butanol after incubation for 24 h at 37°C
butanol
-
6% inhibition at a ratio of 1:2 with enzyme solution
Dimethylsulfoxide
-
the enzyme is inactivated by the addition of 50% (v/v) after incubation for 24 h at 37°C
Dimethylsulfoxide
the enzyme is inactivated by the addition of 50% (v/v) of dimethylsulfoxide after incubation for 24 h at 37°C
DMSO
-
11% inhibition at a ratio of 1:2 with enzyme solution
ethyl acetate
-
the enzyme is inactivated by the addition of 50% (v/v) after incubation for 24 h at 37°C
ethyl acetate
the enzyme is inactivated by the addition of 50% (v/v) of ethyl acetate after incubation for 24 h at 37°C
fenpropimorph
-
irreversible inhibition; morpholine derivative, 50 mg/l, 50% inhibition, instantenous inhibition
fenpropimorph
Nocardia erythropolis
-
morpholine derivative, 50 mg/l, 50% inhibition, instantenous inhibition; reversible non-competitive
fenpropimorph
-
morpholine derivative, 50 mg/l, 50% inhibition, instantenous inhibition; reversible non-competitive
fenpropimorph
-
morpholine derivative, 50 mg/l, 50% inhibition, instantenous inhibition; reversible competitive mechanism
p-chloromercuribenzoate
-
1 mM, 20% inhibition, 0.1 mM, 14% inhibition
SDS
0.5% (w/v), complete inactivation; 0.5% (w/v), complete inactivation
Triton X-100
-
strong decrease in enzyme activity at concentration of 0.2% Triton X-100 or higher
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
-
additional information
-
not inhibited by 1% Triton X-100, 1% Tween 20, 1% sodium cholate and 1% CHAPS
-
additional information
-
not inhibited by 10 mM cyanide or 50 mM arsenite
-
additional information
Nocardia erythropolis
-
not inhibited by 1% Triton X-100, 1% Tween 20, 1% sodium cholate and 1% CHAPS
-
additional information
-
not inhibited by 1% Triton X-100, 1% Tween 20, 1% sodium cholate and 1% CHAPS
-
additional information
-
the enzyme activity is unaffected or poorly affected by Tween-20, Triton X-100, sodium cholate, methanol, toluene, and ethyl acetate
-
additional information
-
not inhibited by p-chloromercuribenzoate; overview: inhibition by steroids
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
acetone
-
3.8fold increase in activity, 1 ml solvent added to 2 ml 50 mM phosphate buffer
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
diphenylmethane
-
strain ST-200, 3.1fold increase in activity, 1 ml solvent added to 2 ml 50 mM phosphate buffer, pH 7.0
Long-chain alcohols
-
maximum activation with decanol and undecanol, shorter and longer alcohols are less effective
p-xylene
-
strain ST-200, 3.4fold increase in activity, 1 ml solvent added to 2 ml 50 mM phosphate buffer, pH 7.0
propylbenzene
-
strain ST-200, 3.2fold increase in activity, 1 ml solvent added to 2 ml 50 mM phosphate buffer, pH 7.0
additional information
-
the bacterial COX exhibits 22 % higher activity in potassium phosphate buffer, pH 7.5, in the presence of a nonionic detergent Triton X-100 at 0.05 % v/v
-
Benzene
-
strain ST-200, 3fold increase in activity, 1 ml solvent added to 2 ml 50 mM phosphate buffer, pH 7.0
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
-
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
-
Isopropanol
-
15% activation at 0.5% w/v
propan-2-ol
-
2fold increase in activity, 1 ml solvent added to 2 ml 50 mM phosphate buffer
propan-2-ol
-
maximal enzyme activity with 10%(v/v) in the presence of 500 mM potassium phosphate, decrease in activity in the presence of 50 mM potassium phosphate
Toluene
-
strain ST-200, 3.5fold increase in activity, 1 ml solvent added to 2 ml 50 mM phosphate buffer, pH 7.0
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Adenocarcinoma of Lung
Cholesterol oxidase from Bordetella species promotes irreversible cell apoptosis in lung adenocarcinoma by cholesterol oxidation.
Atherosclerosis
[Effect of cholesterol oxidase on lipid metabolism in experimental atherosclerosis]
Breast Neoplasms
Extracellular cholesterol oxidase production by Streptomyces aegyptia, in vitro anticancer activities against rhabdomyosarcoma, breast cancer cell-lines and in vivo apoptosis.
Cardiovascular Diseases
Alzheimer disease beta-amyloid activity mimics cholesterol oxidase.
Hypercholesterolemia
[Effect of Actinomyces lavendulae cholesterol oxidase on hypercholesteremia in guinea pigs]
Hypercholesterolemia
[Effect of cholesterol oxidase on the involution of experimental hypercholesterolemia in rabbits]
Hypercholesterolemia
[Effect of the cholesterol oxidase formed by Actinomyces lavendulae on hypercholesterolemia in rabbits]
Neoplasms
Cholesterol-rich fluid membranes solubilize ceramide domains: implications for the structure and dynamics of mammalian intracellular and plasma membranes.
Neoplasms
Cytotoxic activity of cholesterol oxidase produced by Streptomyces sp. AKHSS against cancerous cell lines: mechanism of action in HeLa cells.
Neoplasms
Electrospun CuO-ZnO nanohybrid: Tuning the nanostructure for improved amperometric detection of hydrogen peroxide as a non-enzymatic sensor.
Rhabdomyosarcoma
Extracellular cholesterol oxidase production by Streptomyces aegyptia, in vitro anticancer activities against rhabdomyosarcoma, breast cancer cell-lines and in vivo apoptosis.
Starvation
Growth-related modulation of human skin fibroblast cholesterol distribution and metabolism.
Tuberculosis
Cholesterol oxidase binds TLR2 and modulates functional responses of human macrophages.
Tuberculosis
Cholesterol Oxidase Is Indispensable in the Pathogenesis of Mycobacterium tuberculosis.
Tuberculosis
Determination of in vitro and in vivo immune response to recombinant cholesterol oxidase from Mycobacterium tuberculosis.
Tuberculosis
Initial step in the catabolism of cholesterol by Mycobacterium smegmatis mc(2) 155.
Tuberculosis
Mycobacterium tuberculosis Requires Cholesterol Oxidase to Disrupt TLR2 Signalling in Human Macrophages.
Vesicular Stomatitis
Effect of phospholipase C and cholesterol oxidase on membrane integrity, microviscosity, and infectivity of vesicular stomatitis virus.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.3
3beta-hydroxy-androst-5-en-17-one
-
assay relies on spectroscopic detection of 4-cholesten-3-one formation
0.5
3beta-hydroxy-androst-5-en-17-one
-
assay relies on detection of H2O2 formation
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
0.27
5-Cholesten-3-one
-
assay relies on spectroscopic detection of 4-cholesten-3-one formation
1.52
5-Cholesten-3-one
-
assay relies on spectroscopic detection of 4-cholesten-3-one formation
0.17842
beta-sitosterol
-
pH 7.5, temperature not specified in the publication, mutant enzyme F70V
0.18
beta-sitosterol
pH 7.5, 37°C, full-length isozyme ChoM2
0.19
beta-sitosterol
pH 7.5, 37°C, truncated isozyme ChoM2
0.22076
beta-sitosterol
-
pH 7.5, temperature not specified in the publication, mutant enzyme V64C
0.32861
beta-sitosterol
-
pH 7.5, temperature not specified in the publication, wild-type enzyme
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
0.7
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
0.0015
cholesterol
mutant enzyme G347N, determined by cholest-4-en-3-one detection
0.0027
cholesterol
wild-type enzyme, determined by cholest-4-en-3-one detection
0.0027
cholesterol
mutant enzyme F359W, determined by cholest-4-en-3-one detection
0.0027
cholesterol
apparent value, wild type enzyme, pH 7.0, temperature not specified in the publication
0.0046
cholesterol
apparent value, mutant enzyme N485L, pH 7.0, temperature not specified in the publication
0.0062
cholesterol
apparent value, mutant enzyme N485L, pH 5.1, temperature not specified in the publication
0.0063
cholesterol
apparent value, mutant enzyme N485D, pH 5.1, temperature not specified in the publication
0.0066
cholesterol
apparent value, mutant enzyme N485D, pH 7.0, temperature not specified in the publication
0.0067
cholesterol
apparent value, wild type enzyme, pH 5.1, temperature not specified in the publication
0.007
cholesterol
mutant enzyme N485D, determined by cholest-4-en-3-one detection
0.01
cholesterol
pH 7.0, 37°C, mutant enzyme S153C/A205C/S312C/T435C, cholesterol solubilized in detergent micelles as a substrate
0.011
cholesterol
pH 7.0, 37°C, mutant enzyme L80C, cholesterol solubilized in detergent micelles as a substrate
0.011
cholesterol
pH 7.0, 37°C, mutant enzyme A32C/S129C/T371C/A423C, cholesterol solubilized in detergent micelles as a substrate
0.011
cholesterol
pH 7.0, 37°C, mutant enzyme A184C/A301C/T394C, cholesterol solubilized in detergent micelles as a substrate
0.012
cholesterol
pH 7.0, 37°C, mutant enzyme A32C/T168C/S312C/A465C, cholesterol solubilized in detergent micelles as a substrate
0.013
cholesterol
Nocardia erythropolis
-
Km increases when enzyme is entrapped in reverse micelles of the synthetic surfactant aerosol-OT-isooctane
0.013
cholesterol
pH 7.0, 37°C, wild-type enzyme, cholesterol solubilized in detergent micelles as a substrate
0.013
cholesterol
pH 7.0, 37°C, mutant enzyme A184C/T239C/A407C/A465C, cholesterol solubilized in detergent micelles as a substrate
0.014
cholesterol
pH 7.0, 37°C, mutant enzyme T168C/A276C, cholesterol solubilized in detergent micelles as a substrate
0.017
cholesterol
pH 7.0, 37°C, mutant enzyme L274C, cholesterol solubilized in detergent micelles as a substrate
0.0188
cholesterol
pH and temperature not specified in the publication
0.0262
cholesterol
pH and temperature not specified in the publication
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
0.0962
cholesterol
-
enzyme from cultured immobilized cells, pH and temperature not specified in the publication
0.1013
cholesterol
-
enzyme from cultured free cells, pH and temperature not specified in the publication
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
0.12
cholesterol
pH 7.5, 37°C, full-length isozyme ChoM2
0.13
cholesterol
pH 7.5, 40°C, recombinant isozyme ChoM1
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
0.14
cholesterol
pH 7.5, 37°C, truncated isozyme ChoM2
0.15483
cholesterol
-
pH 7.5, temperature not specified in the publication, mutant enzyme F70V
0.16
cholesterol
pH 7.5, 40°C, recombinant isozyme ChoM1
0.17
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
0.17831
cholesterol
-
pH 7.5, temperature not specified in the publication, mutant enzyme V64C
0.2
cholesterol
-
assay relies on spectroscopic detection of 4-cholesten-3-one formation
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
0.2
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
0.20485
cholesterol
-
pH 7.5, temperature not specified in the publication, wild-type enzyme
0.2123
cholesterol
-
apparent value, free enzyme, in 50 mM potassium phosphate buffer, pH 7.5, 30°C
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
0.25
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
0.2599
cholesterol
-
apparent value, silk mat-immobilized enzyme, in 50 mM potassium phosphate buffer, pH 7.5, 30°C
0.4
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
0.47
cholesterol
-
H69A mutant enzyme, 50 mM phosphate buffer, pH 7.5, 1% thesit, 1% 2-propanol
