Information on EC 1.1.3.6 - cholesterol oxidase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY
1.1.3.6
-
RECOMMENDED NAME
GeneOntology No.
cholesterol oxidase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
cholesterol + O2 = cholest-5-en-3-one + H2O2
show the reaction diagram
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; isomerization is not the rate limiting step
-
cholesterol + O2 = cholest-5-en-3-one + H2O2
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
Rhodococcus sp. GK1, Streptomyces sp. SA-COO
-
-
cholesterol + O2 = cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
oxidation
-
-
oxidation
-
-
-
redox reaction
-
-
radical or hydride transfer mechanism
-
reduction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
cholesterol degradation to androstenedione I (cholesterol oxidase)
-
Steroid degradation
-
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).
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3beta-hydroxy steroid oxidoreductase
-
-
-
-
3beta-hydroxysteroid:oxygen oxidoreductase
-
-
-
-
3beta-hydroxysterol oxidase
-
-
3beta-hydroxysterol oxidase
Mycobacterium sp., Nocardia erythropolis, Nocardia rhodochrous, Pseudomonas spp.
-
-
3beta-hydroxysterol oxidase
-
-
3beta-hydroxysterol oxidase
-
-
3beta-hydroxysterol oxidase
-
-
3beta-hydroxysterol oxidase
-
-
3beta-hydroxysterol oxidase
Streptomyces violascens, Streptoverticillum cholesterolicum, uncultured gamma proteobacterium
-
-
3beta-hydroxysterol oxidase
uncultured gamma proteobacterium Y-134
-
-
-
CHO
H9NJ43, H9NJ52
-
CHO
Streptomyces parvus 13647 J
-
-
-
choBb
Q2I2N2
-
choBb
Brevibacterium sp. CCTCC M201008
Q2I2N2
-
-
CHOD
-
-
-
-
ChoG
C5II17
a class II cholesterol oxidase
ChoG
Rhodococcus sp. CECT3014
C5II17
a class II cholesterol oxidase
-
ChoL
A7LGL0
a fragment of a cholesterol oxidase
ChoL
Streptomyces virginiae IBL-14
A7LGL0
a fragment of a cholesterol oxidase
-
cholesterol oxidase
-
-
cholesterol oxidase
-
-
cholesterol oxidase
Mycobacterium sp., Nocardia erythropolis, Nocardia rhodochrous, Pseudomonas spp., Rhodococcus equi, Schizophyllum commune
-
-
cholesterol oxidase
-
-
cholesterol oxidase
Streptomyces violascens, Streptoverticillum cholesterolicum, uncultured gamma proteobacterium
-
-
cholesterol oxidase
uncultured gamma proteobacterium Y-134
-
-
-
cholesterol oxidase I
-
-
cholesterol oxidase II
-
-
cholesterol-O2 oxidoreductase
-
-
-
-
CHOLOX
B5MGF8
belongs to the type II cholesterol oxidases
ChoM2
H9NJ43, H9NJ52
-
ChOx
Mycobacterium sp., Nocardia erythropolis, Nocardia rhodochrous
-
-
ChOx
-
-
ChOx
Streptomyces violascens, Streptoverticillum cholesterolicum, uncultured gamma proteobacterium
-
-
ChOx
uncultured gamma proteobacterium Y-134
-
-
-
CO1
Bacillus sp. SFF34
-
-
-
COD
-
-
-
COD
Brevibacterium sp. M201008
-
-
-
COD
Streptomyces sp. R-6
-
-
-
oxidase, cholesterol
-
-
-
-
type I ChOx
-
-
CAS REGISTRY NUMBER
COMMENTARY
9028-76-6
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Arthrobacter sp. IM79
-
-
-
Manually annotated by BRENDA team
SFF34
-
-
Manually annotated by BRENDA team
Bacillus sp. SFF34
SFF34
-
-
Manually annotated by BRENDA team
isolated from a soil sample collected from the riverside of the Yellow River in Jinan City, Shandong Province, China
-
-
Manually annotated by BRENDA team
isolated from a soil sample collected from the riverside of the Yellow River in Jinan City, Shandong Province, China
-
-
Manually annotated by BRENDA team
CCTCC M201008
SwissProt
Manually annotated by BRENDA team
Brevibacterium sp. CCTCC M201008
CCTCC M201008
SwissProt
Manually annotated by BRENDA team
Brevibacterium sp. M201008
-
-
-
Manually annotated by BRENDA team
nov. sp. ATCC21387
-
-
Manually annotated by BRENDA team
strain ST-200
-
-
Manually annotated by BRENDA team
Burkholderia cepacia ST-200
-
UniProt
Manually annotated by BRENDA team
Burkholderia cepacia ST-200
strain ST-200
-
-
Manually annotated by BRENDA team
-
Q13UN0
UniProt
Manually annotated by BRENDA team
Corynebacterium cholesterolicum
-
-
-
Manually annotated by BRENDA team
Corynebacterium urealyticum DSM7109
-
UniProt
Manually annotated by BRENDA team
isozyme ChoM1
UniProt
Manually annotated by BRENDA team
isozyme ChoM2; several strains
UniProt
Manually annotated by BRENDA team
probably identical with cholesterol decompositing Mycobacterium cholesterolicum
-
-
Manually annotated by BRENDA team
Nocardia farcinica IFM10152
-
UniProt
Manually annotated by BRENDA team
Nocardia rhodochrous
-
-
-
Manually annotated by BRENDA team
Nocardia rhodochrous
3 forms
-
-
Manually annotated by BRENDA team
Nocardia rhodochrous
renamed as Rhodococcus rhodochrous
-
-
Manually annotated by BRENDA team
strain F2, gene choF
SwissProt
Manually annotated by BRENDA team
Pimelobacter simplex F2
strain F2, gene choF
SwissProt
Manually annotated by BRENDA team
ST-200
-
-
Manually annotated by BRENDA team
Pseudomonas sp. COX629
-
-
-
Manually annotated by BRENDA team
Pseudomonas sp. ST-200
ST-200
-
-
Manually annotated by BRENDA team
Pseudomonas spp.
-
-
-
Manually annotated by BRENDA team
high levels of ChOx activity, significant similarities to putative ChOxs encoded by Mycobacterium tuberculosis and Mycobacterium leprae
-
-
Manually annotated by BRENDA team
Rhodococcus equi ATCC33706
-
UniProt
Manually annotated by BRENDA team
ATCC 25544, de novo enzyme synthesis is induced by cholesterol
-
-
Manually annotated by BRENDA team
solated from soil
-
-
Manually annotated by BRENDA team
Rhodococcus sp. CECT3014
-
UniProt
Manually annotated by BRENDA team
Rhodococcus sp. GK1
solated from soil
-
-
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
from soil sample collected from effluent sediment of a steel plant in Barabanki (Uttar Pradesh, India)
-
-
Manually annotated by BRENDA team
Streptomyces parvus 13647 J
from soil sample collected from effluent sediment of a steel plant in Barabanki (Uttar Pradesh, India)
-
-
Manually annotated by BRENDA team
strain A19249
-
-
Manually annotated by BRENDA team
strain SA-COO
-
-
Manually annotated by BRENDA team
Streptomyces sp. A19249
strain A19249
-
-
Manually annotated by BRENDA team
Streptomyces sp. R-6
-
-
-
Manually annotated by BRENDA team
strain SA-COO
-
-
Manually annotated by BRENDA team
Streptomyces virginiae IBL-14
-
UniProt
Manually annotated by BRENDA team
Streptoverticillium cholesterolieum
-
-
-
Manually annotated by BRENDA team
Streptoverticillum cholesterolicum
-
-
-
Manually annotated by BRENDA team
uncultured gamma proteobacterium Y-134
-
-
-
Manually annotated by BRENDA team
uncultured gamma proteobacterium Y-134
Y-134
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
C5II17, -
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
H9NJ43, H9NJ52
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; 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
Rhodococcus sp. CECT3014
-
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
Q9EW96
PimE is a key enzyme in the biosynthesis of the polyene macrolide pimaricin
metabolism
H9NJ43, H9NJ52
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; 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
physiological function
Q57307
ChoD plays a significant role in the pathogenesis of Mycobacterium tuberculosis
physiological function
H9NJ43, H9NJ52
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; 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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,4-androstadiene-3,17-dione + H2O
?
show the reaction diagram
-
11% of the activity with cholesterol, enzyme CO1
-
-
?
1-propanol + O2
propanal + H2O2
show the reaction diagram
-
-
-
?
17beta-hydroxymethyl-5-androsten-3beta-ol + O2
17beta-hydroxymethyl-5-androsten-3-one + H2O2
show the reaction diagram
Nocardia erythropolis
-
-
-
?
20,22-dihydroxycholesterol + O2
20,22-dihydroxycholest-5-en-3-one + H2O2
show the reaction diagram
Nocardia erythropolis
-
-
-
?
20,25-diazacholesterol + O2
20,25-diazacholest-4-en-3-one + H2O2
show the reaction diagram
Nocardia erythropolis
-
-
-
?
20-hydroxycholesterol + O2
20-hydroxycholest-5-en-3-one + H2O2
show the reaction diagram
Nocardia erythropolis
-
-
-
?
22-hydroxycholesterol + O2
22-hydroxycholest-5-en-3-one + H2O2
show the reaction diagram
Nocardia erythropolis
-
-
-
?
23,24-dinor-5-cholen-3beta,22-diol + O2
23,24-dinor-5-cholen-22-ol-3-one + H2O2
show the reaction diagram
Nocardia erythropolis
-
-
-
?
24-hydroxycholesterol + O2
24-hydroxycholest-5-en-3-one + H2O2
show the reaction diagram
Nocardia erythropolis
-
-
-
?
24-oxocholesterol + O2
24-oxocholest-5-en-3-one + H2O2
show the reaction diagram
Nocardia erythropolis
-
-
-
?
25-hydroxy-27-norcholesterol + O2
?
show the reaction diagram
Nocardia erythropolis
-
-
-
-
?
25-hydroxycholesterol + O2
25-hydroxycholest-5-en-3-one + H2O2
show the reaction diagram
Nocardia erythropolis
-
-
-
?
26-hydroxycholesterol + O2
26-hydroxycholest-5-en-3-one + H2O2
show the reaction diagram
Nocardia erythropolis
-
-
-
-
-
26-hydroxycholesterol + O2
26-hydroxycholest-5-en-3-one + H2O2
show the reaction diagram
Nocardia erythropolis
-
-
-
?
3beta-chlorocholest-5-ene + O2
? + H2O2
show the reaction diagram
H9NJ43, H9NJ52
-
-
-
?
3beta-chlorocholest-5-ene + O2
? + H2O2
show the reaction diagram
H9NJ43, H9NJ52
low activity
-
-
?
3beta-hydroxyandrost-5-en-17-one + O2
androst-5-en-3,17-dione + H2O2
show the reaction diagram
Streptomyces parvus, Streptomyces parvus 13647 J
-
30% of the activity with cholesterol
-
-
?
3beta-hydroxypregn-5-en-20-one + O2
pregn-5-en-3,20-dione + H2O2
show the reaction diagram
Streptomyces parvus, Streptomyces parvus 13647 J
-
42% of the activity with cholesterol
-
-
?
4,4-dimethylcholesterol + O2
4,4-dimethylcholest-5-en-3-one
show the reaction diagram
Nocardia erythropolis
-
-
-
?
4alpha-methylcholesterol + O2
4alpha-methylcholest-5-en-3-one + H2O2
show the reaction diagram
Nocardia erythropolis
-
-
-
?
4beta-methylcholesterol + O2
4beta-methylcholest-5-en-3-one + H2O2
show the reaction diagram
Nocardia erythropolis
-
-
-
?
5,7-cholestadien-3beta-ol + O2
5,7-cholestadien-3-one + H2O2
show the reaction diagram
Nocardia erythropolis
-
-
-
?
5-androstene-3beta,17beta-diol + O2
5-androsten-17beta-ol-3-one + H2O2
show the reaction diagram
Nocardia erythropolis
-
-
-
?
5-cholene-3beta,24-diol + O2
5-cholen-24-ol-3-one + H2O2
show the reaction diagram
Nocardia erythropolis
-
-
-
?
5-pregnen-3beta,20beta-diol + O2
5-pregnen-20beta-ol-3-one + H2O2
show the reaction diagram
Nocardia erythropolis
-
-
-
?
5alpha-androstan-3-ol-17-one + O2
5alpha-androstan-3,17-dione + H2O2
show the reaction diagram
-
15% of the activity with cholesterol
-
-
?
5alpha-cholest-8(14)-en-3beta-ol + O2
5alpha-cholest-8(14)-en-3-one + H2O2
show the reaction diagram
Nocardia erythropolis
-
-
-
?
5alpha-cholestan-3beta-ol + O2
5alpha-cholestan-3-one + H2O2
show the reaction diagram
-
-
-
?
5alpha-cholestan-3beta-ol + O2
5alpha-cholestan-3-one + H2O2
show the reaction diagram
Nocardia erythropolis
-
-
-
?
5alpha-cholestan-3beta-ol + O2
5alpha-cholestan-3-one + H2O2
show the reaction diagram
-
-
-
?
5alpha-cholestan-3beta-ol + O2
5alpha-cholestan-3-one + H2O2
show the reaction diagram
Nocardia erythropolis
-
87% of activity
-
?
5alpha-cholestan-3beta-ol + O2
5alpha-cholestan-3-one + H2O2
show the reaction diagram
-
13.2% of activity with cholesterol
-
-
-
5alpha-cholestan-3beta-ol + O2
5alpha-cholestan-3-one + H2O2
show the reaction diagram
Streptomyces parvus, Streptomyces parvus 13647 J
-
equally active as cholesterol
-
-
?
5alpha-cholestane + O2
?
show the reaction diagram
-
72% of the activity with cholesterol, enzyme CO1, 90% of the activity with cholesterol, enzyme CO2
-
-
?
5alpha-cholestane-3beta-ol-7-one + O2
5alpha-cholestane-3,7,dione
show the reaction diagram
-
74% of the activity with cholesterol, enzyme CO1, 84% of the activity with cholesterol, enzyme CO2
-
-
?
7-dehydrocholesterol + O2
cholest-4,7-dien-3-one + H2O2
show the reaction diagram
-
14% of the activity with cholesterol
-
-
?
7-dehydrocholesterol + O2
cholest-4,7-dien-3-one + H2O2
show the reaction diagram
-
26% of the activity with cholesterol
-
-
?
7-keto-cholesterol + O2
?
show the reaction diagram
-
-
-
-
?
7alpha-hydroxy-cholesterol + O2
7alpha-hydroxy-cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
-
?
7beta-hydroxy-cholesterol + O2
7beta-hydroxy-cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
-
?