0.8
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
35.4
cholesterol
-
N-terminally His-tagged recombinant enzyme , pH 7.2, 37°C
45.2
cholesterol
-
C-terminally His-tagged recombinant enzyme , pH 7.2, 37°C
0.2
dehydroandrosterone
pH 7.5, 37°C, full-length isozyme ChoM2
0.25
dehydroandrosterone
pH 7.5, 37°C, truncated isozyme ChoM2
0.27352
dehydroepiandrosterone
-
pH 7.5, temperature not specified in the publication, mutant enzyme F70V
0.31881
dehydroepiandrosterone
-
pH 7.5, temperature not specified in the publication, mutant enzyme V64C
0.34121
dehydroepiandrosterone
-
pH 7.5, temperature not specified in the publication, wild-type enzyme
0.23
diosgenin
pH 7.5, 37°C, full-length isozyme ChoM2
0.26
diosgenin
pH 7.5, 37°C, truncated isozyme ChoM2
0.45
O2
-
H69A mutant enzyme, 50 mM phosphate buffer, pH 7.5, 1% thesit, 1% 2-propanol
0.19061
pregnenolone
-
pH 7.5, temperature not specified in the publication, mutant enzyme F70V
0.2
pregnenolone
-
assay relies on spectroscopic detection of 4-cholesten-3-one formation
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
0.2
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
0.2
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
0.22842
pregnenolone
-
pH 7.5, temperature not specified in the publication, mutant enzyme V64C
0.29455
pregnenolone
-
pH 7.5, temperature not specified in the publication, wild-type enzyme
0.33
pregnenolone
pH 7.5, 37°C, full-length isozyme ChoM2
0.35
pregnenolone
pH 7.5, 37°C, truncated isozyme ChoM2
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
0.38412
stigmasterol
-
pH 7.5, temperature not specified in the publication, mutant enzyme F70V
0.52884
stigmasterol
-
pH 7.5, temperature not specified in the publication, mutant enzyme V64C
0.78961
stigmasterol
-
pH 7.5, temperature not specified in the publication, wild-type enzyme
0.5
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
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
0.2
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
0.3
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
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
additional information
additional information
-
Km-values of enzyme immobilized on platinum electrode modified with thiolipid/lipid bilayer membranes
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
7
epiandrosterone
-
H2O2 production assayed, 100 mM phosphate buffer
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
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
7
3beta-hydroxy-androst-5-en-17-one
-
assay relies on detection of H2O2 formation
8.2
3beta-hydroxy-androst-5-en-17-one
-
assay relies on spectroscopic detection of 4-cholesten-3-one formation
8.2
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
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
330
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
332
5-Cholesten-3-one
-
assay relies on spectroscopic detection of 4-cholesten-3-one formation
670
5-Cholesten-3-one
-
isomerization to 4-cholesten-3-one, rapid reaction, stopped-flow measurement, 50 mM phosphate buffer, pH 7.5, in the presence of 1% thesit and 1.25% 2-propanol
9.86
beta-sitosterol
-
pH 7.5, temperature not specified in the publication, wild-type enzyme
13.25
beta-sitosterol
-
pH 7.5, temperature not specified in the publication, mutant enzyme V64C
16.06
beta-sitosterol
-
pH 7.5, temperature not specified in the publication, mutant enzyme F70V
37
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
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
0.035
cholesterol
apparent value, mutant enzyme N485L, pH 5.1, temperature not specified in the publication
0.044
cholesterol
apparent value, mutant enzyme N485L, pH 7.0, temperature not specified in the publication
0.073
cholesterol
mutant enzyme N485D, determined by cholest-4-en-3-one detection
0.073
cholesterol
apparent value, mutant enzyme N485D, pH 7.0, temperature not specified in the publication
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
0.86
cholesterol
mutant enzyme F359W, determined by cholest-4-en-3-one detection
1
cholesterol
mutant enzyme G347N, determined by cholest-4-en-3-one detection
1.4
cholesterol
apparent value, mutant enzyme N485D, pH 5.1, temperature not specified in the publication
1.6
cholesterol
-
H69A mutant enzyme, cholesterol oxidation, 50 mM phosphate buffer, 1% thesit, 1% 2-propanol
3
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
6
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
9
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
11
cholesterol
-
assay relies on spectroscopic detection of 4-cholesten-3-one formation
11
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
12.29
cholesterol
-
pH 7.5, temperature not specified in the publication, wild-type enzyme
15.48
cholesterol
-
pH 7.5, temperature not specified in the publication, mutant enzyme F70V
23
cholesterol
pH 7.0, 37°C, mutant enzyme A32C/S129C/T371C/A423C, cholesterol solubilized in detergent micelles as a substrate
23.02
cholesterol
-
pH 7.5, temperature not specified in the publication, mutant enzyme V64C
30
cholesterol
pH 7.0, 37°C, mutant enzyme A32C/T168C/S312C/A465C, cholesterol solubilized in detergent micelles as a substrate
32
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
42
cholesterol
wild-type enzyme, determined by cholest-4-en-3-one detection
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
46
cholesterol
apparent value, wild type enzyme, pH 5.1, temperature not specified in the publication
46
cholesterol
pH 7.0, 37°C, mutant enzyme T168C/A276C, cholesterol solubilized in detergent micelles as a substrate
47
cholesterol
apparent value, wild type enzyme, pH 7.0, temperature not specified in the publication
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
57
cholesterol
pH 7.0, 37°C, mutant enzyme A184C/A301C/T394C, cholesterol solubilized in detergent micelles as a substrate
60
cholesterol
pH 7.0, 37°C, mutant enzyme A184C/T239C/A407C/A465C, cholesterol solubilized in detergent micelles as a substrate
63
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
63
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
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
67
cholesterol
pH 7.0, 37°C, wild-type enzyme, cholesterol solubilized in detergent micelles as a substrate
68
cholesterol
pH 7.0, 37°C, mutant enzyme S153C/A205C/S312C/T435C, cholesterol solubilized in detergent micelles as a substrate
75
cholesterol
pH 7.0, 37°C, mutant enzyme L274C, cholesterol solubilized in detergent micelles as a substrate
89
cholesterol
pH 7.0, 37°C, mutant enzyme L80C, cholesterol solubilized in detergent micelles as a substrate
105
cholesterol
-
50 mM phosphate buffer, pH 7.5, 1% thesit, 10% 2-propanol
345
cholesterol
-
50 mM phosphate buffer, pH 7.5, 1% thesit, 10% 2-propanol
6.82
dehydroepiandrosterone
-
pH 7.5, temperature not specified in the publication, wild-type enzyme
9.56
dehydroepiandrosterone
-
pH 7.5, temperature not specified in the publication, mutant enzyme V64C
13.68
dehydroepiandrosterone
-
pH 7.5, temperature not specified in the publication, mutant enzyme F70V
11.78
pregnenolone
-
pH 7.5, temperature not specified in the publication, wild-type enzyme
13.71
pregnenolone
-
pH 7.5, temperature not specified in the publication, mutant enzyme V64C
15.25
pregnenolone
-
pH 7.5, temperature not specified in the publication, mutant enzyme F70V
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
21
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
24
pregnenolone
-
assay relies on spectroscopic detection of 4-cholesten-3-one formation
24
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
24
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
0.08
stigmasterol
-
pH 7.5, temperature not specified in the publication, mutant enzyme F70V
1.58
stigmasterol
-
pH 7.5, temperature not specified in the publication, wild-type enzyme
4.23
stigmasterol
-
pH 7.5, temperature not specified in the publication, mutant enzyme V64C
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
7
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
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
6
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
8.2
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
30
beta-sitosterol
-
pH 7.5, temperature not specified in the publication, wild-type enzyme
60
beta-sitosterol
-
pH 7.5, temperature not specified in the publication, mutant enzyme V64C
90
beta-sitosterol
-
pH 7.5, temperature not specified in the publication, mutant enzyme F70V
0.0013
cholesterol
-
apparent value, silk mat-immobilized enzyme, in 50 mM potassium phosphate buffer, pH 7.5, 30°C
60
cholesterol
-
pH 7.5, temperature not specified in the publication, wild-type enzyme
100
cholesterol
-
pH 7.5, temperature not specified in the publication, mutant enzyme F70V
130
cholesterol
-
pH 7.5, temperature not specified in the publication, mutant enzyme V64C
2000
cholesterol
pH 7.0, 37°C, mutant enzyme A32C/S129C/T371C/A423C, cholesterol solubilized in detergent micelles as a substrate
2400
cholesterol
pH 7.0, 37°C, mutant enzyme A32C/T168C/S312C/A465C, cholesterol solubilized in detergent micelles as a substrate
3400
cholesterol
pH 7.0, 37°C, mutant enzyme T168C/A276C, cholesterol solubilized in detergent micelles as a substrate
4500
cholesterol
pH 7.0, 37°C, mutant enzyme L274C, cholesterol solubilized in detergent micelles as a substrate
4600
cholesterol
pH 7.0, 37°C, mutant enzyme A184C/T239C/A407C/A465C, cholesterol solubilized in detergent micelles as a substrate
5000
cholesterol
pH 7.0, 37°C, mutant enzyme A184C/A301C/T394C, cholesterol solubilized in detergent micelles as a substrate
5100
cholesterol
pH 7.0, 37°C, wild-type enzyme, cholesterol solubilized in detergent micelles as a substrate
7000
cholesterol
pH 7.0, 37°C, mutant enzyme S153C/A205C/S312C/T435C, cholesterol solubilized in detergent micelles as a substrate
8400
cholesterol
pH 7.0, 37°C, mutant enzyme L80C, cholesterol solubilized in detergent micelles as a substrate
20
dehydroepiandrosterone
-
pH 7.5, temperature not specified in the publication, wild-type enzyme
30
dehydroepiandrosterone
-
pH 7.5, temperature not specified in the publication, mutant enzyme V64C
50
dehydroepiandrosterone
-
pH 7.5, temperature not specified in the publication, mutant enzyme F70V
40
pregnenolone
-
pH 7.5, temperature not specified in the publication, wild-type enzyme
60
pregnenolone
-
pH 7.5, temperature not specified in the publication, mutant enzyme V64C
80
pregnenolone
-
pH 7.5, temperature not specified in the publication, mutant enzyme F70V
2
stigmasterol
-
pH 7.5, temperature not specified in the publication, wild-type enzyme
8
stigmasterol
-
pH 7.5, temperature not specified in the publication, mutant enzyme V64C
20
stigmasterol
-
pH 7.5, temperature not specified in the publication, mutant enzyme F70V
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.1