7E,22-ergostadien-3beta-ol + O2
7E,22-ergostadien-3-one + H2O2
show the reaction diagram
-
-
-
?
andost-4-ene-3,17-dione + O2
? + H2O2
show the reaction diagram
H9NJ43, H9NJ52
-
-
-
?
beta-cholestanol + O2
?
show the reaction diagram
-
95% of the activity with cholesterol
-
-
?
beta-cholestanol + O2
?
show the reaction diagram
-
101% activity compared to cholesterol
-
-
?
beta-cholestanol + O2
?
show the reaction diagram
-
13% activity compared to cholesterol
-
-
?
beta-cholestanol + O2
?
show the reaction diagram
Q93RE1
69% activity compared to cholesterol
-
-
?
beta-cholestanol + O2
?
show the reaction diagram
Q55020
75% activity compared to cholesterol
-
-
?
beta-cholestanol + O2
?
show the reaction diagram
-
78% activity compared to cholesterol
-
-
?
beta-cholestanol + O2
?
show the reaction diagram
-
79% activity compared to cholesterol
-
-
?
beta-cholestanol + O2
?
show the reaction diagram
B5MGF8
95% activity compared to cholesterol
-
-
?
beta-cholestanol + O2
?
show the reaction diagram
Streptoverticillium cholesterolieum
-
96% activity compared to cholesterol
-
-
?
beta-cholestanol + O2
?
show the reaction diagram
Pseudomonas sp. COX629
-
78% activity compared to cholesterol
-
-
?
beta-cholestanol + O2
?
show the reaction diagram
uncultured gamma proteobacterium Y-134
-
79% activity compared to cholesterol
-
-
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
show the reaction diagram
Nocardia erythropolis
-
-
-
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
show the reaction diagram
-
19.7% of activity with cholesterol
-
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
show the reaction diagram
-
19% of the activity with cholesterol
-
-
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
show the reaction diagram
-
29% of the activity with cholesterol
-
-
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
show the reaction diagram
-
57% of the activity with cholesterol, enzyme CO1, 79% of the activity with cholesterol, enzyme CO2
-
-
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
show the reaction diagram
-
about 30% of the activity with cholesterol, cholesterol oxidase I
-
-
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
show the reaction diagram
-
20% activity compared to cholesterol
-
-
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
show the reaction diagram
-
29% activity compared to cholesterol
-
-
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
show the reaction diagram
Streptoverticillium cholesterolieum
-
39% activity compared to cholesterol
-
-
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
show the reaction diagram
Corynebacterium cholesterolicum
-
50% activity compared to cholesterol
-
-
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
show the reaction diagram
-
64% activity compared to cholesterol
-
-
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
show the reaction diagram
Q157H4
64% activity compared to cholesterol
-
-
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
show the reaction diagram
Q55020
72% activity compared to cholesterol
-
-
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
show the reaction diagram
B5MGF8
80% activity compared to cholesterol
-
-
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
show the reaction diagram
Burkholderia cepacia, Burkholderia cepacia ST-200
Q93RE1
84% activity compared to cholesterol
-
-
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
show the reaction diagram
-
72% activity compared to cholesterol
-
-
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
show the reaction diagram
Q157H4
64% activity compared to cholesterol
-
-
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
show the reaction diagram
Bacillus sp. SFF34
-
57% of the activity with cholesterol, enzyme CO1, 79% of the activity with cholesterol, enzyme CO2
-
-
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
show the reaction diagram
uncultured gamma proteobacterium Y-134
-
29% activity compared to cholesterol
-
-
?
beta-sitosterol + O2
?
show the reaction diagram
-
about 55% of the activity with cholesterol, cholesterol oxidase II
-
-
?
beta-sitosterol + O2
?
show the reaction diagram
-
80% of the activity with cholesterol
-
-
?
beta-sitosterol + O2
?
show the reaction diagram
uncultured gamma proteobacterium Y-134
-
-
-
-
?
beta-sitosterol + O2
? + H2O2
show the reaction diagram
H9NJ43, H9NJ52
-
-
-
?
beta-stigmasterol + O2
?
show the reaction diagram
-
36% of the activity with cholesterol
-
-
?
beta-stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
show the reaction diagram
-
10% activity compared to cholesterol
-
-
?
beta-stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
show the reaction diagram
Corynebacterium cholesterolicum
-
12% activity compared to cholesterol
-
-
?
beta-stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
show the reaction diagram
Streptoverticillium cholesterolieum
-
17% activity compared to cholesterol
-
-
?
beta-stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
show the reaction diagram
-
32% activity compared to cholesterol
-
-
?
beta-stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
show the reaction diagram
B5MGF8
36% activity compared to cholesterol
-
-
?
beta-stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
show the reaction diagram
Q55020
37% activity compared to cholesterol
-
-
?
beta-stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
show the reaction diagram
-
40% activity compared to cholesterol
-
-
?
beta-stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
show the reaction diagram
-
47% activity compared to cholesterol
-
-
?
beta-stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
show the reaction diagram
-
50% activity compared to cholesterol
-
-
?
beta-stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
show the reaction diagram
Q93RE1
59% activity compared to cholesterol
-
-
?
beta-stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
show the reaction diagram
Q157H4
33% activity compared to cholesterol
-
-
?
beta-stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
show the reaction diagram
Pseudomonas sp. COX629
-
40% activity compared to cholesterol
-
-
?
beta-stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
show the reaction diagram
uncultured gamma proteobacterium Y-134
-
32% activity compared to cholesterol
-
-
?
campesterol + O2
(24R)-ergost-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
campesterol + O2
(24R)-ergost-5-en-3-one + H2O2
show the reaction diagram
Nocardia erythropolis
-
67% of activity with cholesterol
-
?
cholest-4-en-3-one + O2
? + H2O2
show the reaction diagram
H9NJ43, H9NJ52
-
-
-
?
cholest-5-en-3beta-ol 7-one + O2
cholest-5-en-3,17-dione + H2O2
show the reaction diagram
-
low activity with wild-type and mutant enzymes L119A, L119F, V145Q, P357N, Q286R and S379T
-
-
?
cholestanol + O2
?
show the reaction diagram
-
-
-
-
?
cholestanol + O2
?
show the reaction diagram
-
-
-
-
-
cholestanol + O2
?
show the reaction diagram
-
-
-
-
?
cholestanol + O2
?
show the reaction diagram
-
-
-
-
-
cholestanol + O2
?
show the reaction diagram
-
-
-
-
?
cholestanol + O2
?
show the reaction diagram
-
-
-
-
?
cholestenone + O2
?
show the reaction diagram
C5II17, -
-
-
-
?
cholestenone + O2
?
show the reaction diagram
Rhodococcus sp. CECT3014
C5II17
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
-
ir
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Q56DL0
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
P12676
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Nocardia rhodochrous
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Nocardia rhodochrous
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Nocardia rhodochrous
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Nocardia rhodochrous
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Nocardia rhodochrous
-
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Nocardia erythropolis
-
-
-
-
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Nocardia erythropolis
-
-
-
-
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Nocardia erythropolis
-
-
-
-
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Nocardia erythropolis
-
-
-
-
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Nocardia erythropolis
-
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Pseudomonas spp.
-
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
P22637
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Corynebacterium cholesterolicum
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Corynebacterium cholesterolicum
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Q56DL0
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Streptoverticillum cholesterolicum
-
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Q93JS8
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Q93H76
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
A7RA76
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Q9EW96
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Q55020
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
B1VGH1
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Q5YRJ2
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Q59530
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Q57307
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Q9L0H6
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
A9QAE7
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Q2T0X3
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Q13UN0
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
A7LGL0
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Nocardia erythropolis
-
-
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
show the reaction diagram
C5II17, -
highest activity
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Nocardia erythropolis
-
overview: substrate specificity
-
-
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Nocardia erythropolis
-
overview: substrate specificity
-
-
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
overview: substrate specificity
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Nocardia erythropolis
-
relatively unreactive 17keto-DELTA5-3beta-hydroxysteroids are converted to satisfactory substrates by formation of isopentyloximes or benzyloximes, size and shape of steroid 17beta-side-chain and oxygenation of nucleus
-
-
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
specific for steroid substrates with an OH group in position 3, preference for steroids with at least a C2 chain at position C17
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
enzyme specifically oxidizes 3beta-hydroxy groups in steroids
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Nocardia erythropolis
-
enzyme specifically oxidizes 3beta-hydroxy groups in steroids
-
-
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
100% activity
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Q55020
100% activity
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Q93RE1
100% activity
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
B5MGF8
100% activity
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Streptoverticillium cholesterolieum
-
100% activity
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Q157H4
100% activity
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
100% activity
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
cholesterol oxidase is required for the biosynthesis of the antifungal polyene pimaricin
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
cholesterol oxidase is required for the biosynthesis of the antifungal polyene pimaricin, apparently acting as an antifungal sensor
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Burkholderia cepacia ST-200
-
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Burkholderia cepacia ST-200
Q93RE1
100% activity
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
P12676
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
100% activity
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Q157H4
100% activity
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Rhodococcus sp. CECT3014
C5II17
highest activity
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Pseudomonas sp. COX629
-
100% activity
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Brevibacterium sp. M201008
-
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Bacillus sp. SFF34
-
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Pimelobacter simplex F2
Q56DL0
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
uncultured gamma proteobacterium Y-134
-
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
uncultured gamma proteobacterium Y-134
-
100% activity
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Rhodococcus sp. GK1
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Corynebacterium urealyticum DSM7109
B1VGH1
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Nocardia farcinica IFM10152
Q5YRJ2
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Streptomyces sp. A19249
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Pseudomonas sp. ST-200
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Streptomyces sp. R-6
-
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Streptomyces parvus 13647 J
-
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Arthrobacter sp. IM79
-
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Q56DL0
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Rhodococcus equi ATCC33706
Q93JS8
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Streptomyces virginiae IBL-14
A7LGL0
-
-
-
?
cholesterol + O2
6beta-hydroperoxycholest-4-en-3-one + H2O2
show the reaction diagram
Burkholderia cepacia, Burkholderia cepacia ST-200
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
P12676
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
Nocardia rhodochrous
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
Nocardia rhodochrous
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
Nocardia rhodochrous
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
Nocardia erythropolis
-
-
-
-
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
Nocardia erythropolis
-
-
-
-
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
Nocardia erythropolis
-
-
-
-
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
Nocardia erythropolis
-
-
-
-
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
Nocardia erythropolis
-
-
-
-
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
Nocardia erythropolis
-
-
-
-
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
Nocardia erythropolis
-
-
-
r
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
Corynebacterium cholesterolicum
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
Corynebacterium cholesterolicum
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
H9NJ43, H9NJ52
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
subsequent isomerization to cholest-4-en-3-one
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
Nocardia rhodochrous
-
first step in cholesterol degradation
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
Nocardia erythropolis
-
first step in cholesterol degradation
-
-
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
first step in cholesterol degradation
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
assay with phenazine sulfate and dichlorophenylindophenol as electron acceptors
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
Burkholderia cepacia ST-200
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
Rhodococcus sp. GK1
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
Streptomyces sp. A19249
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
Pseudomonas sp. ST-200
-
-
-
?
cholesterol-5alpha,6beta-epoxide + O2
?
show the reaction diagram
-
10% of the activity with cholesterol, enzyme CO2, 9% of the activity with cholesterol, enzyme CO1
-
-
?
coprostane + O2
?
show the reaction diagram
-
63% of the activity with cholesterol, enzyme CO1, 67% of the activity with cholesterol, enzyme CO2
-
-
?
cyclohexanol + O2
cyclohexanal + H2O2
show the reaction diagram
-
-
-
?
dehydro-epi-androsterone + O2
?
show the reaction diagram
-
about 35% of the activity with cholesterol, cholesterol oxidase I, about 5% of the activity with cholesterol, cholesterol oxidase II
-
-
?
dehydroandrosterone + O2
? + H2O2
show the reaction diagram
H9NJ43, H9NJ52
-
-
-
?
dehydroepiandrosterone + O2
androst-5-en-3,17-dione + H2O2
show the reaction diagram
Nocardia erythropolis
-
-
-
r
dehydroepiandrosterone + O2
androst-5-en-3,17-dione + H2O2
show the reaction diagram
-
-
-
-
dehydroepiandrosterone + O2
androst-5-en-3,17-dione + H2O2
show the reaction diagram
-
-
-
-
dehydroepiandrosterone + O2
androst-5-en-3,17-dione + H2O2
show the reaction diagram
-
-
-
-
dehydroepiandrosterone + O2
androst-5-en-3,17-dione + H2O2
show the reaction diagram
-
41.4% of the activity with cholesterol
-
-
dehydroepiandrosterone + O2
androst-5-en-3,17-dione + H2O2
show the reaction diagram
Q93RE1
16% activity compared to cholesterol
-
-
?
dehydroepiandrosterone + O2
androst-5-en-3,17-dione + H2O2
show the reaction diagram
Q55020
24% activity compared to cholesterol
-
-
?
dehydroepiandrosterone + O2
androst-5-en-3,17-dione + H2O2
show the reaction diagram
B5MGF8
27% activity compared to cholesterol
-
-
?
dehydroepiandrosterone + O2
androst-5-en-3,17-dione + H2O2
show the reaction diagram
-
28% activity compared to cholesterol
-
-
?
dehydroepiandrosterone + O2
androst-5-en-3,17-dione + H2O2
show the reaction diagram
-
37% activity compared to cholesterol
-
-
?
dehydroepiandrosterone + O2
androst-5-en-3,17-dione + H2O2
show the reaction diagram
-
41% activity compared to cholesterol
-
-
?
dehydroepiandrosterone + O2
androst-5-en-3,17-dione + H2O2
show the reaction diagram
Streptoverticillium cholesterolieum
-
48% activity compared to cholesterol
-
-
?
dehydroepiandrosterone + O2
androst-5-en-3,17-dione + H2O2
show the reaction diagram
Corynebacterium cholesterolicum
-
5% activity compared to cholesterol
-
-
?
dehydroepiandrosterone + O2
androst-5-en-3,17-dione + H2O2
show the reaction diagram
Burkholderia cepacia ST-200
Q93RE1
16% activity compared to cholesterol
-
-
?
dehydroepiandrosterone + O2
androst-5-en-3,17-dione + H2O2
show the reaction diagram
-
24% activity compared to cholesterol
-
-
?
dehydroepiandrosterone + O2
?
show the reaction diagram
-
27% of the activity with cholesterol
-
-
?
dehydroepiandrosterone + O2
androst-5-en-3,17-dione + H2O
show the reaction diagram
Streptomyces virginiae, Streptomyces virginiae IBL-14
A7LGL0
-
-
-
?
dehydroisoandrosterone + O2
androst-5-en-3,17-dione + H2O
show the reaction diagram
P12676
-
-
-
-
dehydroisoandrosterone + O2
androst-5-en-3,17-dione + H2O
show the reaction diagram
-
low activity with wild-type and mutant enzymes L119A, L119F, V145Q, P357N, Q286R and S379T
-
-
?
desmosterol + O2
cholesta-5,24-dien-3-one + H2O2
show the reaction diagram
-
-
-
?
desmosterol + O2
cholesta-5,24-dien-3-one + H2O2
show the reaction diagram
Nocardia erythropolis
-
98% of activity with cholesteol
-
?