purified full-length isozyme ChoM2, substrate pregnenolone, pH 7.5, 37°C
0.12
purified truncated isozyme ChoM2, substrate pregnenolone, pH 7.5, 37°C
0.13
purified isozyme ChoM1, substrate pregnenolone, pH 7.5, 37°C
0.16
purified isozyme ChoM1, substrate dehydroandrosterone, pH 7.5, 37°C
0.17
purified truncated isozyme ChoM2, substrate dehydroandrosterone, pH 7.5, 37°C
0.19
0.21
purified full-length isozyme ChoM2, substrate diosgenin, pH 7.5, 37°C
0.22
0.23
purified isozyme ChoM1, substrate cholesterol, pH 7.5, 37°C
0.24
native crude enzyme intracellular in strain JC-12, both ChoM isozymes, pH 7.5, 40°C
0.25
purified full-length isozyme ChoM2, substrate beta-sitosterol, pH 7.5, 37°C
0.26
purified truncated isozyme ChoM2, substrate diosgenin, pH 7.5, 37°C
0.28
0.33
purified truncated isozyme ChoM2, substrate beta-sitosterol, pH 7.5, 37°C
0.42
purified truncated isozyme ChoM2, substrate cholesterol, pH 7.5, 37°C
0.78
native crude enzyme extracellular in strain JC-12, both ChoM isozymes, pH 7.5, 40°C
11.2
purified recombinant His-tagged isozyme ChoM1, pH 7.5, 40°C
12
-
N-terminally His-tagged recombinant enzyme expressed in Escherichia coli, pH 7.2, 37°C
16
-
non-tagged recombinant enzyme expressed in Escherichia coli, pH 7.2, 37°C
17.2
purified recombinant His-tagged isozyme ChoM2, pH 7.5, 40°C
4
-
C-terminally His-tagged recombinant enzyme expressed in Escherichia coli, pH 7.2, 37°C
additional information
0.19
purified isozyme ChoM1, substrate diosgenin, pH 7.5, 37°C
0.19
purified full-length isozyme ChoM2, substrate dehydroandrosterone, pH 7.5, 37°C
0.22
purified isozyme ChoM1, substrate beta-sitosterol, pH 7.5, 37°C
0.28
purified full-length isozyme ChoM2, substrate cholesterol, pH 7.5, 37°C
additional information
-
comparison of the effect of detergents and solvents on ChOx activity and stability (from different sources)
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)
additional information
-
comparison of the effect of detergents and solvents on ChOx activity and stability (from different sources)
additional information
Nocardia erythropolis
-
comparison of the effect of detergents and solvents on ChOx activity and stability (from different sources)
additional information
Nocardia rhodochrous
-
comparison of the effect of detergents and solvents on ChOx activity and stability (from different sources)
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)
additional information
Pseudomonas spp.
-
comparison of the effect of detergents and solvents on ChOx activity and stability (from different sources)
additional information
-
1162 U/ml, crude enzyme, pH 7.5, 35°C
additional information
-
comparison of the effect of detergents and solvents on ChOx activity and stability (from different sources)
additional information
-
comparison of the effect of detergents and solvents on ChOx activity and stability (from different sources)
additional information
Streptoverticillum cholesterolicum
-
comparison of the effect of detergents and solvents on ChOx activity and stability (from different sources)
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)
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 7
the enzyme activity retains more than 95% of its maximal activity within the pH range of 6-7 at 25°C
6.5
6.8 - 8
7 - 7.5
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 13
-
activity range, profile overview
4 - 10
4 - 7.5
-
the activity increases with increasing pH value from 4.0 to 7.5 and then declines as pH increases further
4 - 8
-
pH 4.0: native enzyme showes about 40% of maximal activity, enzyme immobilized on polyacrylonitrile hollow fibers shows about 65% of maximal activity, pH 8.0: native enzyme showes about 60% of maximal activity, enzyme immobilized on polyacrylonitrile hollow fibers shows about 85% of maximal activity
4.5 - 8
Nocardia rhodochrous
-
about 50% of maximal activity at pH 4.5, about 90% of maximal activity at pH 8
5 - 6.5
-
pH 5.0: about 90% of maximal activity, pH 6.5: about 60% of maximal activity, pH 7.0: about 20% of maximal activity
5 - 7.5
-
pH 5.0: about 70% of maximal activity, pH 7.5: about 30% of maximal activity
5 - 8
5 - 8.5
5 - 9
5 - 9.5
5.5 - 8
relative high activities in a broad pH range of 6.0-8.0, however activity rapidly declines under pH 5.5
5.5 - 8.5
6 - 7
the enzyme activity retains more than 95% of its maximal activity within the pH range of 6-7 at 25°C
6 - 9
6 - 9.5
6.5 - 9
additional information
-
pH-dependencies of native and recombinant non-tagged or His-tagged enzyme is similar, overview
5 - 8
-
pH 5: 78% of maximal activity, pH 8.0: 75% of maximal activity, reaction with cholestero, enzyme CO2
5 - 8
pH 5.0: about 45% of maximal activity, pH 8.0: about 40% of maximal activity
5 - 8.5
-
pH 5.0: about 75% of maximalm acttivity, pH 8.5: about 60% of maximal activity, cholesterol oxidase II
5 - 9
-
pH 5: 83% of maximal activity, pH 9.0: 77% of maximal activity, reaction with cholesterol, enzyme CO1
5 - 9
-
more than 75% of the maximal activity is retained over the pH range of 5.0-9.0
5 - 9.5
-
pH 5.0: about 50% of maximal activity, pH 9.5: about 40% of maximal activity
5.5 - 8.5
-
pH 5.5: about 50% of maximal activity, pH 8.5: about 40% of maximal activity, cholesterol oxidase I
5.5 - 8.5
pH 5.5: about 50% of maximal activity, pH 8.5: about 55% of maximal activity
5.5 - 8.5
pH 5.5: about 60% of maximal activity, pH 8.5: about 65% of maximal activity
6 - 9
-
pH 6.0: about 20% of maximal activity, pH 9.0: about 55% of maximal activity
6 - 9
-
pH 6.0: about 50% of maximal activity, pH 9.0: about 40% of maximal activity
6 - 9.5
-
pH 6.0: about 65% of maximal activity, pH 9.5: about 60% of maximal activcity
6 - 9.5
-
inducible enzyme, 80% of maximal activity at pH 6.0, 50% at pH 9.5, constitutive enzyme, 70% of maximal activity at pH 6.0, 50% at pH 9.5
6.5 - 9
pH 6.5: about 50% of maximal activity, pH 9.0: about 50% of maximal activity
6.5 - 9
ChoL retains more than 80% activity in the pH range 6.5-9.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
35
37
40
45
50
55
60
65
70
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15 - 55
-
activity range, profile overview
20 - 50
-
20°C: about 45% of maximal activity, 50°C: about 35% of maximal activity
25 - 45
25 - 50
30 - 50
30 - 55
-
30°C: about 65% of maximal activity, 55°C: about 60% of maximal activity, reaction with cholesterol, enzyme CO2
30 - 70
-
30°C: about 85% of maximal activity, 70°C: about 80% of maximal activity
30 - 80
30°C: about 42% of maximal activity, 80°C: about 24% of maximal activity
33 - 60
-
constitutive enzyme, 50% of maximal activity at 33°C, 70% at 60°C, inducible enzyme, 50% of maximal activity at 33°C and 60°C
35 - 48
ChoL retains more than 80% activity in the temperature range 35-48°C
35 - 75
-
about 50% of maximal activity at 35°C and at 75°C, reaction with cholesterol, enzyme CO1
40 - 60
40°C: about 40% of maximal activity, 60°C: about 80% of maximal activity
40 - 70
the enzyme activity retains more than 60% of its activity at the temperatures from 40°C to 70°C
40 - 80
25 - 45
25°C: about 85% of maximal activity, 45°C: about 40% of maximal activity
25 - 45
-
the oxygen depletion rate is increased with increasing temperature from 25°C to 40°C but it decreases sharply as the temperature increases further to 45°C
25 - 50
-
25°C: about 70% of maximal activity, 50°C: about 55% of maximal activity
25 - 50
-
25°C: about % of maximal activity, 50°C: about 60% of maximal activity
30 - 50
30°C: about 60% of maximal activity, 50°C: about 60% of maximal activity
40 - 80
-
40°C: about 70% of maximal activity, 80°C: about 40% of maximal activity
40 - 80
40°C: about 50% of maximal activity, 80°C: about 70% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.9
-
isoelectric focusing with carrier ampholites pH 4-6, cholesterol oxidase II
5.7
calculated from amino acid sequence
9
pI-value about 9.0, isoelectric focusing
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isolated from a soil sample collected from the riverside of the Yellow River in Jinan City, Shandong Province, China
-
-
brenda
Nocardia erythropolis
-
-
-
brenda
Nocardia rhodochrous
isolated from urban compost and dairy soil samples
-
-
brenda
isolated from brackish water of the Chilika Lake at Odisha state of India
-
-
brenda
from soil sample collected from effluent sediment of a steel plant in Barabanki (Uttar Pradesh, India)
-
-
brenda
from soil sample collected from effluent sediment of a steel plant in Barabanki (Uttar Pradesh, India)
-
-
brenda
isolated from pre-treated soil sample collected from the agricultural fields of Northern India
-
-
brenda
isolated from a soil sample collected from the riverside of the Yellow River in Jinan City, Shandong Province, China
-
-
brenda
-
287646, 287656, 287663, 287665, 287667, 287668, 287670, 287673, 287674, 287675, 287676, 287677, 672460, 674444, 687754
-
-
brenda
probably identical with cholesterol decompositing Mycobacterium cholesterolicum
-
-
brenda
isozyme ChoM2; isolated from the environment, China
UniProt
brenda
isozyme ChoM2; isolated from the environment, China
UniProt
brenda
high levels of ChOx activity, significant similarities to putative ChOxs encoded by Mycobacterium tuberculosis and Mycobacterium leprae
-
-
brenda
ATCC 25544, de novo enzyme synthesis is induced by cholesterol
-
-
brenda
isolated from brackish water of the Chilika Lake at Odisha state of India
-
-
brenda
isolated from urban compost and dairy soil samples
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
the strain reaches its maximal utilization of cholesterol as the only C source for production of extracellular cholesterol oxidase
brenda
additional information
-
production of cholesterol oxidase under batch conditions through Ca-alginate immobilized cells of Streptomyces sp., optimization of immobilization method and production conditions, overview. The enzyme production with immobilized cells is higher in comparison to free cells under optimized conditions. Production medium inoculated with 2% v/v or 8.8 mg dry cell weight seed culture and incubated at 200 rpm and 30°C for 96 h gves maximum COD enzyme production after 96 h whereas the immobilized culture gives maximum production at 37°C and 300 rpm after 72 h of incubation. The immobilized cells can be used for three consecutive fermentation cycles for COD production in higher quantities as compared with free cells
brenda
additional information
-
enzyme production reaches its maximum by incubation at 30°C for 12 d
brenda
additional information
-
optimization of conditions for cholesterol oxidase production by the microorganism isolated from urban compost and dairy soil samples, optimal conditions for production of enzyme CHO from Rhodococcus sp. strain COP2 are pH 7.5 and 35°C, effect of inorganic and organic nitrogen sources on enzyme production, overview
brenda
additional information
-
optimization of conditions for cholesterol oxidase production by the microorganism isolated from urban compost and dairy soil samples, optimal conditions for production of enzyme CHO from Rhodococcus sp. strain COP2 are pH 7.5 and 35°C, effect of inorganic and organic nitrogen sources on enzyme production, overview
-
brenda
additional information
-
Streptomyces parvus shows markedly high cho activity in culture broth
brenda
additional information
-
Streptomyces parvus shows markedly high cho activity in culture broth
-
brenda
additional information
-
effect of carbon and nitrogen sources on COD production, highest activity on lactose and sucrose and on yeast extract, respectively, overview
brenda
additional information
-
optimization of cell growth and cholesterol oxidase production by using Streptomyces sp. strain NCIM 5500 using artificial neural networks (ANNs), complex mathematical models that successfully mimic biological neural networks, modeling, development and optomizationof a regression model, overview
brenda
additional information
-
effect of carbon and nitrogen sources on COD production, highest activity on lactose and sucrose and on yeast extract, respectively, overview
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
produces both cell-linked and extracellular enzyme in high amount
-
brenda
ChoM1 is mainly associated with the cell envelope
brenda
ChooM2 is mainly extracellular and soluble
-
brenda
-
produces both cell-linked and extracellular enzyme in high amount
-
brenda
-
the enzyme is secreted
-
brenda
-
the enzyme is secreted
-
-
brenda
the lack of a signal peptide indicated the intracellular localization of the enzyme in the native host
brenda
-
the lack of a signal peptide indicated the intracellular localization of the enzyme in the native host
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug target
cholesterol oxidase can alter the structure of the cell membrane in pathogenic bacteria and is thus a potential antimicrobial drug target
evolution
malfunction
metabolism
physiological function
additional information
evolution
CgChoA belongs to the non-covalent FAD-dependent enzymes belonging to the class I family
evolution
the type I CO from Streptomyces sp. SA-COO is a member of the glucosemethanolcholine (GMC) oxidoreductase family and contains a single molecule of flavin adenine dinucleotide (FAD) noncovalently but tightly bound to the protein
evolution
-
CgChoA belongs to the non-covalent FAD-dependent enzymes belonging to the class I family
-
malfunction
the disruption of the choG gene does not alter the ability of strain CECT3014 cells to grow on cholesterol, but it abolishes the production of extracellular cholesterol oxidase
malfunction
the deletion mutant of choM1 completely lose the ability to form colonies on the cholesterol agar, the catabolism of sterols is greatly blocked, phenotype, overview
malfunction
-
intracellular replication of an Mycobacterium tuberculosis mutant lacking a functional choD gene (DELTAchoD) is less efficient in macrophages than that of the wild-type strain. In contrast to wild-type tb, the DELTA strain inducesnitric oxide production in macrophages, an action that depends on the TLR2, but not the CR3, signaling pathway. Both wild-type and mutant strains inhibit the production of reactive oxygen species, but the DELTAchoD strain does so to a significantly lesser extent. Blocking TLR2-mediated signaling abolishes the inhibitory effect of wild-type Mycobacterium tuberculosis on reactive oxygen species production by macrophages. The mutant DELTAchoD strain, does not decrease phorbol myristate acetate-induced phosphorylation of extracellular signal-regulated kinases 1 and 2 (ERK1/2) ib contrast to the wild-type. The production of interleukin 10 by macrophages is significantly lower in DELTAchoD-infected macrophages than in wild-type Mtb-infected macrophages
malfunction
-
the disruption of the choG gene does not alter the ability of strain CECT3014 cells to grow on cholesterol, but it abolishes the production of extracellular cholesterol oxidase
-
metabolism
PimE is a key enzyme in the biosynthesis of the polyene macrolide pimaricin
metabolism
cholesterol oxidase ChoM1 is involved in the oxidation of sterols to sterones, a rate-limiting step in the catabolic pathway of sterols in Mycobacterium neoaurum. The bacterium exhibits definite preference for steroidal substrates possessing the 3-keto-4-ene moiety rather than the 3beta-ol-5-ene moiety
metabolism
cholesterol oxidase ChoM2 is involved in the oxidation of sterols to sterones, a rate-limiting step in the catabolic pathway of sterols in Mycobacterium neoaurum
metabolism
-
the enzyme that is involved but is dispensable in the process of cholesterol degradation by Mycobacterium tuberculosis
metabolism
the enzyme catalyzes the first step in the biodegradation of cholesterol
physiological function
ChoD plays a significant role in the pathogenesis of Mycobacterium tuberculosis
physiological function
the conversion of sterols from 3beta-ol-5-ene moiety to 3-keto-4-ene moiety, i.e. the transformation of sterols to sterones, is a rate-limiting step in the catabolic pathway of sterols in Mycobacterium neoaurum. The conversion of 3beta-ol-5-ene moiety to 3-keto-4-ene moiety of sterols is indispensible for the catabolism of sterols in strain ATCC25795
physiological function
-
cholesterol oxidase from Bordetella species promotes irreversible cell apoptosis in lung adenocarcinoma by cholesterol oxidation in vitro and in vivo. COD-B treatment results in JNK and p38 phosphorylation, downregulation of Bcl-2, upregulation of Bax, activated caspase-3 and cytochrome C release, which likely responds to freshly produced hydrogen peroxide that accompanies cholesterol oxidation. COD-B leads to irreversible cell apoptosis by decreasing cholesterol content and increasing reactive oxygen species level. Cholesterol oxidase (COD) is a flavoprotein that catalyzes the oxidation of cholesterol to 4-cholesten-3-one with the reduction of oxygen to hydrogen peroxide. COD can convert membrane cholesterol to 4-cholesten-3-one and can inhibit the formation of lipid rafts. Different from other cholesterol-depleting agents, COD disrupts lipid rafts by displacing cholesterol with 4-cholesten-3-one. COD-B catalyzes the oxidation of membrane cholesterol in lung adenocarcinoma cell. When cells are pretreated with catalase before adding COD-B and cholesterol, the phosphorylation of Akt and ERK1/2 remaines attenuated compared with the group without catalase treatment. Catalase pretreatment also partially blocks the activation of caspase-3, effect of catalase on the COD-B-induced signaling response, overview. COD-B induces the reversible translocation of caveolin-1, which is involved in trafficking membrane cholesterol, in a cholesterol-reversable manner
physiological function
-
cholesterol oxidase ChoD is capable of modifying the bactericidal and pro-inflammatory activity of human macrophages. and is indispensable in the pathogenesis of Mycobacterium tuberculosis. The enzyme is enzyme capable of converting cholesterol to its 3-keto-4-ene derivative, cholestenone. The wild-type strain inhibits the production of reactive oxygen species. Wild-type Mycobacterium tuberculosis, but not the DELTAchoD strain, decreases phorbol myristate acetate-induced phosphorylation of extracellular signal-regulated kinases 1 and 2 (ERK1/2), which are involved in both TLR2-and CR3-mediated signaling pathways
physiological function
cholesterol oxidase (ChoD) is a virulence factor that enables Mycobacterium tuberculosis to disturb the TLR2-related signalling pathway in macrophages and modulate their response
physiological function
-
the enzyme (ChoD) is a virulence factor of Mycobacterium tuberculosis, and it strongly modulates the function of human macrophages in vitro, allowing the intracellular survival of bacteria. It is an active protein, which is able to induce the immune response both in vivo and in vitro
physiological function
-
ChoD plays a significant role in the pathogenesis of Mycobacterium tuberculosis
-
physiological function
-
cholesterol oxidase (ChoD) is a virulence factor that enables Mycobacterium tuberculosis to disturb the TLR2-related signalling pathway in macrophages and modulate their response
-
additional information
-
a extracellular halo tolerant, detergent and organic solvent stable alkaline cholesterol oxidase. The enzyme is stable in presence of chemical reagents (NaN3, EDTA), detergents (Tween-80, Tween-20, Triton X-100, sodium cholate) and various organic solvents (isopropanol, ethanol, benzene, chloroform, methanol, toluene, ethyl acetate, butanol and dimethylsulfoxide)
additional information
key amino acid residues involved in substrate oxidation are His470 and Asn513 in ChoM1
additional information
key amino acid residues involved in substrate oxidation are His470 and Asn513 in ChoM1
additional information
key amino acid residues involved in substrate oxidation are His479 and Asn517 in ChoM1
additional information
key amino acid residues involved in substrate oxidation are His479 and Asn517 in ChoM1
additional information
the structure of the dithionite-reduced enzyme reveals a sulfite molecule covalently bound to the FAD cofactor. The isoalloxazine ring system displays a bent structure relative to that of the oxidized enzyme, and alternate conformations of a triad of aromatic residues near to the cofactor are evident. The strutcure of anaerobically trapped reduced enzyme structure in the presence of 2-propanol does not show a similar bending of the flavin ring system, but does show alternate conformations of the aromatic triad. The hydride transfer generates a tetrahedral geometry about the flavin N5 atom
additional information
-
key amino acid residues involved in substrate oxidation are His470 and Asn513 in ChoM1
-
additional information
-
key amino acid residues involved in substrate oxidation are His479 and Asn517 in ChoM1
-
additional information
-
a extracellular halo tolerant, detergent and organic solvent stable alkaline cholesterol oxidase. The enzyme is stable in presence of chemical reagents (NaN3, EDTA), detergents (Tween-80, Tween-20, Triton X-100, sodium cholate) and various organic solvents (isopropanol, ethanol, benzene, chloroform, methanol, toluene, ethyl acetate, butanol and dimethylsulfoxide)
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
48000
53000
55000
55700
x * 57900, recombinant His-tagged isozyme ChoM2, SDS-PAGE x * 55700, recombinant His-tagged isozyme ChoM2 lacking the signal peptide, SDS-PAGE
56000
57000
57900
x * 57900, recombinant His-tagged isozyme ChoM2, SDS-PAGE x * 55700, recombinant His-tagged isozyme ChoM2 lacking the signal peptide, SDS-PAGE
58000
59000
60000
63300
calculated from amino acid sequence
64300
x * 64300, recombinant His-tagged isozyme ChoM1, SDS-PAGE
85000
recombinant N-terminally His-tagged enzyme, gel filtration
55000
-
x * 55000, wild-type and mutant enzymes V145Q, V145E, S379A and S379V, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
?