dihydrocholesterol + O2
5alpha-cholestan-3-one + H2O2
show the reaction diagram
-
-
-
?
dihydrocholesterol + O2
5alpha-cholestan-3-one + H2O2
show the reaction diagram
-
-
-
-
?
dihydrocholesterol + O2
5alpha-cholestan-3-one + H2O2
show the reaction diagram
-
22% of the activity with cholesterol
-
-
?
dihydrocholesterol + O2
5alpha-cholestan-3-one + H2O2
show the reaction diagram
-
58% of the activity with cholesterol, enzyme CO1, 70% of the activity with cholesterol, enzyme CO2
-
-
?
dihydrocholesterol + O2
5alpha-cholestan-3-one + H2O2
show the reaction diagram
-
79% of the activity with cholesterol
-
-
?
diosgenin + O2
diosgenone + H2O2
show the reaction diagram
Streptomyces virginiae, Streptomyces virginiae IBL-14
A7LGL0
i.e. (25R)-spirost-5-en-3beta-ol
-
-
?
diosgenin + O2
? + H2O2
show the reaction diagram
H9NJ43, H9NJ52
-
-
-
?
epiandosterone + O2
?
show the reaction diagram
-
1% activity compared to cholesterol
-
-
?
epiandosterone + O2
?
show the reaction diagram
Q93RE1
10% activity compared to cholesterol
-
-
?
epiandosterone + O2
?
show the reaction diagram
B5MGF8
15% activity compared to cholesterol
-
-
?
epiandrosterone + O2
?
show the reaction diagram
-
-
-
-
-
epiandrosterone + O2
?
show the reaction diagram
-
15% of the activity with cholesterol
-
-
?
ergosta-5,7,22-trien-3beta-ol + O2
ergostan-5,7,22-trien-3-one + H2O2
show the reaction diagram
-
18% of the activity with cholesterol
-
-
?
ergosterol + O2
dehydroergosterol + H2O2
show the reaction diagram
-
-
-
?
ergosterol + O2
dehydroergosterol + H2O2
show the reaction diagram
-
-
-
?
ergosterol + O2
dehydroergosterol + H2O2
show the reaction diagram
-
low activity
-
?
ergosterol + O2
dehydroergosterol + H2O2
show the reaction diagram
-
no substrate
-
-
-
ergosterol + O2
dehydroergosterol + H2O2
show the reaction diagram
Q55020
12% activity compared to cholesterol
-
-
?
ergosterol + O2
dehydroergosterol + H2O2
show the reaction diagram
B5MGF8
12% activity compared to cholesterol
-
-
?
ergosterol + O2
dehydroergosterol + H2O2
show the reaction diagram
-
14% activity compared to cholesterol
-
-
?
ergosterol + O2
dehydroergosterol + H2O2
show the reaction diagram
-
17% activity compared to cholesterol
-
-
?
ergosterol + O2
dehydroergosterol + H2O2
show the reaction diagram
Q93RE1
20% activity compared to cholesterol
-
-
?
ergosterol + O2
dehydroergosterol + H2O2
show the reaction diagram
Corynebacterium cholesterolicum
-
4% activity compared to cholesterol
-
-
?
ergosterol + O2
dehydroergosterol + H2O2
show the reaction diagram
Streptoverticillium cholesterolieum
-
5% activity compared to cholesterol
-
-
?
ergosterol + O2
dehydroergosterol + H2O2
show the reaction diagram
-
51% activity compared to cholesterol
-
-
?
ergosterol + O2
dehydroergosterol + H2O2
show the reaction diagram
Burkholderia cepacia ST-200
Q93RE1
20% activity compared to cholesterol
-
-
?
ergosterol + O2
dehydroergosterol + H2O2
show the reaction diagram
-
12% activity compared to cholesterol
-
-
?
ergosterol + O2
dehydroergosterol + H2O2
show the reaction diagram
Pseudomonas sp. COX629
-
51% activity compared to cholesterol
-
-
?
ergosterol + O2
?
show the reaction diagram
-
22% of the activity with cholesterol
-
-
?
ergosterol + O2
?
show the reaction diagram
-
12% of the activity with cholesterol
-
-
?
ergosterol + O2
?
show the reaction diagram
uncultured gamma proteobacterium Y-134
-
-
-
-
?
estrone + O2
estra-1,5(10)-dien-3,17-dione + H2O2
show the reaction diagram
-
low activity with wild-type enzyme, no activity with mutant enzymes L119A, L119F, V145Q, P357N, Q286R and S379T
-
-
?
ethanol + O2
ethanal + H2O2
show the reaction diagram
-
-
-
?
fucosterol + O2
stigmasta-5,24(28)-dien-3-one + H2O2
show the reaction diagram
-
-
-
?
fucosterol + O2
stigmasta-5,24(28)-dien-3-one + H2O2
show the reaction diagram
Nocardia erythropolis
-
-
-
-
-
hecogenin + O2
5alpha-(25R)-spirostan-3,12-dione + H2O2
show the reaction diagram
-
66% of the activity with cholesterol, enzyme CO1, 80% of the activity with cholesterol, enzyme CO2
-
-
?
lanosterol + O2
lanosta-8,24-dien-3-one + H2O2
show the reaction diagram
-
no substrate
-
-
-
lanosterol + O2
lanosta-8,24-dien-3-one + H2O2
show the reaction diagram
-
slow rate
-
?
lanosterol + O2
5alpha-lanosta-8,24-dien-3-one
show the reaction diagram
-
4% of the activity with cholesterol, enzyme CO1, 5% of the activity with cholesterol, enzyme CO2
-
-
?
pregnenolone + O2
5-pregnen-3,20-dione + H2O2
show the reaction diagram
-
-
-
-
?
pregnenolone + O2
5-pregnen-3,20-dione + H2O2
show the reaction diagram
Nocardia erythropolis
-
-
-
r
pregnenolone + O2
5-pregnen-3,20-dione + H2O2
show the reaction diagram
-
-
-
-
pregnenolone + O2
5-pregnen-3,20-dione + H2O2
show the reaction diagram
-
-
-
-
pregnenolone + O2
5-pregnen-3,20-dione + H2O2
show the reaction diagram
-
-
-
-
pregnenolone + O2
5-pregnen-3,20-dione + H2O2
show the reaction diagram
-
22.4% of activity with chelesterol
-
-
pregnenolone + O2
5-pregnen-3,20-dione + H2O2
show the reaction diagram
-
20% activity compared to cholesterol
-
-
?
pregnenolone + O2
5-pregnen-3,20-dione + H2O2
show the reaction diagram
-
22% activity compared to cholesterol
-
-
?
pregnenolone + O2
5-pregnen-3,20-dione + H2O2
show the reaction diagram
Q93RE1
32% activity compared to cholesterol
-
-
?
pregnenolone + O2
5-pregnen-3,20-dione + H2O2
show the reaction diagram
Streptoverticillium cholesterolieum
-
37% activity compared to cholesterol
-
-
?
pregnenolone + O2
5-pregnen-3,20-dione + H2O2
show the reaction diagram
Corynebacterium cholesterolicum
-
38% activity compared to cholesterol
-
-
?
pregnenolone + O2
5-pregnen-3,20-dione + H2O2
show the reaction diagram
-
42% activity compared to cholesterol
-
-
?
pregnenolone + O2
5-pregnen-3,20-dione + H2O2
show the reaction diagram
-
6% activity compared to cholesterol
-
-
?
pregnenolone + O2
5-pregnen-3,20-dione + H2O2
show the reaction diagram
B5MGF8
95% activity compared to cholesterol
-
-
?
pregnenolone + O2
5-pregnen-3,20-dione + H2O2
show the reaction diagram
Q55020
99% activity compared to cholesterol
-
-
?
pregnenolone + O2
5-pregnen-3,20-dione + H2O2
show the reaction diagram
Burkholderia cepacia ST-200
Q93RE1
32% activity compared to cholesterol
-
-
?
pregnenolone + O2
5-pregnen-3,20-dione + H2O2
show the reaction diagram
-
99% activity compared to cholesterol
-
-
?
pregnenolone + O2
?
show the reaction diagram
-
-
-
-
?
pregnenolone + O2
?
show the reaction diagram
-
-
-
-
-
pregnenolone + O2
?
show the reaction diagram
-
about 60% of the activity with cholesterol, cholesterol oxidase I, about 60% of the activity with cholesterol, cholesterol oxidase II
-
-
?
pregnenolone + O2
?
show the reaction diagram
-
95% of the activity with cholesterol
-
-
?
pregnenolone + O2
?
show the reaction diagram
uncultured gamma proteobacterium Y-134
-
-
-
-
?
pregnenolone + O2
? + H2O2
show the reaction diagram
H9NJ43, H9NJ52
-
-
-
?
sigmast-5-en-3beta-ol + O2
stigmast-5-en-3-one + H2O2
show the reaction diagram
-
68% of the activity with cholesterol
-
-
?
sitost-5-en-3beta-ol + O2
sitost-5-en-3-one + H2O2
show the reaction diagram
-
88% of the activity with cholesterol
-
-
?
sitosterol + O2
?
show the reaction diagram
Streptomyces virginiae, Streptomyces virginiae IBL-14
A7LGL0
-
-
-
?
stigmastanol + O2
stigmastanone + H2O2
show the reaction diagram
-
-
-
?
stigmastanol + O2
stigmasta-5,22t-dien-3-one + H2O2
show the reaction diagram
-
15% of the activity with cholesterol
-
-
?
stigmastanol + O2
stigmasta-5,22t-dien-3-one + H2O2
show the reaction diagram
-
7% of the activity with cholesterol
-
-
?
stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
show the reaction diagram
-
-
-
?
stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
show the reaction diagram
-
-
-
?
stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
show the reaction diagram
Nocardia erythropolis
-
-
-
?
stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
show the reaction diagram
-
-
-
?
stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
show the reaction diagram
-
-
-
?
stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
show the reaction diagram
-
10% of activity with cholesterol
-
-
?
stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
show the reaction diagram
-
102% of the activity with cholesterol, enzyme CO2
-
-
?
stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
show the reaction diagram
-
15% of the activity with cholesterol
-
-
?
stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
show the reaction diagram
-
32% of the activity with cholesterol
-
-
?
stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
show the reaction diagram
-
86% of the activity with cholesterol, enzyme CO1
-
-
?
stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
show the reaction diagram
-
about 10% of the activity with cholesterol, cholesterol oxidase I, about 10% of the activity with cholesterol, cholesterol oxidase II
-
-
?
stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
show the reaction diagram
Bacillus sp. SFF34
-
102% of the activity with cholesterol, enzyme CO2, 86% of the activity with cholesterol, enzyme CO1
-
-
?
trans-androsterone + O2
?
show the reaction diagram
-
-
-
-
?
trans-dehydroandrosterone + O2
?
show the reaction diagram
-
-
-
-
?
methanol + O2
methanal + H2O2
show the reaction diagram
-
-
-
?
additional information
?
-
-
no activity with dehydroepiandrosterone
-
-
-
additional information
?
-
-
less than 3% of the activity with cholesterol: ergosterol and epiandrosterone. No activity: dehydroepiandrosterone, pregnenolone
-
-
-
additional information
?
-
-
no activity with: ergosterol, dehydroepiandrosterone, epiandrosterone, pregnenolone
-
-
-
additional information
?
-
-
cholesterol oxidase is involved in pimaricin biosynthesis
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
no activity with epicholesterol
-
-
-
additional information
?
-
-
no activity with ergosterol
-
-
-
additional information
?
-
-
no activity with ergosterol, pregnenolone, dehydroepiandrosterone, and epiandosterone
-
-
-
additional information
?
-
A9QAE7
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
-
-
-
additional information
?
-
Q157H4
no activity with cholic acid, progesterone and 4-androsten-3,17-dione
-
-
-
additional information
?
-
C5II17, -
the enzyme does not use glycerol as substrate
-
-
-
additional information
?
-
-
no activity with cholest-5-en-3alpha-ol
-
-
-
additional information
?
-
-
the wild-type enzyme also shows cholesterol dehydrogenase activity with 0.001 U/mg
-
-
-
additional information
?
-
Q157H4
no activity with cholic acid, progesterone and 4-androsten-3,17-dione
-
-
-
additional information
?
-
Rhodococcus sp. CECT3014
C5II17
the enzyme does not use glycerol as substrate
-
-
-
additional information
?
-
Pseudomonas sp. COX629
-
no activity with dehydroepiandrosterone
-
-
-
additional information
?
-
uncultured gamma proteobacterium Y-134
-
no activity with ergosterol, pregnenolone, dehydroepiandrosterone, and epiandosterone
-
-
-
additional information
?
-
Streptomyces parvus 13647 J
-
no activity with cholest-5-en-3alpha-ol
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3beta-chlorocholest-5-ene + O2
? + H2O2
show the reaction diagram
H9NJ43, H9NJ52
low activity
-
-
?
andost-4-ene-3,17-dione + O2
? + H2O2
show the reaction diagram
H9NJ43, H9NJ52
-
-
-
?
beta-cholestanol + O2
?
show the reaction diagram
-
101% activity compared to cholesterol
-
-
?
beta-cholestanol + O2
?
show the reaction diagram
-
13% activity compared to cholesterol
-
-
?
beta-cholestanol + O2
?
show the reaction diagram
Q93RE1
69% activity compared to cholesterol
-
-
?
beta-cholestanol + O2
?
show the reaction diagram
Q55020
75% activity compared to cholesterol
-
-
?
beta-cholestanol + O2
?
show the reaction diagram
-
78% activity compared to cholesterol
-
-
?
beta-cholestanol + O2
?
show the reaction diagram
-
79% activity compared to cholesterol
-
-
?
beta-cholestanol + O2
?
show the reaction diagram
B5MGF8
95% activity compared to cholesterol
-
-
?
beta-cholestanol + O2
?
show the reaction diagram
Streptoverticillium cholesterolieum
-
96% activity compared to cholesterol
-
-
?
beta-cholestanol + O2
?
show the reaction diagram
Pseudomonas sp. COX629
-
78% activity compared to cholesterol
-
-
?
beta-cholestanol + O2
?
show the reaction diagram
uncultured gamma proteobacterium Y-134
-
79% activity compared to cholesterol
-
-
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
show the reaction diagram
-
20% activity compared to cholesterol
-
-
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
show the reaction diagram
-
29% activity compared to cholesterol
-
-
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
show the reaction diagram
Streptoverticillium cholesterolieum
-
39% activity compared to cholesterol
-
-
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
show the reaction diagram
Corynebacterium cholesterolicum
-
50% activity compared to cholesterol
-
-
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
show the reaction diagram
-
64% activity compared to cholesterol
-
-
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
show the reaction diagram
Q55020
72% activity compared to cholesterol
-
-
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
show the reaction diagram
B5MGF8
80% activity compared to cholesterol
-
-
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
show the reaction diagram
Q93RE1
84% activity compared to cholesterol
-
-
?