x * 64300, recombinant His-tagged isozyme ChoM1, SDS-PAGE
?
x * 57900, recombinant His-tagged isozyme ChoM2, SDS-PAGE x * 55700, recombinant His-tagged isozyme ChoM2 lacking the signal peptide, SDS-PAGE
?
x * 64100, recombinant His-tagged isoyzme ChoM1, SDS-PAGE
?
x * 58800, recombinant His-tagged isoyzme ChoM2, SDS-PAGE
?
-
x * 55000, wild-type and mutant enzymes V145Q, V145E, S379A and S379V, SDS-PAGE
monomer
1 x 60400, about, recombinant N-terminally His-tagged enzyme, sequence calculation, 1 * 60000, recombinant N-terminally His-tagged enzyme, SDS-PAGE
monomer
-
1 x 60400, about, recombinant N-terminally His-tagged enzyme, sequence calculation, 1 * 60000, recombinant N-terminally His-tagged enzyme, SDS-PAGE
-
additional information
-
native cholesterol oxidase is composed of 39% alpha-helix, 40% beta-sheet, and 20% random coil, while the non-tagged enzyme is composed of 40% alpha-helix, 35% beta-sheet, and 24% random coil. In contrast, the N-terminally His-tagged enzyme is composed of 45% alpha-helix, 29% beta-sheet, and 25% random coil, and the C-terminally His-tagged enzyme is composed of 55% alpha-helix, 16% beta-sheet, and 28% random coil
additional information
-
native cholesterol oxidase is composed of 39% alpha-helix, 40% beta-sheet, and 20% random coil, while the non-tagged enzyme is composed of 40% alpha-helix, 35% beta-sheet, and 24% random coil. In contrast, the N-terminally His-tagged enzyme is composed of 45% alpha-helix, 29% beta-sheet, and 25% random coil, and the C-terminally His-tagged enzyme is composed of 55% alpha-helix, 16% beta-sheet, and 28% random coil
-
additional information
the overall enzyme structure comprises two domains, the FAD binding domain and the substrate binding domain, structure comparisons
additional information
-
the overall enzyme structure comprises two domains, the FAD binding domain and the substrate binding domain, structure comparisons
additional information
-
the overall enzyme structure comprises two domains, the FAD binding domain and the substrate binding domain, structure comparisons
-
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
Nocardia rhodochrous
-
3 enzyme forms differ chiefly in the presence or absence of hydrophobic anchor region connected by a trypsin-sensitive region, no phospholipids are extracted with the enzyme
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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
-
hanging-drop vapour-diffusion method using polyethylene glycol as a precipitating agent. The crystals belong to space group P3(1)21 with unit-cell parameters a = b = 119.6, c = 101.1 A, and has one subunit in the asymmetric unit
-
crystal screen based on sparse matrix formulation, using 500 mM ammonium sulfate, 1.0 M lithium sulfate and 10 mM sodium citrate
crystals of the H447Q/E361Q mutant protein are grown by hanging-drop vapor diffusion method, high-resolution crystal structure of mutant enzyme H447Q/E361Q with glycerol and without glycerol
-
mutant enzymes N485D and N485L, hanging drop vapor diffusion method, using 9-11% (w/v) polyethylene glycol 8000, 75 mM MnSO4 and 100 mM sodium cacodylate pH 5.2
structure of the F359W mutant enzyme, hanging drop vapor diffusion method. In the atomic-resolution structure of F359W, the indole ring of the tryptophan completely fills the tunnel and is observed in only a single conformation
Sub-atomic resolution crystal structure, crystallographic data: space group P2(1), a = 52.23 A, b * 72.9 A, c = 62.95 A, beta = 105.1
vapor diffusion by hanging drop method, 1.5 A resolution, wild-type, E361Q, H447N and H447Q mutant, structure consists of FAD-binding and a steroid-binding domain with a large active site cavity in between
purified nontagged and His6-tagged enzyme reduced with dithionite under aerobic conditions and in the presence of the substrate 2-propanol under both aerobic and anaerobic conditions, vapour diffusion using the hanging-drop method, mixing of 7 mg/ml protein in 50 mM HEPES pH 7.0 with reservoir solution containing 7% PEG 8000, 100 mM cacodylate, pH 5.2, 125 mM MnSO4, followed by microseeding in 12% PEG 8000, 100 mM sodium cacodylate, pH 5.2, 125 mM MnSO4, X-ray diffraction structure determination and analysis at 1.12-1.34 A resolution
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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
F70A
-
improved activities toward cholestane skeleton substrates. Improved activity toward beta-sitosterol, dehydroepiandrosterone, pregnenolone and stigmasterol
F70L
-
the mutant enzyme shows almost the same level of activity as the wild-type enzyme
F70V
-
mutation increases the binding free energy between the mutant enzyme (PsChO) and cholesterol and might cause the movement of loops L56-P77, K45-P49 and L350-E354 at active site. Improved activities toward cholestane skeleton substrates. 50% higher activities toward cholesterol when compared with that of the wild-type enzyme
V64C
-
mutation increases the binding free energy between the mutant enzyme (PsChO) and cholesterol and might cause the movement of loops L56-P77, K45-P49 and L350-E354 at active site. Improved activities toward cholestane skeleton substrates. 50% higher activities toward cholesterol when compared with that of the wild-type enzyme
V64I
-
improved activities toward cholestane skeleton substrates. Improved activity toward beta-sitosterol, dehydroepiandrosterone, pregnenolone and stigmasterol
V64L
-
improved activities toward cholestane skeleton substrates. Improved activity toward beta-sitosterol, dehydroepiandrosterone, pregnenolone and stigmasterol
E361A
-
site-directed mutagenesis, the mutant shows no dehydrogenase activity
E361Q
F359A
-
site-directed mutagenesis, the dehydrogenase/oxidase ratio is 12fold increased compared with the ratio for the wild-type enzyme
F359W
kcat for the F359W mutant-catalyzed reaction decreases 13fold relative to that of the wild-type-catalyzed reaction. Transfer of hydride from the sterol to the flavin prosthetic group is no longer rate-limiting for the mutant enzyme. Kinetic cooperativity with respect to molecular oxygen is observed with the tunnel mutant, but not with the wild-type enzyme. In the atomic-resolution structure of F359W, the indole ring of the tryptophan completely fills the tunnel and is observed in only a single conformation. The size of the indole is proposed to limit conformational rearrangement of residue 359 that leads to tunnel opening in the wild-type enzyme
F444A
-
site-directed mutagenesis, the dehydrogenase/oxidase ratio is 4fold increased compared with the ratio for the wild-type enzyme
G347N
mutant can not be saturated with oxygen. Transfer of hydride from the sterol to the flavin prosthetic group is no longer rate-limiting for the mutant enzyme. Kinetic cooperativity with respect to molecular oxygen is observed with the tunnel mutant, but not with the wild-type enzyme
H447E
-
turnover number for cholesterol is decreased about 2600fold compared to wild-type enzyme
H447E/E361Q
-
turnover number for cholesterol is decreased about 31500fold compared to wild-type enzyme. Mutant enzyme is not able to isomerize cholest-5-en-3-one. Mutant enzyme is folded like native enzyme and still associates with model membranes
H447N
H447Q mutant shows wild-type activity in isomerization, kcat for oxidation reaction is reduced 120fold, Km increases 2fold compared to wild-type, E361Q mutant has no isomerization activity, kcat is 30fold slower than for wild-type, Glu361 may therefore act as general base in oxidation reaction
H447Q
H447Q/E361Q
-
turnover number for cholesterol is decreased 473fold compared to wild-type enzyme, 1.7fold increase in Km-value for cholesterol compared to wild-type enzyme. Mutant enzyme is not able to isomerize cholest-5-en-3-one
M122A
-
site-directed mutagenesis, the dehydrogenase/oxidase ratio is 26fold increased compared with the ratio for the wild-type enzyme
N485A
-
site-directed mutagenesis, the mutant shows no dehydrogenase activity
N485D
N485L
the kcat of N485D is diminished about 1110times compared with that of wild type, while the apparent Km value is minimally affected
V124A
-
site-directed mutagenesis, the dehydrogenase/oxidase ratio is 30fold increased compared with the ratio for the wild-type enzyme
V191A
-
site-directed mutagenesis, the mutant enzymes shows a significant decrease in its oxidase activity, but shows increased dehydrogenase activity. The dehydrogenase/oxidase ratio of Val191Ala is more than 150%, which is a 408fold increase compared with the ratio for the wild-type enzyme, substrate inhibition with cholesterol
Y446A
-
site-directed mutagenesis, the dehydrogenase/oxidase ratio is 3fold increased compared with the ratio for the wild-type enzyme
A184C/T239C/A407C/A465C
kcat/KM is 1.1fold lower than wild-type value
A32C/S129C/T371C/A423C
kcat/KM is 2.55fold lower than wild-type value
A32C/T168C/S312C/A465C
kcat/KM is 2.1fold lower than wild-type value
His447Gln/H447N
mutations cause notable decreases in the catalytic activity
S153C/A205C/S312C/T435C
kcat/KM is 1.4fold higher than wild-type value
additional information
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
E361Q
H447Q mutant shows wild-type activity in isomerization, kcat for oxidation reaction is reduced 120fold, Km increases 2fold compared to wild-type, E361Q mutant has no isomerization activity, kcat is 30fold slower than for wild-type, Glu361 may therefore act as general base in oxidation reaction
E361Q
-
turnover number for cholesterol is decreased 31.4fold compared to wild-type enzyme, 1.8fold increase in Km-value for cholesterol compared to wild-type enzyme
H447Q
H447Q mutant shows wild-type activity in isomerization, kcat for oxidation reaction is reduced 120fold, Km increases 2fold compared to wild-type, E361Q mutant has no isomerization activity, kcat is 30fold slower than for wild-type, Glu361 may therefore act as general base in oxidation reaction
H447Q
-
turnover number for cholesterol is decreased 137.5fold compared to wild-type enzyme, Km-value for cholesterol is identical to wild-type value
N485D
mutant can not be saturated with oxygen. Transfer of hydride from the sterol to the flavin prosthetic group is no longer rate-limiting for the mutant enzyme. Kinetic cooperativity with respect to molecular oxygen is observed with the tunnel mutant, but not with the wild-type enzyme
N485D
the kcat of N485D is diminished about 650times compared with that of wild type, while the apparent Km value is minimally affected. For the N485D mutant, pH 5.1results in a 20fold increase in the rate of oxidation compared with that at pH 7.0
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
additional information
development of a strategy to overcome the rate-limiting step catalzed by the enzyme by augmenting the activity of cholesterol oxidases in Mycobacterium neoaurum strains to enhance their transformation productivity of sterols to valuable steroids, overview
additional information
development of a strategy to overcome the rate-limiting step catalzed by the enzyme by augmenting the activity of cholesterol oxidases in Mycobacterium neoaurum strains to enhance their transformation productivity of sterols to valuable steroids, overview
additional information
-
development of a strategy to overcome the rate-limiting step catalzed by the enzyme by augmenting the activity of cholesterol oxidases in Mycobacterium neoaurum strains to enhance their transformation productivity of sterols to valuable steroids, overview
additional information
-
engineered ChOx to improve activity and alter specificity
additional information
-
site-directed mutagenesis on oxygen-binding residues, which are observed in the high-resolution crystal structure, in order to elucidate the amino acid residues responsible for the oxidase activity, overview. Engineering of the enzyme for electrochemical monitoring of cholesterol
additional information
-
engineered ChOx to improve activity and alter specificity
additional information
Streptoverticillum cholesterolicum
-
engineered ChOx to improve activity and alter specificity
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1 - 2
purified recombinant enzyme, 30°C, 10% activity remaining after 30 min
10
11
purified recombinant enzyme, 30°C, 30 min, 70% activity remaining
3 - 11
4 - 10
4 - 11
4.5 - 10.5
ChoRII is stable. Shows higher stability than ChoRI even at pH 11 to 12
5 - 8
6 - 10
6 - 8.5
-
purified enzyme, completely stable at
9.5
-
purified enzyme, loss of 85% activity
4
-
purified enzyme, loss of 80% activity
5
-
the enzyme retains 82.36% of its activity after 3 h and losing most of its activity (15.95%) after 24 h
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
138.5
Tm-value, enzyme immobilized and encapsulated as Cu-COD hybrid nanoflowers
37
4 - 50
-
strain ST-200, 27% activity lost after incubation at 60°C, complete loss of activity at 70°C
4 - 65
40
40 - 50
-
purified enzyme, about 80% reduction of activity after 100 days
40 - 60
the enzyme is stable below 40°C without obvious inactivation after 6 h of incubation. When the temperature exceeds 50°C, the ChoL activity rapidly decreases. The enzyme retains approximately 40% of its initial activity after incubation for 6 h at 50°C and 17% after incubation for 1 h at 60°C
45 - 55
after 1 h of incubation, more than 70 and 50% of activity remains at 45 and 55°C, respectively
50
50 - 60
Corynebacterium cholesterolicum
-
96% activity after 30 min at 50°C, 6% activity after 30 min at 60°C
55
60
60 - 70
-
purified enzyme, activity s reduced to 85% and 48% after 10 days and is rapidly reduced during further incubation
60 - 85
the enzyme retains more than 90% of its original activity after incubation for 240 min at 60°C, 90% activity after 1 h at 80°C, and 80% activity after 30 min at 85°C
70
70 - 80
75 - 80
purified recombinant enzyme, pH 7.0, 30 min, inactivation
80
50
-
purified enzyme, 90% or 80% activity remaining after 1 h or 2 h, respectively
50
-
half-life: 156.25 min. 63.86% of the initial activity is retained by the enzyme after 20 min of incubation at 50 °C
55
-
tetraethylorthosilicate sol-gel/ChEt/ChOx (cholesterol esterase (ChEt) and cholesterol oxidase (ChOx) immobilized onto tetraethylorthosilicate derived sol-gel film) reveal thermal stability up to 55°C
60
-
half-lives of S103T, V121A, R135H, V145E mutants and wild-type: 11.3, 12.2, 11.0, 24.1 and 7.8 min respectively, half-lives of S103T/V145A double mutants and S103T/V145A/V121A triple mutants: 32.4 and 52.2 min respectively
70
purified recombinant enzyme, pH 7.0, 30 min, 90% activity remaining
70 - 80
70% residual activity after 30 min at 70°C, complete loss of activity after 30 min at 80°C
70 - 80
-
70% activity after 30 min at 70°C, complete loss of activity after 30 min at 80°C
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
65% activity remains after 24 h at 25C 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
after being reused six times, the enzyme immobilized on polyacrylonitrile hollow fibers retains more than 80% of its activity
-
purified enzyme, 80% residual activity with 20% NaCl (3.42 M) and 83% relative activity with 12% NaCl (2.05 M) concentration. The enzyme is stable in presence of chemical reagents (NaN3, EDTA), detergents (Tween-80, Tween-20, Triton X-100, sodium cholate)
-
stable in nonionic detergents over a wide range. More than 90% of activity remains after 60 min at 60°C, at concentrations of 0.1% and 0.5% of emulgen A-60, Triton X-100, Triton X-405 or sodium cholate
-
stable in nonionic detergents over a wide range. More than 90% of activity remains after 60 min at 60°C, pH 7.0, at concentrations of 0.1% Emulgen A-60, Triton X-100, Triton X-405 or sodium cholate
-
the ChOx-immobilized silk mat maintains its initial activity till the fourth successive measurement and retains about 50% of its initial activity at the end of 25 measurements
-
thermostability of the enzyme immobilized and encapsulated as Cu-COD hybrid nanoflowers is significantly enhanced
65% activity remains after 24 h at 25C 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
-
65% activity remains after 24 h at 25C 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
-
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acetone
benzene
Butanol
chloroform
cyclohexane
-
119% activity remaining, pH 7.0, 37°C, 24 h, with mechanical shaking
cyclooctane
dimethyl sulfoxide
DMSO
the enzyme remains stable after incubation in 50% (v/v) for 24 h at 37°C
Emal 20CM
Ethanol
Ethyl acetate
isopropanol
Methanol
p-xylene
propan-2-ol
the activity of the enzyme is rapidly inactivated in the presence of 30% (v/v) propan-2-ol at 25°C
sarcosyl
SDS
the enzyme is relatively tolerant to treatment with SDS after incubation for 1 h at 30°C
sodium cholate
sodium dodecyl sarcosinate
the enzyme is relatively tolerant to treatment with sodium dodecyl sarcosinate even at 60°C
sodium laurylbenzenesulfonate
the enzyme is relatively tolerant to treatment with sodium laurylbenzenesulfonate after incubation for 1 h at 30°C
sodium polyoxyethylene alkyl ether sulfate
toluene
Triton X-100
Triton X-405
Tween 20
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
xylene
-
93% the activity remaining, pH 7.0, 37°C, 24 h, with mechanical shaking
additional information
Acetone
the enzyme remains stable after incubation in 50% (v/v) for 24 h at 37°C
Acetone
-
37°C, 24 h, 1 ml organic solvent added to 2 ml culture filtrate, 90% loss of activity
Acetone
in a ratio 1:2 with enzyme solution, pH 7.0, 37°C, 24 h, 2% activity remaining
Acetone
-
in a ratio 1:2 with enzyme solution, pH 7.0, 37°C, 24 h, 2% activity remaining
-
benzene
-
127% activity remaining, pH 7.0, 37°C, 24 h, with mechanical shaking
benzene
-
37°C, 24 h, 1 ml organic solvent added to 2 ml culture filtrate, stable
Butanol
the enzyme remains stable after incubation in 50% (v/v) for 24 h at 37°C
Butanol
-
37°C, 24 h, 1 ml organic solvent added to 2 ml culture filtrate, stable
chloroform
-
96% activity remaining, pH 7.0, 37°C, 24 h, with mechanical shaking
chloroform
-
96% activity remaining, pH 7.0, 37°C, 24 h, with mechanical shaking
-
chloroform
-
37°C, 24 h, 1 ml organic solvent added to 2 ml culture filtrate, stable
chloroform
in a ratio 1:2 with enzyme solution, pH 7.0, 37°C, 24 h, 89% activity remaining
chloroform
-
in a ratio 1:2 with enzyme solution, pH 7.0, 37°C, 24 h, 89% activity remaining
-
cyclooctane
-
37°C, 24 h, 1 ml organic solvent added to 2 ml culture filtrate, stable
cyclooctane
in a ratio 1:2 with enzyme solution, pH 7.0, 37°C, 24 h, 108% activity remaining
dimethyl sulfoxide
-
88% activity remaining, pH 7.0, 37°C, 24 h, with mechanical shaking
dimethyl sulfoxide
-
88% activity remaining, pH 7.0, 37°C, 24 h, with mechanical shaking
-
dimethyl sulfoxide
-
37°C, 24 h, 1 ml organic solvent added to 2 ml culture filtrate, stable
dimethyl sulfoxide
-
stable in presence of
Emal 20CM
the enzyme is relatively tolerant to treatment with Emal 20CM even at 60°C
Emal 20CM
stable and partially or slightly activated in the presence of 0.5% (w/v) detergent
Ethanol
the enzyme remains stable after incubation in 50% (v/v) for 24 h at 37°C
Ethanol
-
37°C, 24 h, 1 ml organic solvent added to 2 ml culture filtrate, stable
Ethanol
in a ratio 1:2 with enzyme solution, pH 7.0, 37°C, 24 h, 31% activity remaining
Ethanol
-
in a ratio 1:2 with enzyme solution, pH 7.0, 37°C, 24 h, 31% activity remaining
-
Ethyl acetate
-
93% activity remaining, pH 7.0, 37°C, 24 h, with mechanical shaking
Ethyl acetate
-
93% activity remaining, pH 7.0, 37°C, 24 h, with mechanical shaking
-
Ethyl acetate
the enzyme remains stable after incubation in 50% (v/v) for 24 h at 37°C
Ethyl acetate
-
37°C, 24 h, 1 ml organic solvent added to 2 ml culture filtrate, stable
isopropanol
the enzyme remains stable after incubation in 50% (v/v) for 24 h at 37°C
isopropanol
-
37°C, 24 h, 1 ml organic solvent added to 2 ml culture filtrate, stable
isopropanol
in a ratio 1:2 with enzyme solution, pH 7.0, 37°C, 24 h, 6% activity remaining
isopropanol
-