beta-sitosterol + O2
? + H2O2
show the reaction diagram
H9NJ43, H9NJ52
-
-
-
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
show the reaction diagram
Burkholderia cepacia ST-200
Q93RE1
84% activity compared to cholesterol
-
-
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
show the reaction diagram
-
72% activity compared to cholesterol
-
-
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
show the reaction diagram
uncultured gamma proteobacterium Y-134
-
29% activity compared to cholesterol
-
-
?
beta-stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
show the reaction diagram
-
10% activity compared to cholesterol
-
-
?
beta-stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
show the reaction diagram
Corynebacterium cholesterolicum
-
12% activity compared to cholesterol
-
-
?
beta-stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
show the reaction diagram
Streptoverticillium cholesterolieum
-
17% activity compared to cholesterol
-
-
?
beta-stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
show the reaction diagram
-
32% activity compared to cholesterol
-
-
?
beta-stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
show the reaction diagram
B5MGF8
36% activity compared to cholesterol
-
-
?
beta-stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
show the reaction diagram
Q55020
37% activity compared to cholesterol
-
-
?
beta-stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
show the reaction diagram
-
40% activity compared to cholesterol
-
-
?
beta-stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
show the reaction diagram
-
47% activity compared to cholesterol
-
-
?
beta-stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
show the reaction diagram
-
50% activity compared to cholesterol
-
-
?
beta-stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
show the reaction diagram
Q93RE1
59% activity compared to cholesterol
-
-
?
beta-stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
show the reaction diagram
Pseudomonas sp. COX629
-
40% activity compared to cholesterol
-
-
?
beta-stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
show the reaction diagram
uncultured gamma proteobacterium Y-134
-
32% activity compared to cholesterol
-
-
?
cholest-4-en-3-one + O2
? + H2O2
show the reaction diagram
H9NJ43, H9NJ52
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Q56DL0
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Streptomyces fradiae, Nocardia rhodochrous
-
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Q93JS8
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Q93H76
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
A7RA76
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Q9EW96
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Q55020
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
B1VGH1
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Q5YRJ2
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Q59530
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Q57307
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Q9L0H6
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
A9QAE7
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Q2T0X3
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Q13UN0
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
100% activity
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Q55020
100% activity
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Q93RE1
100% activity
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
B5MGF8
100% activity
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Streptoverticillium cholesterolieum, Brevibacterium sterolicum
-
100% activity
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
cholesterol oxidase is required for the biosynthesis of the antifungal polyene pimaricin
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
cholesterol oxidase is required for the biosynthesis of the antifungal polyene pimaricin, apparently acting as an antifungal sensor
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
P12676
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
Nocardia rhodochrous
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
Nocardia rhodochrous
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
Nocardia rhodochrous
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
Nocardia erythropolis
-
-
-
-
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
Nocardia erythropolis
-
-
-
-
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
Nocardia erythropolis
-
-
-
-
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
Nocardia erythropolis
-
-
-
-
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
Nocardia erythropolis
-
-
-
-
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
Nocardia erythropolis
-
-
-
-
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
Nocardia erythropolis
-
-
-
r
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
Corynebacterium cholesterolicum
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
Corynebacterium cholesterolicum
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
H9NJ43, H9NJ52
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
Nocardia rhodochrous
-
first step in cholesterol degradation
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
Nocardia erythropolis
-
first step in cholesterol degradation
-
-
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
first step in cholesterol degradation
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
Burkholderia cepacia ST-200
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Burkholderia cepacia ST-200
Q93RE1
100% activity
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Streptomyces sp. SA-COO, Pseudomonas sp. COX629
-
100% activity
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Brevibacterium sp. M201008
-
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
uncultured gamma proteobacterium Y-134
-
100% activity
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
Rhodococcus sp. GK1
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Corynebacterium urealyticum DSM7109
B1VGH1
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Nocardia farcinica IFM10152
Q5YRJ2
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
Streptomyces sp. A19249
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
show the reaction diagram
Pseudomonas sp. ST-200
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
-
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Streptomyces sp. R-6
-
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Streptomyces parvus 13647 J
-
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Arthrobacter sp. IM79
-
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Q56DL0
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
Rhodococcus equi ATCC33706
Q93JS8
-
-
-
?
dehydroandrosterone + O2
? + H2O2
show the reaction diagram
H9NJ43, H9NJ52
-
-
-
?
dehydroepiandrosterone + O2
androst-5-en-3,17-dione + H2O2
show the reaction diagram
Q93RE1
16% activity compared to cholesterol
-
-
?
dehydroepiandrosterone + O2
androst-5-en-3,17-dione + H2O2
show the reaction diagram
Q55020
24% activity compared to cholesterol
-
-
?
dehydroepiandrosterone + O2
androst-5-en-3,17-dione + H2O2
show the reaction diagram
B5MGF8
27% activity compared to cholesterol
-
-
?
dehydroepiandrosterone + O2
androst-5-en-3,17-dione + H2O2
show the reaction diagram
-
28% activity compared to cholesterol
-
-
?
dehydroepiandrosterone + O2
androst-5-en-3,17-dione + H2O2
show the reaction diagram
-
37% activity compared to cholesterol
-
-
?
dehydroepiandrosterone + O2
androst-5-en-3,17-dione + H2O2
show the reaction diagram
-
41% activity compared to cholesterol
-
-
?
dehydroepiandrosterone + O2
androst-5-en-3,17-dione + H2O2
show the reaction diagram
Streptoverticillium cholesterolieum
-
48% activity compared to cholesterol
-
-
?
dehydroepiandrosterone + O2
androst-5-en-3,17-dione + H2O2
show the reaction diagram
Corynebacterium cholesterolicum
-
5% activity compared to cholesterol
-
-
?
dehydroepiandrosterone + O2
androst-5-en-3,17-dione + H2O2
show the reaction diagram
Burkholderia cepacia ST-200
Q93RE1
16% activity compared to cholesterol
-
-
?
dehydroepiandrosterone + O2
androst-5-en-3,17-dione + H2O2
show the reaction diagram
-
24% activity compared to cholesterol
-
-
?
diosgenin + O2
? + H2O2
show the reaction diagram
H9NJ43, H9NJ52
-
-
-
?
epiandosterone + O2
?
show the reaction diagram
-
1% activity compared to cholesterol
-
-
?
epiandosterone + O2
?
show the reaction diagram
Q93RE1
10% activity compared to cholesterol
-
-
?
epiandosterone + O2
?
show the reaction diagram
B5MGF8
15% activity compared to cholesterol
-
-
?
ergosterol + O2
dehydroergosterol + H2O2
show the reaction diagram
Q55020
12% activity compared to cholesterol
-
-
?
ergosterol + O2
dehydroergosterol + H2O2
show the reaction diagram
B5MGF8
12% activity compared to cholesterol
-
-
?
ergosterol + O2
dehydroergosterol + H2O2
show the reaction diagram
-
14% activity compared to cholesterol
-
-
?
ergosterol + O2
dehydroergosterol + H2O2
show the reaction diagram
-
17% activity compared to cholesterol
-
-
?
ergosterol + O2
dehydroergosterol + H2O2
show the reaction diagram
Q93RE1
20% activity compared to cholesterol
-
-
?
ergosterol + O2
dehydroergosterol + H2O2
show the reaction diagram
Corynebacterium cholesterolicum
-
4% activity compared to cholesterol
-
-
?
ergosterol + O2
dehydroergosterol + H2O2
show the reaction diagram
Streptoverticillium cholesterolieum
-
5% activity compared to cholesterol
-
-
?
ergosterol + O2
dehydroergosterol + H2O2
show the reaction diagram
-
51% activity compared to cholesterol
-
-
?
ergosterol + O2
dehydroergosterol + H2O2
show the reaction diagram
Burkholderia cepacia ST-200
Q93RE1
20% activity compared to cholesterol
-
-
?
ergosterol + O2
dehydroergosterol + H2O2
show the reaction diagram
-
12% activity compared to cholesterol
-
-
?
pregnenolone + O2
5-pregnen-3,20-dione + H2O2
show the reaction diagram
-
20% activity compared to cholesterol
-
-
?
pregnenolone + O2
5-pregnen-3,20-dione + H2O2
show the reaction diagram
-
22% activity compared to cholesterol
-
-
?
pregnenolone + O2
5-pregnen-3,20-dione + H2O2
show the reaction diagram
Q93RE1
32% activity compared to cholesterol
-
-
?
pregnenolone + O2
5-pregnen-3,20-dione + H2O2
show the reaction diagram
Streptoverticillium cholesterolieum
-
37% activity compared to cholesterol
-
-
?
pregnenolone + O2
5-pregnen-3,20-dione + H2O2
show the reaction diagram
Corynebacterium cholesterolicum
-
38% activity compared to cholesterol
-
-
?
pregnenolone + O2
5-pregnen-3,20-dione + H2O2
show the reaction diagram
-
42% activity compared to cholesterol
-
-
?
pregnenolone + O2
5-pregnen-3,20-dione + H2O2
show the reaction diagram
-
6% activity compared to cholesterol
-
-
?
pregnenolone + O2
5-pregnen-3,20-dione + H2O2
show the reaction diagram
B5MGF8
95% activity compared to cholesterol
-
-
?
pregnenolone + O2
5-pregnen-3,20-dione + H2O2
show the reaction diagram
Q55020
99% activity compared to cholesterol
-
-
?
pregnenolone + O2
? + H2O2
show the reaction diagram
H9NJ43, H9NJ52
-
-
-
?
pregnenolone + O2
5-pregnen-3,20-dione + H2O2
show the reaction diagram
Burkholderia cepacia ST-200
Q93RE1
32% activity compared to cholesterol
-
-
?
pregnenolone + O2
5-pregnen-3,20-dione + H2O2
show the reaction diagram
-
99% activity compared to cholesterol
-
-
?
ergosterol + O2
dehydroergosterol + H2O2
show the reaction diagram
Pseudomonas sp. COX629
-
51% activity compared to cholesterol
-
-
?
additional information
?
-
-
no activity with dehydroepiandrosterone
-
-
-
additional information
?
-
-
cholesterol oxidase is involved in pimaricin biosynthesis
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
no activity with ergosterol
-
-
-
additional information
?
-
-
no activity with ergosterol, pregnenolone, dehydroepiandrosterone, and epiandosterone
-
-
-
additional information
?
-
A9QAE7
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
-
-
-
additional information
?
-
Pseudomonas sp. COX629
-
no activity with dehydroepiandrosterone
-
-
-
additional information
?
-
uncultured gamma proteobacterium Y-134
-
no activity with ergosterol, pregnenolone, dehydroepiandrosterone, and epiandosterone
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
FAD
-
1 mol of FAD per mol of protein; flavoprotein
FAD
-
firmly bound; flavoprotein
FAD
-
firmly bound; flavoprotein
FAD
-
exogenous addition increases activity
FAD
-
non-covalently bound in native enzyme
FAD
-
covalently bound in His-tagged recombinant enzyme
FAD
-
non-covalently bound
FAD
-
covalently linked to His69 in a second enzyme form
FAD
-
flavoenzyme, FAD is covalently linked to His69
FAD
-
enzyme contains 1 mol of FAD per mole of protein
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
-
covalently linked
FAD
-
noncovalently bound to the enzyme
FAD
Arthrobacter sp., Brevibacterium sterolicum, Mycobacterium sp., Nocardia erythropolis, Nocardia rhodochrous, Pseudomonas spp., Rhodococcus equi, Schizophyllum commune, Streptomyces violascens, Streptoverticillum cholesterolicum
-
both as a covalently or noncovalently bound cofactor
FAD
Q56DL0
dependent on; dependent on
FAD
Q93RE1
dependent on
FAD
Q2T0X3
dependent on
FAD
Q13UN0
dependent on
FAD
Chromobacterium sp., Corynebacterium cholesterolicum
-
dependent on
FAD
B1VGH1
dependent on
FAD
Q59530
dependent on
FAD
Q57307
dependent on
FAD
Q5YRJ2
dependent on
FAD
Q93JS8
dependent on
FAD
A9QAE7
dependent on
FAD
Q93H76
dependent on
FAD
Q9L0H6
dependent on
FAD
-
dependent on
FAD
A7RA76
dependent on
FAD
Q9EW96
dependent on
FAD
Q55020
dependent on; dependent on
FAD
Streptomyces violascens, Streptoverticillium cholesterolieum, uncultured gamma proteobacterium
-
dependent on
FAD
-
the type II cholesterol oxidase fully active enzyme contains covalently bound FAD
FAD
-
the FAD cofactor is covalently attached to the protein
FAD
-
responsible for electron transfer to O2
FAD
H9NJ43, H9NJ52
;
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ba2+
-
activates slightly at 1 mM
Ca2+
-
15% activation at 1 mM
Co2+
-
10% activation at 1 mM
Co2+
-
activates 3.6% at 5 mM
Cu2+
-
activates 2.19fold at 1 mM
Cu2+
-
activates 3fold at 5 mM
Fe3+
-
activates slightly at 1 mM
K+
-
activates slightly at 1 mM
Li+
-
activates slightly at 1 mM
Mg2+
-
activates slightly at 1 mM
MgCl2
-
1 mM, 30 min at 4C, activation to 113% of control
Mn2+
-
partially activated by the addition of Mn2+
Mn2+
-
activates
Mn2+
-
25% activation at 1 mM
Sr2+
-
activates slightly at 1 mM
Zn2+
-
activates slightly at 1 mM
MnCl2
-
1 mM, 30 min at 4C, 35% inhibition
additional information
-
contains no metal ions
additional information
-
Ag+ scarcely influences the activity of the enzyme
additional information
-
no or poor effects at 5 mM by Ca2+, Zn2+, Mg2+, and Fe2+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1-Fluoro-2,4-dinitrobenzene
-
0.1 mM, 71% inhibition
2-mercaptoethanol
-
-
2-mercaptoethanol
-
-
2-pyridylhydroxymethane sulfate
-
1 mM, 30 min at 4C, 34% inhibition
2-pyridylhydroxymethane sulfate
-
1 mM, 30 min at 4C, 32% inhibition
5,10-Seco-19-nor-5-cholestyn-3,10-dione
Nocardia erythropolis
-
-
5alpha-Cholestan-3-one
-
-
5alpha-Cholestan-3beta,5alpha-diol
-
-
5alpha-Cholestan-3beta-ol
-
-
5alpha-Lanosta-8,24-dien-3beta-ol
-
-
5beta-Cholestan-3beta-ol
-
-
8-hydroxyquinoline
-
1 mM, 30 min at 4C, 29% inhibition
8-hydroxyquinoline
-
1 mM, 30 min at 4C, 20% inhibition
acetone
-
inhibits 43% at 10%
Ag+
-
88% inhibition at 1 mM
AgNO3
-
1 mM, 100% inhibition, 0.1 mM, 62% inhibition
AgNO3
-
cholesterol oxidase II
AgNO3
Brevibacterium sterolicum, Corynebacterium cholesterolicum
-
markedly inhibited by AgNO3
AgNO3
Q55020
markedly inhibited by AgNO3
AgNO3
Streptomyces violascens, Streptoverticillium cholesterolieum, uncultured gamma proteobacterium
-
markedly inhibited by AgNO3
Ba2+
-
inhibits 21.4% at 5 mM
Benzene
-
inhibits 20% at 10%
butanol
-
the enzyme is inactivated by the addition of 50% (v/v) after incubation for 24 h at 37C
butanol
A9QAE7
the enzyme is inactivated by the addition of 50% (v/v) of butanol after incubation for 24 h at 37C
Chloroform
-
inhibits 80% at 10%
cholest-4-en-3-one
Nocardia rhodochrous
-
-
cholesterol
-
substrate inhibition of mutant V191A
CoCl2
-
1 mM, 30 min at 4C, 21% inhibition
CuCl2
-
1 mM, 30 min at 4C, 29% inhibition
CuSO4
-
slight inhibition
CuSO4
-
1 mM, complete inhibition
CuSO4
Streptoverticillium cholesterolieum
-
significant inhibition
Dimethylsulfoxide
-
the enzyme is inactivated by the addition of 50% (v/v) after incubation for 24 h at 37C
Dimethylsulfoxide
A9QAE7
the enzyme is inactivated by the addition of 50% (v/v) of dimethylsulfoxide after incubation for 24 h at 37C
dithiothreitol
-
-
DMSO
-
inhibits 5% at 10%
ethyl acetate
-
the enzyme is inactivated by the addition of 50% (v/v) after incubation for 24 h at 37C
ethyl acetate
A9QAE7
the enzyme is inactivated by the addition of 50% (v/v) of ethyl acetate after incubation for 24 h at 37C
FAD
-
1 mM, 30 min at 4C, 9% inhibition
FAD
-
1 mM, 30 min at 4C, 21% inhibition
Fe2+
-
-
-
Fe2+
-
markedly inhibited by Fe2+
-
FeCl3
-
1.7 mM, 95% inhibition
FeCl3
-
markedly inhibited by FeCl3
fenpropimorph
-
irreversible inhibition; morpholine derivative, 50 mg/l, 50% inhibition, instantenous inhibition
fenpropimorph
Nocardia erythropolis, Schizophyllum commune
-
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
FeSO4
-
1.7 mM, 71% inhibition
FeSO4
-
markedly inhibited by FeSO4
FMN
-
1 mM, 30 min at 4C, 11% inhibition
FMN
-
1 mM, 30 min at 4C, 21% inhibition
Hg2+
Brevibacterium sterolicum, Corynebacterium cholesterolicum, Pimelobacter simplex
-
markedly inhibited by HgCl2
Hg2+
-
markedly inhibited by Hg2+
Hg2+
Q55020
markedly inhibited by HgCl2
Hg2+
Streptomyces violascens, Streptoverticillium cholesterolieum, uncultured gamma proteobacterium
-
markedly inhibited by HgCl2
Hg2+
-
90% inhibition at 1 mM
Hg2+
-
inhibits 21.8% at 5 mM
HgCl2
Nocardia rhodochrous
-
10 mM, complete inhibition
HgCl2
-
1 mM, 68% inhibition, 0.1 mM, 38% inhibition
HgCl2
-
cholesterol oxidase II
Iodine
-
0.1 mM, 91% inhibition
iodoacetic acid
-
1 mM, 30 min at 4C, 15% inhibition
MgCl2
-
1 mM, 30 min at 4C, 23% inhibition
MgCl2
-
1 mM, complete inhibition
Mn2+
-
inhibits 4.5% at 5 mM
N-bromosuccinimide
-
0.01 mM, 100% inhibition
Na+
-
slight inhibition at 1 mM
NEM
-
1 mM, 30 min at 4C, 24% inhibition
o-phenanthroline
-
1 mM, 30 min at 4C, 30% inhibition
o-phenanthroline
-
1 mM, 30 min at 4C, 26% inhibition
p-chloromercuribenzoate
-
1 mM, 20% inhibition, 0.1 mM, 14% inhibition
p-chloromercuribenzoate
-
0.01 mM, complete inhibition
p-chloromercuribenzoic acid
-
the addition of p-chloromercuribenzoic acid partially reduces the activity of the enzyme
Pb(OAc)2
-
1 mM, complete inhibition
PCMB
-
cholesterol oxidase II
potassium cyanide
-
1 mM, 30 min at 4C, 12% inhibition
potassium cyanide
-
1 mM, 30 min at 4C, 15% inhibition
propan-2-ol
-
at 10% propan-2-ol kcat reaches 65% of that at 1.25% propan-2-ol
riboflavin
-
1 mM, 30 min at 4C, 20% inhibition
rotenone
-
1 mM, 30 min at 4C, 12% inhibition
Sarcosyl
-
1%, 88% inhibition
Sarcosyl
-
1%, 56% inhibition
SDS
-
0.1% complete inhibition
SDS
-
0.1%, 20% inhibition, 1%, 41% inhibition
SDS
Nocardia erythropolis, Pseudomonas sp.
-
0.1% complete inhibition
Sodium deoxycholate
-
-
Sodium dodecyl sulfate
-
inactivates the enzyme
sulfhydryl reagents
-
-
Trinitrobenzene sulfonate
-
0.3 mM, 66% inhibition
Triton X-100
-
inactivates at a concentration of 0.02%
Triton X-100
-
stimulates at concentration up to 0.2%
Triton X-100
-
strong decrease in enzyme activity at concentration of 0.2% Triton X-100 or higher
Zn2+
-
1 mM, 34% loss of activity
Zn2+
-
markedly inhibited by Zn2+
MnCl2
-
1 mM, 30 min at 4C, 35% inhibition
additional information
-
not inhibited by p-chloromercuribenzoate; overview: inhibition by steroids
-
additional information
-
not inhibited by 10 mM cyanide or 50 mM arsenite
-
additional information
-
not inhibited by 1% Triton X-100, 1% Tween 20, 1% sodium cholate and 1% CHAPS
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
acetone
-
3.8fold increase in activity, 1 ml solvent added to 2 ml 50 mM phosphate buffer
Benzene
-
strain ST-200, 3fold increase in activity, 1 ml solvent added to 2 ml 50 mM phosphate buffer, pH 7.0
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
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
-
ethanol
-
activates 1.6fold at 10%
Isopropanol
-
activates 2.3fold at 10%
Long-chain alcohols
-
maximum activation with decanol and undecanol, shorter and longer alcohols are less effective
methanol
-
activates 1.15fold at 10%
p-xylene
-
strain ST-200, 3.4fold increase in activity, 1 ml solvent added to 2 ml 50 mM phosphate buffer, pH 7.0
phosphate ions
-
activity is enhanced by high concentrations
phosphate ions
-
marked increase above 90 mM
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
propan-2-ol
-
2fold increase in activity, 1 ml solvent added to 2 ml 50 mM phosphate buffer
propylbenzene
-
strain ST-200, 3.2fold increase in activity, 1 ml solvent added to 2 ml 50 mM phosphate buffer, pH 7.0
Toluene
-
strain ST-200, 3.5fold increase in activity, 1 ml solvent added to 2 ml 50 mM phosphate buffer, pH 7.0
Triton X-100
Nocardia rhodochrous
-
stimulates at concentration up to 0.2%
Triton X-100
-
inactivates at a concentration of 0.02%
Triton X-100
-
stimulates at concentration up to 0.2%
Triton X-100
-
acivates 3.5fold at 0.5%
Triton X-114
-
acivates 2fold at 0.5%
Tween 80
-
acivates 1.5fold at 0.5%
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0031
-
17beta-Hydroxymethyl-5-androsten-3beta-ol
Nocardia erythropolis
-
-
0.0071
-
20,22-dihydroxycholesterol
Nocardia erythropolis
-
-
0.124
-
20,25-Diazacholesterol
Nocardia erythropolis
-
-
0.0042
-
20-hydroxycholesterol
Nocardia erythropolis
-
-
0.0051
-
22-hydroxycholesterol
Nocardia erythropolis
-
-
0.0093
-
23,24-dinor-5-cholene-3beta,22-diol
Nocardia erythropolis
-
-
0.0043
-
24-hydroxycholesterol
Nocardia erythropolis
-
-
0.0027
-
24-oxocholesterol
Nocardia erythropolis
-
-
0.0014
-
25-Hydroxy-27-norcholesterol
Nocardia erythropolis
-
-
0.0015
-
25-hydroxycholesterol
Nocardia erythropolis
-
-
0.0012
-
26-Hydroxycholesterol
Nocardia erythropolis
-
5-androstene-3beta,17beta-diol
0.0012
-
26-Hydroxycholesterol
Nocardia erythropolis
-
-
0.0036
-
3beta-hydroxy-5-androsten-17-one
Nocardia erythropolis
-
-
0.0017
-
3beta-hydroxy-5-pregnen-20-one
Nocardia erythropolis
-
-
0.3
-
3beta-hydroxy-androst-5-en-17-one
-
assay relies on spectroscopic detection of 4-cholesten-3-one formation
0.3
-
3beta-hydroxy-androst-5-en-17-one
-
-
0.5
-
3beta-hydroxy-androst-5-en-17-one
-
assay relies on detection of H2O2 formation
0.5
-
3beta-hydroxy-androst-5-en-17-one
-
-
0.8
-
3beta-hydroxy-androst-5-en-17-one
-
assay relies on detection of H2O2 formation
0.8
-
3beta-hydroxy-androst-5-en-17-one
-
-
1.2
-
3beta-hydroxy-androst-5-en-17-one
-
assay relies on spectroscopic detection of 4-cholesten-3-one formation
1.2
-
3beta-hydroxy-androst-5-en-17-one
-
-
0.0075
-
4,4-Dimethylcholesterol
Nocardia erythropolis
-
-
0.0126
-
4alpha-Methylcholesterol
Nocardia erythropolis
-
-
0.0284
-
4beta-methylcholesterol
Nocardia erythropolis
-
-
0.0055
-
5,7-cholestadien-3beta-ol
Nocardia erythropolis
-
-
0.548
-
5-Androstene-3,17-dione
Nocardia erythropolis
-
-
0.0048
-
5-Cholene-3beta,24-diol
Nocardia erythropolis
-
-
0.007
-
5-Cholesten-3-one
Nocardia erythropolis
-
-
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
0.0125
-
5-Pregnene-3,20-dione
Nocardia erythropolis
-
-
0.0037
-
5-pregnene-3beta,20beta-diol
Nocardia erythropolis
-
-
0.0028
-
5alpha-Cholest-8(14)-en-3beta-ol
Nocardia erythropolis
-
-
0.0107
-
5alpha-cholest-8(14)en-3beta-ol
Nocardia erythropolis
-
-
0.0023
-
5alpha-Cholestan-3beta-ol
Nocardia erythropolis
-
-
0.18
-
beta-sitosterol
H9NJ43, H9NJ52
pH 7.5, 37C, full-length isozyme ChoM2
0.19
-
beta-sitosterol
H9NJ43, H9NJ52
pH 7.5, 37C, truncated isozyme ChoM2
0.2
-
beta-sitosterol
H9NJ43, H9NJ52
pH 7.5, 37C
0.25
-
beta-sitosterol
-
in the presence of undecanol
0.5
-
beta-sitosterol
-
-
0.02
-
cholestanol
-
-
0.2
-
cholestanol
-
assay relies on detection of H2O2 formation
0.2
-
cholestanol
-
substrate cholestanol, rate of H2O2 formation detected with o-dianisidine and horseradish peroxidase. 0.1 M potassium phosphate, 1% Triton X-100, 1.25% propan-2-ol, 25C and pH 7.5
0.7
-
cholestanol
-
assay relies on detection of H2O2 formation
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, 25C and pH 7.5
0.0000081
-
cholesterol
-
pH 7.0, 37C, mutant enzyme S379T
0.00002
-
cholesterol
-
pH 7.0, 37C, wild-type enzyme
0.00003
-
cholesterol
-
pH 7.0, 37C, mutant enzyme S379A
0.000046
-
cholesterol
-
pH 7.0, 37C, mutant enzyme S379V
0.000072
-
cholesterol
-
pH 7.0, 37C, mutant enzyme V145Q
0.000081
-
cholesterol
-
pH 7.0, 37C, mutant enzyme L119A
0.00011
-
cholesterol
-
pH 7.0, 37C, mutant enzyme P357N
0.00013
-
cholesterol
-
pH 7.0, 37C, mutant enzyme Q286R
0.00017
-
cholesterol
-
pH 7.0, 37C, mutant enzyme L119F
0.0004
-
cholesterol
-
pH 7.0, 37C, mutant enzyme V145D
0.00067
-
cholesterol
-
pH 7.0, 37C, mutant enzyme V145E
0.0015
-
cholesterol
-
mutant enzyme G347N, determined by cholest-4-en-3-one detection
0.00245
-
cholesterol
-
recombinant mutant V191A, pH 7.0, 22C
0.0027
-
cholesterol
-
mutant enzyme F359W, determined by cholest-4-en-3-one detection; wild-type enzyme, determined by cholest-4-en-3-one detection; wild-type enzyme, determined by H2O2 detection
0.0027
-
cholesterol
-
apparent value, wild type enzyme, pH 7.0, temperature not specified in the publication
0.0029
-
cholesterol
Nocardia erythropolis
-
-
0.003
-
cholesterol
-
-
0.003
-
cholesterol
-
mutant enzyme H447Q; wild-type enzyme
0.004
-
cholesterol
-
strain ST-200
0.004
-
cholesterol
-
mutant enzyme F359W, determined by H2O2 detection
0.0046
-
cholesterol
-
apparent value, mutant enzyme N485L, pH 7.0, temperature not specified in the publication
0.005
-
cholesterol
-
mutant enzyme H447Q/E361Q
0.005
-
cholesterol
-
mutant enzyme G347N, determined by H2O2 detection
0.0051
-
cholesterol
Nocardia erythropolis
-
-
0.0054
-
cholesterol
-
mutant enzyme E361
0.0062
-
cholesterol
-
mutant enzyme N485D, determined by H2O2 detection
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
0.011
-
cholesterol
-
V145E mutant
0.013
-
cholesterol
Nocardia erythropolis
-
Km increases when enzyme is entrapped in reverse micelles of the synthetic surfactant aerosol-OT-isooctane
0.013
-
cholesterol
-
S103T mutant; wild-type
0.0184
-
cholesterol
-
pH 7.0, temperature not specified in the publication
0.0188
-
cholesterol
A9QAE7
pH and temperature not specified in the publication
0.025
-
cholesterol
-
-
0.026
-
cholesterol
-
pH 6.0 or pH 7.0
0.026
-
cholesterol
-
-
0.0262
-
cholesterol
-