in a ratio 1:2 with enzyme solution, pH 7.0, 37°C, 24 h, 6% activity remaining
-
Methanol
the enzyme remains stable after incubation in 50% (v/v) for 24 h at 37°C
Methanol
-
37°C, 24 h, 1 ml organic solvent added to 2 ml culture filtrate, stable
Methanol
in a ratio 1:2 with enzyme solution, pH 7.0, 37°C, 24 h, 65% activity remaining
Methanol
-
in a ratio 1:2 with enzyme solution, pH 7.0, 37°C, 24 h, 65% activity remaining
-
p-xylene
-
37°C, 24 h, 1 ml organic solvent added to 2 ml culture filtrate, stable
p-xylene
in a ratio 1:2 with enzyme solution, pH 7.0, 37°C, 24 h, 102% activity remaining
sarcosyl
stable and partially or slightly activated in the presence of 0.5% (w/v) detergent
sarcosyl
-
stable and partially or slightly activated in the presence of 0.5% (w/v) detergent
-
sodium cholate
-
the enzyme is stable at 50% (v/v) sodium cholate after incubation for 1 h at 30°C
sodium cholate
the enzyme is stable in sodium cholate after incubation for 1 h at 30°C
sodium cholate
stable and partially or slightly activated in the presence of 0.5% (w/v) detergent
sodium cholate
-
stable and partially or slightly activated in the presence of 0.5% (w/v) detergent
-
sodium cholate
-
the enzyme retains more than 80% of its original activity in 0.5% (v/v) sodium cholate after incubation for 1 h at 60°C
sodium cholate
-
the enzyme retains more than 80% of its original activity in 0.5% (v/v) sodium cholate after incubation for 1 h at 60°C
-
sodium polyoxyethylene alkyl ether sulfate
-
the enzyme is stable at 50% (v/v) sodium polyoxyethylene alkyl ether sulfate after incubation for 1 h at 30°C
sodium polyoxyethylene alkyl ether sulfate
the enzyme is stable in sodium polyoxyethylene alkyl ether sulfate after incubation for 1 h at 30°C
toluene
-
37°C, 24 h, 1 ml organic solvent added to 2 ml culture filtrate, stable
toluene
in a ratio 1:2 with enzyme solution, pH 7.0, 37°C, 24 h, 112% activity remaining
Triton X-100
-
the enzyme is stable at 50% (v/v) Triton X-100 after incubation for 1 h at 30°C
Triton X-100
the enzyme is stable in Triton X-100 after incubation for 1 h at 30°C
Triton X-100
stable and partially or slightly activated in the presence of 0.5% (w/v) detergent
Triton X-100
-
stable and partially or slightly activated in the presence of 0.5% (w/v) detergent
-
Triton X-405
-
the enzyme is stable at 50% (v/v) Triton X-405 after incubation for 1 h at 30°C
Triton X-405
the enzyme is stable in Triton X-405 after incubation for 1 h at 30°C
Triton X-405
stable and partially or slightly activated in the presence of 0.5% (w/v) detergent
Triton X-405
-
stable and partially or slightly activated in the presence of 0.5% (w/v) detergent
-
Triton X-405
-
the enzyme retains more than 80% of its original activity in 0.5% (v/v) Triton X-405 after incubation for 1 h at 60°C
Triton X-405
-
the enzyme retains more than 80% of its original activity in 0.5% (v/v) Triton X-405 after incubation for 1 h at 60°C
-
Tween 20
-
the enzyme is stable at 50% (v/v) Tween 20 after incubation for 1 h at 30°C
Tween 20
the enzyme is stable in Tween 20 after incubation for 1 h at 30°C
Tween 20
stable and partially or slightly activated in the presence of 0.5% (w/v) detergent
Tween 20
-
stable and partially or slightly activated in the presence of 0.5% (w/v) detergent
-
additional information
-
the enzyme shows moderate stability towards all organic solvents except acetone, benzene and chloroform. The activity increases in presence of isopropanol and ethanol
additional information
-
the enzyme shows moderate stability towards all organic solvents except acetone, benzene and chloroform. The activity increases in presence of isopropanol and ethanol
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0-5°C, crystallized enzyme in lyophilized state, in the dark, stable for at least 10 months
-
30°C, purified enzyme, completely stable for 60 days, 24% reduction after 70 days, 60% reduction after 100 days
-
4-8°C, purified native enzyme, the enzyme maintains approximately 36% and 58.5% of its activity after 18 days of storage
-
4°C, ChOx-immobilized silk mat, when the measurements are made at 3 days interval the immobilized ChOx can retain about 50% of its original activity after 45 days of storage and when the same carried out with 7 days interval, about 70% of its original activity is retained till 60 days
-
4°C, enzyme immobilized on polyacrylonitrile hollow fibers retains 80% of its activity after 15 days, native enzym retains about 55% of its activity after 15 days
-
4°C, purified enzyme, completely stable for 60 days, 24% reduction after 70 days, 60% reduction after 100 days
-
95°C, purified natie enzyme, the enzyme loses activity by gradual thermal treatment, but it maintains 58.5% activity at 95°C after 2 h
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
butyl-Sepharose column chromatography and DEAE-cellulose column chromatography
effective method for the preparation of active PsChO3 using urea as denaturing agent, combined with his-tag trapping and on-column refolding. Using this method, the enzyme is successfully refolded from inclusion bodies expressed in Escherichia coli
extracellular enzyme 59fold from strain PKPD-CL by ammonium sulfate fractionation, anion exchange chromatography, ultrafiltration, and gel filtration
-
native enzyme 2.3fold by ammnium sulfate fractionation and gel filtration
-
native extracellular enzyme 14.3fold by ammonium sulfate fractionation and affinity chromatography
-
native extracellular enzyme 18fold by anion exchange chromatography and gel filtration
-
native extracellular enzyme 28.4fold from cell culture supernatant by ammonium sulfate fractionation, dialysis, and riboflavin affinity chromatography
-
native extracellular enzyme from medium 12fold to homogeneity by ammonium sulfate fractionation, dialysis, ultrafiltration, anion exchange chromatography and gel filtration
-
partially purified by precipitation with ammonium sulfate
-
polyethylene glycol 4000 precipitation, diethylaminoethyl Sephacel anionic column chromatography and Superdex-200 gel filtration
Streptomyces sp. AKHSS
-
recombinant His-tagged isozyme CHOM1 from Bacillus subtilis strain 168/pMA5 by nickel affinity chromatography
recombinant His-tagged isozyme CHOM2 from Bacillus subtilis strain 168/pMA5 by nickel affinity chromatography
recombinant His6-tagged enzyme from Escherichia coli train BL21(DE3) by nickel affinity chromatography, dialysis and ultrafiltration
recombinant N-terminally His-tagged enzyme from Escherichia coli strain JM109 by nickel affinity chromatography
recombinant wild-type and mutant enzymes with with His-tags both at the N-terminus and at the C-terminus from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography
-
strain ST-200, ammonium sulfate, DEAE-cellulose, butyl-toyopearl, Sephadex G-100
-
to purify the recombinant enzyme, 500 mg cholesterol is added to 50 ml of crude extract, and then incubated for 2 h at 4°C followed by centrifugation at 10000g for 10 min
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
ChoL, a fragment of a cholesterol oxidase is expressed in Escherichia coli BL21(DE3) plysS cells
cholesterol oxidase II, expression in Escherichia coli MM294/pnH10
-
cloning, sequencing and analysis of partial segment of cholesterol oxidase, the pTZ57R/T vector is used for molecular cloning
construction of a constitutive high-level-expression vector for the genus Bifidobacterium to express cholesterol oxidase from Streptomyces coelicola. The promoter region of the 16S rRNA gene is amplified by inverse PCR and used for the construction of pBES16PR. The optimal ribosome-binding site for Bifidobacterium is incorporated in pBES16PR. pBES16PR-CHOL with the structural gene for cholesterol oxidase under the control of the 16S rRNA promoter is used to transform Bifidobacterium longum. The gene is successfully expressed and high level of cholesterol oxidase activity is obtained in Bifidobacterium longum
-
expressed in Escherichia coli BL21(DE3)pLysS cells
expression in Escherichia coli
expression in Escherichia coli strain BL21-CodonPlus (DE3)-RP of the enzyme with and without N- or C-terminal His-tags, the hydrophobicity of the enzyme is reduced by His-tags
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expression in Escherichia coli. Applying the optimized protocol, the production of recombinant cholesterol oxidase is significantly enhanced from 3.2 to 158 U/l. Under the optimized condition, the enzyme is produced on a large-scale
expression of wild-type and mutant enzymes with with His-tags both at the N-terminus and at the C-terminus in Escherichia coli strain BL21 (DE3)
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gene choF, DNA and amino acid sequence determination and analysis, expression in Escherichia coli and Pichia pastoris
gene choM, DNA and amino acid sequence determination and analysis, recombinant expression of N-terminally His-tagged isozyme in Bacillus subtilis strain 168/pMA5 mainly intracellularly
gene choM1, DNA and amino acid sequence determination and analysis, genetic organization, expression of His-tagged isozyme ChoM1 in Escherichia coli strain BL21(DE3), subcloning in Escherichia cli strain DH5alpha, overexpression of isozyme ChoM1 in Mycobacterium neoaurum strain NwIB-01MS
gene choM2, DNA and amino acid sequence determination and analysis, genetic organization, expression of full-length isozyme ChoM2 and of the isozyme without the putative signal peptide sequence in Escherichia coli strain BL21(DE3), subcloning in Escherichia cli strain DH5alpha, overexpression of isozyme ChoM2 in Mycobacterium neoaurum strain NwIB-R10
gene choP, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic tree, subcloning in Escherichia coli strain DH5alpha, recombinant overexpression in Escherichia coli strain Rosetta (DE3) pLysS in inclusion bodies from cells grown at 20°C and 30°C. A soluble and active PA157 enzyme is obtained when the recombinant cells were grown at 10°C