pH and temperature not specified in the publication
0.03
-
cholesterol
-
R135H mutant
0.03
-
cholesterol
-
pH 7.0, 37C, cholesterol oxidase II
0.031
-
cholesterol
-
cell-linked and extracellular enzyme
0.032
-
cholesterol
Q157H4
pH 7.0, 50C
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, 25C and pH 7.5
0.07
-
cholesterol
-
-
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, 25C and pH 7.5
0.1013
-
cholesterol
-
pH 7.0, 37C
0.11
-
cholesterol
-
-
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, 25C and pH 7.5
0.12
-
cholesterol
-
recombinant wild-type enzyme, pH 7.0, 22C
0.12
-
cholesterol
H9NJ43, H9NJ52
pH 7.5, 37C, full-length isozyme ChoM2
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, 25C and pH 7.5
0.14
-
cholesterol
H9NJ43, H9NJ52
pH 7.5, 37C, truncated isozyme ChoM2
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, 25C and pH 7.5
0.17
-
cholesterol
H9NJ43, H9NJ52
pH 7.5, 37C
0.2
-
cholesterol
-
-
0.2
-
cholesterol
-
-
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, 25C 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, 25C and pH 7.5
0.2123
-
cholesterol
-
apparent value, free enzyme, in 50 mM potassium phosphate buffer, pH 7.5, 30C
0.25
-
cholesterol
-
-
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, 25C 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, 25C and pH 7.5
0.2599
-
cholesterol
-
apparent value, silk mat-immobilized enzyme, in 50 mM potassium phosphate buffer, pH 7.5, 30C
0.33
-
cholesterol
-
-
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, 25C and pH 7.5
0.47
-
cholesterol
-
H69A mutant enzyme, 50 mM phosphate buffer, pH 7.5, 1% thesit, 1% 2-propanol
0.524
-
cholesterol
A7LGL0
pH 7.5, 37C
0.556
-
cholesterol
-
pH 7.0, 37C
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, 25C and pH 7.5
1
-
cholesterol
-
in the presence of undecanol
1.1
-
cholesterol
-
pH 7.0, 37C, cholesterol oxidase I
2
-
cholesterol
-
in the presence of undecanol
4.5
-
cholesterol
-
pH 7, 30C, enzyme CO2
6.76
-
cholesterol
-
pH 7, 30C, enzyme CO1
24.3
-
cholesterol
-
native enzyme, pH 7.2, 37C
25.4
-
cholesterol
-
non-tagged recombinant enzyme, pH 7.2, 37C
35.4
-
cholesterol
-
N-terminally His-tagged recombinant enzyme , pH 7.2, 37C
45.2
-
cholesterol
-
C-terminally His-tagged recombinant enzyme , pH 7.2, 37C
0.2
-
dehydroandrosterone
H9NJ43, H9NJ52
pH 7.5, 37C, full-length isozyme ChoM2
0.24
-
dehydroandrosterone
H9NJ43, H9NJ52
pH 7.5, 37C
0.25
-
dehydroandrosterone
H9NJ43, H9NJ52
pH 7.5, 37C, truncated isozyme ChoM2
0.0275
-
dehydroepiandrosterone
-
-
0.4
-
dehydroepiandrosterone
-
-
0.491
-
dehydroepiandrosterone
A7LGL0
pH 7.5, 37C
1
-
dehydroepiandrosterone
-
in the presence and absence of undecanol
0.195
-
diosgenin
A7LGL0
pH 7.5, 37C
0.23
-
diosgenin
H9NJ43, H9NJ52
pH 7.5, 37C; pH 7.5, 37C, full-length isozyme ChoM2
0.26
-
diosgenin
H9NJ43, H9NJ52
pH 7.5, 37C, truncated isozyme ChoM2
0.3
-
O2
-
wild-type enzyme
0.45
-
O2
-
H69A mutant enzyme, 50 mM phosphate buffer, pH 7.5, 1% thesit, 1% 2-propanol
0.617
-
O2
-
mutant enzyme F359W
0.0000058
-
pregnenolone
-
pH 7.0, 37C, mutant enzyme S379T
0.000023
-
pregnenolone
-
pH 7.0, 37C, mutant enzyme S379A; pH 7.0, 37C, wild-type enzyme
0.00004
-
pregnenolone
-
pH 7.0, 37C, mutant enzyme L119A; pH 7.0, 37C, mutant enzyme S379V
0.000056
-
pregnenolone
-
pH 7.0, 37C, mutant enzyme Q286R
0.000058
-
pregnenolone
-
pH 7.0, 37C, mutant enzyme V145Q
0.000077
-
pregnenolone
-
pH 7.0, 37C, mutant enzyme L119F
0.000083
-
pregnenolone
-
pH 7.0, 37C, mutant enzyme V145E
0.000098
-
pregnenolone
-
pH 7.0, 37C, mutant enzyme P357N
0.2
-
pregnenolone
-
assay relies on spectroscopic detection of 4-cholesten-3-one formation
0.2
-
pregnenolone
-
-
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, 25C 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, 25C and pH 7.5; 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, 25C and pH 7.5
0.33
-
pregnenolone
H9NJ43, H9NJ52
pH 7.5, 37C, full-length isozyme ChoM2
0.35
-
pregnenolone
H9NJ43, H9NJ52
pH 7.5, 37C, truncated isozyme ChoM2
0.38
-
pregnenolone
H9NJ43, H9NJ52
pH 7.5, 37C
0.4
-
pregnenolone
-
assay relies on spectroscopic detection of 4-cholesten-3-one formation
0.4
-
pregnenolone
-
-
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, 25C and pH 7.5
0.5
-
pregnenolone
-
-
4
-
pregnenolone
-
in the presence of undecanol
0.0066
-
sitosterol
Nocardia erythropolis
-
-
0.59
1
sitosterol
A7LGL0
pH 7.5, 37C
0.0059
-
stigmasterol
Nocardia erythropolis
-
-
0.45
-
stigmasterol
-
-
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, 25C 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, 25C 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, 25C 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, 25C 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, 25C 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, 25C and pH 7.5
0.0115
-
fucosterol
Nocardia erythropolis
-
-
additional information
-
additional information
-
Km-values of enzyme immobilized on platinum electrode modified with thiolipid/lipid bilayer membranes
-
additional information
-
additional information
-
kinetics, modelling
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
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
37
-
cholestanol
-
assay relies on detection of H2O2 formation
37
-
cholestanol
-
H2O2 production assayed, 100 mM phosphate buffer
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, 25C and pH 7.5
40
-
cholestanol
-
assay relies on detection of H2O2 formation
40
-
cholestanol
-
H2O2 production assayed, 100 mM phosphate buffer
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, 25C and pH 7.5
0.0014
-
cholesterol
-
mutant enzyme H447E/E361Q
0.017
-
cholesterol
-
mutant enzyme H447E
0.035
-
cholesterol
-
mutant enzyme N485D, determined by H2O2 detection
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
0.093
-
cholesterol
-
mutant enzyme H447Q/E361Q
0.32
-
cholesterol
-
mutant enzyme H447Q
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
0.85
-
cholesterol
-
mutant enzyme G347N, determined by H2O2 detection
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
1.3
-
cholesterol
-
mutant enzyme F359W, determined by H2O2 detection
1.4
-
cholesterol
-
mutant enzyme E361
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
2.21
-
cholesterol
-
recombinant mutant V191A, pH 7.0, 22C
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, 25C 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, 25C and pH 7.5
9
-
cholesterol
-
pH 7.0, 37C, mutant enzyme P357N
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, 25C and pH 7.5
11
-
cholesterol
-
assay relies on spectroscopic detection of 4-cholesten-3-one formation
11
-
cholesterol
-
pH 7.0, 37C, mutant enzyme V145D; pH 7.0, 37C, mutant enzyme V145Q
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, 25C and pH 7.5
15
-
cholesterol
-
pH 7.0, 37C, mutant enzyme L119A
23
-
cholesterol
-
pH 7.0, 37C, mutant enzyme Q286R; pH 7.0, 37C, mutant enzyme V145E
27
-
cholesterol
-
pH 7.0, 37C, mutant enzyme L119F
28
-
cholesterol
-
50 mM phosphate buffer, pH 7.5
29
-
cholesterol
-
pH 7.0, 37C, mutant enzyme S379T
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, 25C and pH 7.5
40
-
cholesterol
-
pH 7.0, 37C, wild-type enzyme
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, 25C and pH 7.5
44
-
cholesterol
-
-
44
-
cholesterol
-
wild-type enzyme
46
-
cholesterol
-
apparent value, wild type enzyme, pH 5.1, temperature not specified in the publication
47
-
cholesterol
-
wild-type enzyme, determined by H2O2 detection
47
-
cholesterol
-
apparent value, wild type enzyme, pH 7.0, temperature not specified in the publication
47.3
-
cholesterol
-
recombinant wild-type enzyme, pH 7.0, 22C
48
-
cholesterol
-
50 mM phosphate buffer, pH 7.5
48
-
cholesterol
-
substrate cholesterol, detection of product formation (cholest-4-en-3-one) at 240 nm. 0.1 M potassium phosphate, 1% Triton X-100, 1.25% propan-2-ol, 25C and pH 7.5; 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, 25C 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
49
-
cholesterol
-
pH 7.0, 37C, mutant enzyme S379A
51
-
cholesterol
-
pH 7.0, 37C, mutant enzyme S379V
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, 25C 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, 25C and pH 7.5
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, 25C 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, 25C and pH 7.5
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
0.69
-
dehydroepiandrosterone
-
-
7
-
epiandrosterone
-
H2O2 production assayed, 100 mM phosphate buffer
9
-
pregnenolone
-
pH 7.0, 37C, mutant enzyme P357N; pH 7.0, 37C, mutant enzyme V145D
11
-
pregnenolone
-
pH 7.0, 37C, mutant enzyme V145E
12
-
pregnenolone
-
pH 7.0, 37C, mutant enzyme V145Q
13
-
pregnenolone
-
pH 7.0, 37C, mutant enzyme L119A
19
-
pregnenolone
-
pH 7.0, 37C, mutant enzyme Q286R
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
-
pH 7.0, 37C, mutant enzyme L119F
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, 25C 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, 25C 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, 25C and pH 7.5
30
-
pregnenolone
-
pH 7.0, 37C, wild-type enzyme
35
-
pregnenolone
-
pH 7.0, 37C, mutant enzyme S379A
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, 25C and pH 7.5
39
-
pregnenolone
-
pH 7.0, 37C, mutant enzyme S379V
45
-
pregnenolone
-
pH 7.0, 37C, mutant enzyme S379T
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, 25C 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, 25C 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, 25C 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, 25C 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, 25C 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, 25C and pH 7.5
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0013
-
cholesterol
-
apparent value, silk mat-immobilized enzyme, in 50 mM potassium phosphate buffer, pH 7.5, 30C
8550
394
-
cholesterol
-
recombinant wild-type enzyme, pH 7.0, 22C
8550
902
-
cholesterol
-
recombinant mutant V191A, pH 7.0, 22C
8550
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.381
-
O2
-
mutant enzyme F359W
1.383
-
O2
-
wild-type enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.045
0.069
Nocardia rhodochrous
-
substrate cholesterol
0.049
-
-
purified recombinant mutant V191A, oxidase activity, pH 7.0, 22C
0.061
-
-
purified recombinant mutant M122A, oxidase activity, pH 7.0, 22C
0.074
-
-
purified recombinant mutant F359A, oxidase activity, pH 7.0, 22C
0.1
-
H9NJ43, H9NJ52
purified full-length isozyme ChoM2, substrate pregnenolone, pH 7.5, 37C
0.12
-
H9NJ43, H9NJ52
purified truncated isozyme ChoM2, substrate pregnenolone, pH 7.5, 37C
0.13
-
H9NJ43, H9NJ52
purified isozyme ChoM1, substrate pregnenolone, pH 7.5, 37C
0.15
-
-
purified recombinant mutant V124A, oxidase activity, pH 7.0, 22C
0.16
-
H9NJ43, H9NJ52
purified isozyme ChoM1, substrate dehydroandrosterone, pH 7.5, 37C
0.17
-
H9NJ43, H9NJ52
purified truncated isozyme ChoM2, substrate dehydroandrosterone, pH 7.5, 37C
0.19
-
H9NJ43, H9NJ52
purified full-length isozyme ChoM2, substrate dehydroandrosterone, pH 7.5, 37C; purified isozyme ChoM1, substrate diosgenin, pH 7.5, 37C
0.21
-
H9NJ43, H9NJ52
purified full-length isozyme ChoM2, substrate diosgenin, pH 7.5, 37C
0.22
-
-
purified recombinant mutant F444A, oxidase activity, pH 7.0, 22C
0.22
-
H9NJ43, H9NJ52
purified isozyme ChoM1, substrate beta-sitosterol, pH 7.5, 37C
0.23
-
H9NJ43, H9NJ52
purified isozyme ChoM1, substrate cholesterol, pH 7.5, 37C
0.25
-
H9NJ43, H9NJ52
purified full-length isozyme ChoM2, substrate beta-sitosterol, pH 7.5, 37C
0.26
-
H9NJ43, H9NJ52
purified truncated isozyme ChoM2, substrate diosgenin, pH 7.5, 37C
0.28
-
-
purified recombinant mutant Y446A, oxidase activity, pH 7.0, 22C
0.28
-
H9NJ43, H9NJ52
purified full-length isozyme ChoM2, substrate cholesterol, pH 7.5, 37C
0.33
-
H9NJ43, H9NJ52
purified truncated isozyme ChoM2, substrate beta-sitosterol, pH 7.5, 37C
0.42
-
H9NJ43, H9NJ52
purified truncated isozyme ChoM2, substrate cholesterol, pH 7.5, 37C
0.6
-
-
polyethylene glycol derivative-modified enzyme
2.42
-
-
inducible enzyme
2.7
-
-
purified recombinant wild-type enzyme, oxidase activity, pH 7.0, 22C
3.65
-
-
constitutive enzyme
4
-
-
C-terminally His-tagged recombinant enzyme expressed in Escherichia coli, pH 7.2, 37C
7.6
-
-
enzyme CO1
8
-
-
enzyme CO2
12
-
-
N-terminally His-tagged recombinant enzyme expressed in Escherichia coli, pH 7.2, 37C
15.2
-
-
strain ST-200
16
-
-
non-tagged recombinant enzyme expressed in Escherichia coli, pH 7.2, 37C
17.5
-
-
native enzyme from Brevibacterium sp., pH 7.2, 37C
20
-
-
purified enzyme, pH 7.2, 50C
20.81
-
-
purified enzyme, pH 7.0, 37C
21.8
-
-
purified enzyme, pH 7.0, 37C
26.7
-
-
S103T/V145A/V121A/R135H quadruple mutant
27.9
-
-
-
39.9
-
-
S103T/V145A double mutant
47.8
-
-
S103T/V145A/V121A triple mutant
55.2
-
-
cholesterol oxidase II
63.5
-
-
V145E mutant, 37C, pH 7.0
67.7
-
-
wild type
68.9
-
-
R135H mutant, 37C, pH 7.0
72
-
-
V121A mutant, 37C, pH 7.0
86.6
-
-
S103T mutant, 37C, pH 7.0
additional information
-
-
-
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; comparison of the effect of detergents and solvents on ChOx activity and stability (from different sources)
additional information
-
Mycobacterium sp., Nocardia erythropolis, Nocardia rhodochrous, Pseudomonas spp.