gene HMPREF0204_11499, phylogenetic tree, recombinant expression of N-terminally His-tagged enzyme in Escherichia coli strain JM109. Only when the cultivation temperature is decreased to 16°C immediately after induction, soluble and active protein is present
recombinant expression of His6-tagged enzyme in Escherichia coli train BL21(DE3)
the cholesterol oxidase gene, cloned in the vector pET-28a, is overexpressed in Escherichia coli BL21-CodonPlus
expressed in Escherichia coli BL21(DE3)pLysS cells
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
unfolding and folding after urea treatment of wild-type enzyme and mutant H69A, equilibrium unfolding study, kinetics
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
analysis
biotechnology
diagnostics
drug development
medicine
synthesis
the enzyme is used for the production of steroid drugs and insecticides
agriculture
Streptoverticillum cholesterolicum
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recombinant expression in plants gives insect resistance
agriculture
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recombinant expression in plants gives insect resistance
agriculture
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recombinant expression in plants gives insect resistance
agriculture
recombinant expression in plants gives insect resistance
agriculture
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strain A19249, enzyme exhibits a potent insecticidal activity
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agriculture
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recombinant expression in plants gives insect resistance
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analysis
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platinum electrodes modified with thiolipid/lipid bilayer membranes. Cholesterol oxidase spontaneously inserts into the electrode-supported lipid bilayer membrane from solution and is consequently immobilized to the electrode surface. This electrode architecture may be useful in clinical sensing applications
analysis
-
the cholesterol oxidase-immobilized polyacrylonitrile hollow fiber may have an industrial or medical application for cholesterol determination or oxidation
analysis
-
the enzyme can be used as cholesterol biosensor co-immobilized with cholesterol esterase on oxygen electrodes, determination of total cholesterol in food samples
analysis
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cholesterol esterase (ChEt) and cholesterol oxidase (ChOx) can be immobilized onto tetraethylorthosilicate derived sol-gel films. These tetraethylorthosilicate sol-gel/ChEt/ChOx enzyme films can be used for the estimation of cholesterol oleate up to 780 mg/dl (mM). These TEOS sol-gel enzyme films provide selectivity towards glucose, lactate, uric acid and ascorbic acid
analysis
-
the steady state amperometric measurements of free cholesterol are performed by an enzyme electrode which is developed through electrostatic immobilization of the cholesterol oxidase in poly(vinylferrocenium) perchlorate, PVF+ClO4-, film that is coated on a Pt electrode
analysis
-
simple, reliable, fast and reproducible method to prepare cholesterol oxidase electrodes is described
analysis
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Cellulomonas enzyme is analytically reliable when used for serum cholesterol determination by the endpoint method. Its analytical performance is equivalent to Streptomyces enzymes and meets the analytical goals. It has an advantage over the other enzymes in that it does not ship in the frozen state
analysis
-
the development of an enzyme-based sensor employing the enzyme ChOx has great potential as a simple and economical sensor system, engineering of the enzyme for electrochemical monitoring of cholesterol, overview
biotechnology
Streptoverticillum cholesterolicum
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biocatalysis, industrial steroid drug production, steroid production as diagnostic tool
biotechnology
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biocatalysis, industrial steroid drug production, steroid production as diagnostic tool
biotechnology
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biocatalysis, industrial steroid drug production, steroid production as diagnostic tool
biotechnology
-
biocatalysis, industrial steroid drug production, steroid production as diagnostic tool
biotechnology
-
biocatalysis, industrial steroid drug production, steroid production as diagnostic tool
biotechnology
Nocardia erythropolis
-
biocatalysis, industrial steroid drug production, steroid production as diagnostic tool
biotechnology
-
biocatalysis, industrial steroid drug production, steroid production as diagnostic tool
biotechnology
Nocardia rhodochrous
-
biocatalysis, industrial steroid drug production, steroid production as diagnostic tool
biotechnology
Pseudomonas spp.
-
biocatalysis, industrial steroid drug production, steroid production as diagnostic tool
biotechnology
-
biocatalysis, industrial steroid drug production, steroid production as diagnostic tool
biotechnology
biocatalysis, industrial steroid drug production, steroid production as diagnostic tool
biotechnology
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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
biotechnology
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biocatalysis, industrial steroid drug production, steroid production as diagnostic tool
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diagnostics
-
the enzyme is used for a kinetic cholesterol assay for determination of cholesterol content in human serum, overview, the enzyme from Streptomyces is more effective than the enzyme from Brevibacterium
diagnostics
-
the enzyme is used for a kinetic cholesterol assay for determination of cholesterol content in human serum, overview, the enzyme from Streptomyces is more effective than the enzyme from Brevibacterium
diagnostics
Streptoverticillum cholesterolicum
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analytic tool for determining cholesterol in various samples
diagnostics
-
analytic tool for determining cholesterol in various samples
diagnostics
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analytic tool for determining cholesterol in various samples
diagnostics
Nocardia erythropolis
-
analytic tool for determining cholesterol in various samples
diagnostics
Nocardia rhodochrous
-
analytic tool for determining cholesterol in various samples
diagnostics
-
analytic tool for determining cholesterol in various samples
diagnostics
analytic tool for determining cholesterol in various samples
diagnostics
-
the enzyme is used to determine cholesterol in food and blood serum by coupling of the enzyme with peroxidase
diagnostics
the enzyme is an important biotechnological tool for clinical diagnostics. It is also used for tracking intracellular cholesterol. Its utility is limited by the lack of an efficient temporal control of its activity. A rapamycin-inducible fluorescent cholesterol oxidase from Chromobacterium sp. DS-1 (split GFP-COase) is engineered. Induction by rapamycin allows temporal control over enzyme activity and rapidly leads to an efficient reduction of intracellular cholesterol. It is proposed that this drug-inducible split GFP-COase is a new tool to manipulate the cellular cholesterol content and gain insights into cholesterol-dependent proteins and cholesterol-related cell pathologies
diagnostics
-
determination of cholesterol, by rapid, cheap and reliable methods, is very important in clinical diagnosis because its level in blood is closely related to human health. A reproducible cholesterol biosensors is prepared based on the direct adsorption of ChOx onto gold substrates (ChOx-Au)
diagnostics
-
analytic tool for determining cholesterol in various samples
-
diagnostics
-
the enzyme is used to determine cholesterol in food and blood serum by coupling of the enzyme with peroxidase
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drug development
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the cytotoxicity activity against a few cancer cell lines, while broadly sparing the normal cells, suggests the possible use of this enzyme as a promising future contender for anticancer therapy
drug development
Streptomyces sp. AKHSS
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the enzyme showed significant cytotoxicity on breast (MCF-7), nasopharyngeal (KB) and ovarian (OVCAR) cancer cell lines at very low concentrations ranging from 0.000093 to 0.00014 mM. It exhibits relatively less cytotoxicity on primary mouse embryonic fibroblast (3T3) cells. Thus, cholesterol oxidase from Streptomyces sp. AKHSS could be a potential anticancer agent
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
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
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
medicine
Nocardia rhodochrous
-
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
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
medicine
Nocardia erythropolis
-
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
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
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
medicine
Corynebacterium cholesterolicum
-
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
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
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
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
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
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
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
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
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
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
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
-
EXTERNAL LINKS (specific for EC-Number 1.1.3.6)
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Release 2026.1 (March 2026)
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