-
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; comparison of the effect of detergents and solvents on ChOx activity and stability (from different sources)
additional information
-
Schizophyllum commune, Streptomyces violascens, 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; comparison of the effect of detergents and solvents on ChOx activity and stability (from different sources)
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
8
-
extracellular enzyme
6
8.2
-
membrane bound enzyme
6
-
-
wild-type, S103T, V121A and R135H mutants
6
-
-
reaction with cholesterol, enzyme CO2
6
-
-
immobilized enzyme on oxygen electrode
6.5
7
Q55020
-
6.5
-
-
reaction with cholesterol, enzyme CO1
6.5
-
-
cholesterol oxidase II
6.8
8
-
strain ST-200
6.8
8
Q93RE1
-
7
7.5
-
extracellular enzyme
7
7.5
Chromobacterium sp., Corynebacterium cholesterolicum, Streptoverticillium cholesterolieum
-
-
7
-
Nocardia rhodochrous
-
-
7
-
-
native and enzyme immobilized on polyacrylonitrile hollow fibers
7
-
-
cholesterol oxidase I
7
-
-
-
7
-
Q55020
-
7
-
Q157H4
-
7
-
-
assay at
7.5
8.5
Q56DL0
-
7.5
-
Nocardia erythropolis
-
enzyme after micellization
7.5
-
-
V145E mutant
7.5
-
Q56DL0
assay at
7.5
-
-
silk mat-immobilized enzyme
7.5
-
H9NJ43, H9NJ52
assay at; assay at
8
-
-
membrane-bound enzyme
8
-
Q93JS8
-
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
10
-
activity range
4
10
-
activity range, profile overview
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
11
-
activity range
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
-
pH 5: 78% of maximal activity, pH 8.0: 75% of maximal activity, reaction with cholestero, enzyme CO2
5
8.5
-
strain ST-200
5
8.5
-
pH 5.0: about 75% of maximalm acttivity, pH 8.5: about 60% of maximal activity, cholesterol oxidase II
5
9
-
33% of maximal activity at pH 5.0 and pH 9.0
5
9
-
pH 5: 83% of maximal activity, pH 9.0: 77% of maximal activity, reaction with cholesterol, enzyme CO1
5
9.5
-
about 50% of maximal activity at pH 5 and 9.5
5.5
8
Q157H4
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
-
pH 5.5: about 50% of maximal activity, pH 8.5: about 40% of maximal activity, cholesterol oxidase I
6
8
-
wild-type, S103T, V121A, R135H and V145E mutants
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
9.5
-
pH 6.0: about 65% of maximal activity, pH 9.5: about 60% of maximal activcity
6.5
9
-
strong decrease in enzyme activity above
6.5
9
A7LGL0
ChoL retains more than 80% activity in the pH range 6.5-9.0
additional information
-
-
pH-dependencies of native and recombinant non-tagged or His-tagged enzyme is similar, overview
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
-
-
enzyme immobilized on polyacrylonitrile hollow fibers
22
-
-
assay at room temperature
25
-
-
immobilized enzyme on oxygen electrode
30
-
Nocardia rhodochrous
-
-
30
-
Q56DL0
assay at
30
-
-
silk mat-immobilized enzyme
30
-
Nocardia rhodochrous
-
-
37
-
H9NJ43, H9NJ52
assay at; assay at
40
42
Corynebacterium cholesterolicum
-
-
40
50
Q56DL0
-
40
-
Nocardia erythropolis
-
enzyme after micellization
40
-
-
reaction with cholesterol, enzyme CO2
40
-
Q93JS8
-
45
50
Q55020
-
50
-
Q157H4
-
55
-
-
cholesterol oxidase II
60
-
-
wild-type and S103T, V121A, R135H and V145E mutants
60
-
-
strain ST-200
60
-
-
reaction with cholesterol, enzyme CO1
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
50
-
4C: 84% of maximal activity, 50C: about 50% of maximal activity
10
80
-
about 25% of maximal activity at 10C and 80C
13
44
Nocardia rhodochrous
-
about 50% of maximal activity at 13C and 44C
20
60
-
activity range, profile overview
20
70
-
about 50% of maximal activity at 20C and 70C
25
45
-
the oxygen depletion rate is increased with increasing temperature from 25C to 40C but it decreases sharply as the temperature increases further to 45C
30
55
-
30C: about 65% of maximal activity, 55C: about 60% of maximal activity, reaction with cholesterol, enzyme CO2
30
70
-
30C: about 85% of maximal activity, 70C: about 80% of maximal activity
33
60
-
constitutive enzyme, 50% of maximal activity at 33C, 70% at 60C, inducible enzyme, 50% of maximal activity at 33C and 60C
35
48
A7LGL0
ChoL retains more than 80% activity in the temperature range 35-48C
35
75
-
about 50% of maximal activity at 35C and at 75C, reaction with cholesterol, enzyme CO1
40
80
-
40C: about 70% of maximal activity, 80C: about 40% of maximal activity
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.9
-
-
isoelectric focusing with carrier ampholites pH 4-6, cholesterol oxidase II
5.7
-
C5II17, -
calculated from amino acid sequence
7
-
-
isoelectric fucusing, pH-gradient 3.5-10.0
8.5
-
A7LGL0
calculated from amino acid sequence
9
-
Q157H4
pI-value about 9.0, isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
Nocardia erythropolis
-
-
Manually annotated by BRENDA team
-
the strain reaches its maximal utilization of cholesterol as the only C source for production of extracellular cholesterol oxidase
Manually annotated by BRENDA team
additional information
-
enzyme production reaches its maximum by incubation at 30C for 12 d
Manually annotated by BRENDA team
additional information
-
Streptomyces parvus shows markedly high cho activity in culture broth
Manually annotated by BRENDA team
additional information
-
effect of carbon and nitrogen sources on COD production, highest activity on lactose and sucrose and on yeast extract, respectively, overview
Manually annotated by BRENDA team
additional information
Streptomyces parvus 13647 J
-
Streptomyces parvus shows markedly high cho activity in culture broth
-
Manually annotated by BRENDA team
additional information
Streptomyces sp. R-6
-
effect of carbon and nitrogen sources on COD production, highest activity on lactose and sucrose and on yeast extract, respectively, overview
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
H9NJ43, H9NJ52
; ChoM1 is mainly associated with the cell envelope
Manually annotated by BRENDA team
-
produces both cell-linked and extracellular enzyme in high amount
-
Manually annotated by BRENDA team
-
produces both cell-linked and extracellular enzyme in high amount
-
Manually annotated by BRENDA team
Pseudomonas spp.
-
-
-
Manually annotated by BRENDA team
Streptomyces violascens, Streptoverticillum cholesterolicum
-
-
-
Manually annotated by BRENDA team
H9NJ43, H9NJ52
; ChooM2 is mainly extracellular and soluble
-
Manually annotated by BRENDA team
Bacillus sp. SFF34, Bordetella sp. B4, Rhodococcus sp. CECT3014, Streptomyces parvus 13647 J, Streptomyces sp. R-6
-
-
-
-
Manually annotated by BRENDA team
Arthrobacter sp., Mycobacterium sp., Nocardia erythropolis, Nocardia rhodochrous, Rhodococcus equi
-
-
Manually annotated by BRENDA team
Arthrobacter sp., Mycobacterium sp., Nocardia erythropolis, Nocardia rhodochrous, Rhodococcus equi
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Streptomyces sp. (strain SA-COO)
Streptomyces sp. (strain SA-COO)
Streptomyces sp. (strain SA-COO)
Streptomyces sp. (strain SA-COO)
Streptomyces sp. (strain SA-COO)
Streptomyces sp. (strain SA-COO)
Streptomyces sp. (strain SA-COO)
Streptomyces sp. (strain SA-COO)
Streptomyces sp. (strain SA-COO)
Streptomyces sp. (strain SA-COO)
Streptomyces sp. (strain SA-COO)
Streptomyces sp. (strain SA-COO)
Streptomyces sp. (strain SA-COO)
Streptomyces sp. (strain SA-COO)
Streptomyces sp. (strain SA-COO)
Streptomyces sp. (strain SA-COO)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30000
-
-
gel filtration
32500
-
-
gel filtration, sedimentation equilibrium
45000
-
-
gel filtration
46500
-
-
cholesterol oxidase II, gel filtration
48000
-
-
gel filtration
53000
-
-
SDS-PAGE, sedimentation equilibrium, amino acid analysis
55000
-
Q55020
-
55000
-
Q157H4
SDS-PAGE
56000
-
-
SDS-PAGE, gel filtration
56000
-
Pseudomonas sp., Streptoverticillium cholesterolieum
-
-
57000
-
Corynebacterium cholesterolicum, Pimelobacter simplex
-
-
58000
-
-
gel filtration
58000
-
Q55020
-
58900
-
A7LGL0
calculated from amino acid sequence
59000
-
A7LGL0
SDS-PAGE
60000
-
Q93RE1
-
63000
-
Q56DL0
-
63300
-
C5II17, -
calculated from amino acid sequence
65100
-
-
analytical ultracentrifugation
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 60000, SDS-PAGE
?
-
x * 55000, wild-type and mutant enzymes V145Q, V145E, S379A and S379V, SDS-PAGE
?
-
x * 50000, SDS-PAGE
?
-
x * 55000, SDS-PAGE
?
-
x * 55000, SDS-PAGE
?
H9NJ43, H9NJ52
x * 57900, recombinant His-tagged isozyme ChoM2, SDS-PAGE x * 55700, recombinant His-tagged isozyme ChoM2 lacking the signal peptide, SDS-PAGE; x * 64300, recombinant His-tagged isozyme ChoM1, SDS-PAGE
?
-
x * 55000, SDS-PAGE
?
-
x * 62000, SDS-PAGE
?
Bordetella sp. B4, Streptomyces parvus 13647 J
-
x * 55000, SDS-PAGE
-
?
Streptomyces sp. R-6
-
x * 62000, SDS-PAGE
-
monomer
-
1 * 53000, SDS-PAGE
monomer
-
1 * 56000, SDS-PAGE
monomer
-
1 * 55000, SDS-PAGE
monomer
-
1 * 53000, SDS-PAGE
monomer
-
1 * 36000, enzyme CO1, SDS-PAGE; 1 * 37000, enzyme CO2, SDS-PAGE
monomer
-
1 * 58000, SDS-PAGE
monomer
-
structural determinants of the enzymes' stability
monomer
Bacillus sp. SFF34
-
1 * 36000, enzyme CO1, SDS-PAGE; 1 * 37000, enzyme CO2, 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
Brevibacterium sp. M201008
-
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
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
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
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
crystals of recombinant His-tagged enzyme, vapor diffusion by hanging drop, space group P21
-
rod shaped crystals with bright yellow color
-
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
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3
11
-
30C, 1 h, stable
3
11
-
30C, 1 h
4
10
-
37C, 30 min, stable
4
10
-
37C, 30 min
4
10
-
4C, 4 h
4
11
Q93RE1
30C, 1 h
4
11
-
60C, 1 min
4
12.5
Streptoverticillium cholesterolieum
-
22C, 1 h
4
8
Q55020
25C, 20 h
4
-
-
purified enzyme, 4C for 48 h, 80% activity remaining
5
10
-
37C, 30 min, stable
5
6.5
-
60C, 60 min, stable
5
7
-
stable at
5
8
-
60C, 1 min, stable
5
8
-
50C, 1 h, stable
5
8.5
-
60 min, more than 80% of the CHO-U activity remains
5
9
Corynebacterium cholesterolicum
-
30C, 1 h
5
-
-
most stable at, enzyme CO2
5
-
-
purified enzyme, 4C for 48 h, completely stable
6
10
-
30C, 2 h, stable
6
10
-
purified enzyme, 4C for 48 h, 80% activity remaining
6
-
-
most stable at
7.5
-
-
60C, 60 min, about 10% loss of activity
8
-
-
60C, 60 min, about 40% loss of activity
10
-
-
60C, 1 min, 25% loss of activity
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
50
-
strain ST-200, 27% activity lost after incubation at 60C, complete loss of activity at 70C
4
65
-
purified enzyme, stable at
30
40
-
purified enzyme, stable at
40
60
A7LGL0
the enzyme is stable below 40C without obvious inactivation after 6 h of incubation. When the temperature exceeds 50C, the ChoL activity rapidly decreases. The enzyme retains approximately 40% of its initial activity after incubation for 6 h at 50C and 17% after incubation for 1 h at 60C
45
55
Q157H4
after 1 h of incubation, more than 70 and 50% of activity remains at 45 and 55C, respectively
50
60
Corynebacterium cholesterolicum
-
96% activity after 30 min at 50C, 6% activity after 30 min at 60C
50
-
Nocardia rhodochrous
-
60 h, about 25% loss of activity
50
-
-
pH 7.0, 30 min, stable
50
-
-
pH 7.0, 1 h, 10% loss of activity
50
-
-
60 min, stable
50
-
-
240 min, enzyme retains 99% of its activity
50
-
-
purified enzyme, 90% or 80% activity remaining after 1 h or 2 h, respectively
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 55C
55
-
Q55020
less than 50% activity after 15 min at 55C
55
-
-
purified enzyme, 30 min, 68% activity remaining
60
85
-
the enzyme retains more than 90% of its original activity after incubation for 240 min at 60C, 90% activity after 1 h at 80C, and 80% activity after 30 min at 85C
60
-
-
pH 7.0, 30 min, 19% loss of activity
60
-
-
50% loss of activity after 10 min
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
60
-
-
1 h, about 10% loss of activity, enzyme CO1; 1 h, about 10% loss of activity, enzyme CO2
60
-
-
pH 7.0, 1 h, 82% loss of activity
60
-
-
pH 7.0, 60 min, about 10% loss of activity
60
-
-
pH 6.0, 7 h, approximately 65% loss of activity of CHO-U
60
-
-
240 min, enzyme retains 87% of its activity
60
-
-
purified enzyme, 30 min, 66% activity remaining
60
-
-
purified enzyme, 20% activity remaining after 2 h
65
-
-
purified enzyme, 30 min, 46% activity remaining
70
80
Q93RE1
70% residual activity after 30 min at 70C, complete loss of activity after 30 min at 80C
70
80
-
70% activity after 30 min at 70C, complete loss of activity after 30 min at 80C
70
-
-
pH 7, 30 min, about 94% loss of activity
70
-
-
30 min, 15% loss of activity; 5 min, no loss of activity
70
-
-
20% activity lost after incubation for 30 min
70
-
-
pH 7.0, 10 min, about 55% loss of activity
70
-
-
pH 6.0, 1 h, 40% loss of activity of CHO-U
70
-
-
10% activity after 1 h at 70C
75
-
-
purified enzyme, 30 min, 14% activity remaining
80
-
Nocardia rhodochrous
-
5 min, about 70% loss of activity
80
-
-
60 min, the enzyme retains 90% of its activity
85
-
-
30 min, 20% loss of activity
90
-
-
30 min, 72% loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
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
-
stable in nonionic detergents over a wide range. More than 90% of activity remains after 60 min at 60C, 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 60C, 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
-
after being reused six times, the enzyme immobilized on polyacrylonitrile hollow fibers retains more than 80% of its activity
-
bile salts stabilize
-
long-chain primary alcohols stabilize
-
SDS, 0.2 mM, stabilizes
-
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
-
ORGANIC SOLVENT
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Acetone
-
37C, 24 h, 1 ml organic solvent added to 2 ml culture filtrate, 90% loss of activity
Acetone
-
the enzyme is unstable in 50% (v/v) acetone; the enzyme remains stable after incubation in 50% (v/v) for 24 h at 37C
Acetone
-
6% activity remaining, pH 7.0, 37C, 24 h, with mechanical shaking
Acetone
-
6% activity remaining, pH 7.0, 37C, 24 h, with mechanical shaking
-
benzene
-
37C, 24 h, 1 ml organic solvent added to 2 ml culture filtrate, stable
benzene
-
127% activity remaining, pH 7.0, 37C, 24 h, with mechanical shaking
Butanol
-
37C, 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 37C
Butanol
-
77% activity remaining, pH 7.0, 37C, 24 h, with mechanical shaking
Butanol
-
77% activity remaining, pH 7.0, 37C, 24 h, with mechanical shaking
-
chloroform
-
37C, 24 h, 1 ml organic solvent added to 2 ml culture filtrate, stable
chloroform
-
96% activity remaining, pH 7.0, 37C, 24 h, with mechanical shaking
cyclohexane
-
119% activity remaining, pH 7.0, 37C, 24 h, with mechanical shaking
cyclooctane
-
37C, 24 h, 1 ml organic solvent added to 2 ml culture filtrate, stable
dimethyl sulfoxide
-
37C, 24 h, 1 ml organic solvent added to 2 ml culture filtrate, stable
dimethyl sulfoxide
-
88% activity remaining, pH 7.0, 37C, 24 h, with mechanical shaking
DMSO
-
the enzyme remains stable after incubation in 50% (v/v) for 24 h at 37C
Emal 20CM
-
the enzyme is relatively tolerant to treatment with Emal 20CM even at 60C
Ethanol
-
37C, 24 h, 1 ml organic solvent added to 2 ml culture filtrate, stable
Ethanol
-
the enzyme remains stable after incubation in 50% (v/v) for 24 h at 37C
Ethanol
-
5% activity remaining, pH 7.0, 37C, 24 h, with mechanical shaking
Ethanol
-
5% activity remaining, pH 7.0, 37C, 24 h, with mechanical shaking
-
Ethyl acetate
-
37C, 24 h, 1 ml organic solvent added to 2 ml culture filtrate, stable
Ethyl acetate
-
the enzyme remains stable after incubation in 50% (v/v) for 24 h at 37C
Ethyl acetate
-
93% activity remaining, pH 7.0, 37C, 24 h, with mechanical shaking
Ethyl acetate
-
93% activity remaining, pH 7.0, 37C, 24 h, with mechanical shaking
-
isopropanol
-
37C, 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 37C
Methanol
-
37C, 24 h, 1 ml organic solvent added to 2 ml culture filtrate, stable
Methanol
-
the enzyme remains stable after incubation in 50% (v/v) for 24 h at 37C
Methanol
-
4% activity remaining, pH 7.0, 37C, 24 h, with mechanical shaking
p-xylene
-
37C, 24 h, 1 ml organic solvent added to 2 ml culture filtrate, stable
propan-2-ol
-
the activity of the enzyme is rapidly inactivated in the presence of 30% (v/v) propan-2-ol at 25C
SDS
-
the enzyme is relatively tolerant to treatment with SDS after incubation for 1 h at 30C
sodium cholate
-
the enzyme is stable at 50% (v/v) sodium cholate after incubation for 1 h at 30C
sodium cholate
A9QAE7
the enzyme is stable in sodium cholate after incubation for 1 h at 30C
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 60C
sodium cholate
uncultured gamma proteobacterium Y-134
-
the enzyme retains more than 80% of its original activity in 0.5% (v/v) sodium cholate after incubation for 1 h at 60C
-
sodium dodecyl sarcosinate
-
the enzyme is relatively tolerant to treatment with sodium dodecyl sarcosinate even at 60C
sodium laurylbenzenesulfonate
-
the enzyme is relatively tolerant to treatment with sodium laurylbenzenesulfonate after incubation for 1 h at 30C
sodium polyoxyethylene alkyl ether sulfate
-
the enzyme is stable at 50% (v/v) sodium polyoxyethylene alkyl ether sulfate after incubation for 1 h at 30C
sodium polyoxyethylene alkyl ether sulfate
A9QAE7
the enzyme is stable in sodium polyoxyethylene alkyl ether sulfate after incubation for 1 h at 30C
toluene
-
37C, 24 h, 1 ml organic solvent added to 2 ml culture filtrate, stable
Triton X-100
-
the enzyme is stable at 50% (v/v) Triton X-100 after incubation for 1 h at 30C
Triton X-100
A9QAE7
the enzyme is stable in Triton X-100 after incubation for 1 h at 30C
Triton X-405
-
the enzyme is stable at 50% (v/v) Triton X-405 after incubation for 1 h at 30C
Triton X-405
A9QAE7
the enzyme is stable in Triton X-405 after incubation for 1 h at 30C
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 60C
Triton X-405
uncultured gamma proteobacterium Y-134
-
the enzyme retains more than 80% of its original activity in 0.5% (v/v) Triton X-405 after incubation for 1 h at 60C
-
Tween 20
-
the enzyme is stable at 50% (v/v) Tween 20 after incubation for 1 h at 30C
Tween 20
A9QAE7
the enzyme is stable in Tween 20 after incubation for 1 h at 30C
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, 37C, 24 h, with mechanical shaking
Methanol
-
4% activity remaining, pH 7.0, 37C, 24 h, with mechanical shaking
-
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
Streptomyces sp. R-6
-
the enzyme shows moderate stability towards all organic solvents except acetone, benzene and chloroform. The activity increases in presence of isopropanol and ethanol
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
0-5C, crystallized enzyme in lyophilized state, in the dark, stable for at least 10 months
-
4C, 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
-
4C, 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
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
native extracellular enzyme from medium 12fold to homogeneity by ammonium sulfate fractionation, dialysis, ultrafiltration, anion exchange chromatography and gel filtration
-
HiTrap Ni-chelating column chromatography
-
ammonium sulfate, DEAE-cellulose, butyl-toyopearl
-
DEAE-Sepharose column chromatography
-
overview: purification procedures
Nocardia erythropolis
-
inducible and constitutive enzyme
-
choleterylglycine-CM-cellulose; DEAE-cellulose, cholesterol affinity column, Sephadex G-150
-
strain ST-200, ammonium sulfate, DEAE-cellulose, butyl-toyopearl, Sephadex G-100
-
ammonium sulfate, ion-exchange chromatography, gel filtration
-
partially purified by precipitation with ammonium sulfate
-
to purify the recombinant enzyme, 500 mg cholesterol is added to 50 ml of crude extract, and then incubated for 2 h at 4C followed by centrifugation at 10000g for 10 min
Q157H4
native extracellular enzyme 18fold by anion exchange chromatography and gel filtration
-
butyl-Sepharose column chromatography and DEAE-cellulose column chromatography
-
native extracellular enzyme 14.3fold by ammonium sulfate fractionation and 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
-
wild-type and mutant enzymes
-
wild-type and mutant enzymes V145Q, V145E, S379A and S379V
-
Ni2+-chelating Sepharose column chromatography
A7LGL0
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
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
-
the cholesterol oxidase gene, cloned in the vector pET-28a, is overexpressed in Escherichia coli BL21-CodonPlus
Q2I2N2
cholesterol oxidase II, expression in Escherichia coli MM294/pnH10
-
expressed in Escherichia coli BL21(DE3)pLysS cells
-
expression in Escherichia coli, His-tagged enzyme
-
expression in Streptomyces lividans
-
expression in Escherichia coli
-
expressed in Escherichia coli BL21 cells
-
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
H9NJ43, H9NJ52
gene choF, DNA and amino acid sequence determination and analysis, expression in Escherichia coli and Pichia pastoris
Q56DL0
expressed in Escherichia coli BL21(DE3)pLysS cells
Q157H4
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
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cloning, sequencing and analysis of partial segment of cholesterol oxidase, the pTZ57R/T vector is used for molecular cloning
Q1HKZ6
expressed in Escherichia coli BL21(DE3)pLysS cells
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expression in Escherichia coli
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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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ChoL, a fragment of a cholesterol oxidase is expressed in Escherichia coli BL21(DE3) plysS cells
A7LGL0
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
E311D
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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
-
exchange prevents formation of histidyl-FAD bond
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
E361A
-
site-directed mutagenesis, the mutant shows no dehydrogenase activity
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
F359A
-
site-directed mutagenesis, the dehydrogenase/oxidase ratio is 12fold increased compared with the ratio for the wild-type enzyme
F359W
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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
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turnover number for cholesterol is decreased about 2600fold compared to wild-type enzyme
H447E/E361Q
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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 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
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
L117P
-
mutant enzyme without activity
L119A
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specific activity is similar to that of the wild-type enzyme
L119F
-
specific activity is similar to that of the wild-type enzyme
N485A
-
site-directed mutagenesis, the mutant shows no dehydrogenase activity
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
N485L
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the kcat of N485D is diminished about 1110times compared with that of wild type, while the apparent Km value is minimally affected
P357N
-
specific activity is similar to that of the wild-type enzyme
Q286R
-
specific activity is similar to that of the wild-type enzyme
R135H
-
random mutagenesis
S103T
-
random mutagenesis
S279R
-
mutant enzyme without activity on cholesterol and pregnenolone
S379D
-
mutant enzyme without activity on cholesterol and pregnenolone
S379T
-
specific activity is similar to that of the wild-type enzyme
V121A
-
random mutagenesis
V124A
-
site-directed mutagenesis, the dehydrogenase/oxidase ratio is 30fold increased compared with the ratio for the wild-type enzyme
V145E
-
random mutagenesis
V145Q
-
specific activity is similar to that of 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
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site-directed mutagenesis, the dehydrogenase/oxidase ratio is 3fold increased compared with the ratio for 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
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N485L
-
the kcat of N485D is diminished about 1110times compared with that of wild type, while the apparent Km value is minimally affected
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R135H
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random mutagenesis
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S103T
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random mutagenesis
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V121A
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random mutagenesis
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H69A
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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
additional information
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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
H9NJ43, H9NJ52
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; 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
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engineered ChOx to improve activity and alter specifity
M122A
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site-directed mutagenesis, the dehydrogenase/oxidase ratio is 26fold increased compared with the ratio for the wild-type enzyme
additional information
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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
V145E
-
random mutagenesis
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additional information
Streptomyces violascens, Streptoverticillum cholesterolicum
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engineered ChOx to improve activity and alter specificity
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
COMMENTARY
LITERATURE
agriculture
-
recombinant expression in plants gives insect resistance
biotechnology
-
biocatalysis, industrial steroid drug production, steroid production as diagnostic tool
diagnostics
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analytic tool for determining cholesterol in various samples
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
agriculture
-
recombinant expression in plants gives insect resistance
analysis
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the enzyme can be used as cholesterol biosensor co-immobilized with cholesterol esterase on oxygen electrodes, determination of total cholesterol in food samples
biotechnology
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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
diagnostics
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analytic tool for determining cholesterol in various samples
medicine
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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
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
medicine
Corynebacterium cholesterolicum
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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
agriculture
-
recombinant expression in plants gives insect resistance
biotechnology
-
biocatalysis, industrial steroid drug production, steroid production as diagnostic tool
diagnostics
-
analytic tool for determining cholesterol in various samples
medicine
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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
agriculture
Nocardia erythropolis
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recombinant expression in plants gives insect resistance
biotechnology
Nocardia erythropolis
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biocatalysis, industrial steroid drug production, steroid production as diagnostic tool
diagnostics
Nocardia erythropolis
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analytic tool for determining cholesterol in various samples
medicine
Nocardia erythropolis
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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
agriculture
Nocardia rhodochrous
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recombinant expression in plants gives insect resistance
biotechnology
Nocardia rhodochrous
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biocatalysis, industrial steroid drug production, steroid production as diagnostic tool
diagnostics
Nocardia rhodochrous
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analytic tool for determining cholesterol in various samples
medicine
Nocardia rhodochrous, Nocardia sp., Pimelobacter simplex
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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
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
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the cholesterol oxidase-immobilized polyacrylonitrile hollow fiber may have an industrial or medical application for cholesterol determination or oxidation
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
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
agriculture
Pseudomonas spp.
-
recombinant expression in plants gives insect resistance
biotechnology
Pseudomonas spp.
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biocatalysis, industrial steroid drug production, steroid production as diagnostic tool
diagnostics
Pseudomonas spp.
-
analytic tool for determining cholesterol in various samples
agriculture
-
recombinant expression in plants gives insect resistance
biotechnology
-
biocatalysis, industrial steroid drug production, steroid production as diagnostic tool
diagnostics
-
analytic tool for determining cholesterol in various samples
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
Rhodococcus sp. GK1
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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
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agriculture
-
recombinant expression in plants gives insect resistance
biotechnology
-
biocatalysis, industrial steroid drug production, steroid production as diagnostic tool
diagnostics
-
analytic tool for determining cholesterol in various samples
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
diagnostics
-
the enzyme is used to determine cholesterol in food and blood serum by coupling of the enzyme with peroxidase
diagnostics
Streptomyces parvus 13647 J
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the enzyme is used to determine cholesterol in food and blood serum by coupling of the enzyme with peroxidase
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agriculture
-
strain A19249, enzyme exhibits a potent insecticidal activity
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
-
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
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
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
agriculture
Streptomyces sp. A19249
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strain A19249, enzyme exhibits a potent insecticidal activity
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agriculture
-
recombinant expression in plants gives insect resistance
biotechnology
-
biocatalysis, industrial steroid drug production, steroid production as diagnostic tool
diagnostics
-
analytic tool for determining cholesterol in various samples
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
agriculture
Streptoverticillum cholesterolicum
-
recombinant expression in plants gives insect resistance
biotechnology
Streptoverticillum cholesterolicum
-
biocatalysis, industrial steroid drug production, steroid production as diagnostic tool
diagnostics
Streptoverticillum cholesterolicum
-
analytic tool for determining cholesterol in various samples
agriculture
-
recombinant expression in plants gives insect resistance
biotechnology
-
biocatalysis, industrial steroid drug production, steroid production as diagnostic tool
diagnostics
-
analytic tool for determining cholesterol in various samples
agriculture
uncultured gamma proteobacterium Y-134
-
recombinant expression in plants gives insect resistance
-
biotechnology
uncultured gamma proteobacterium Y-134
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biocatalysis, industrial steroid drug production, steroid production as diagnostic tool
-
diagnostics
uncultured gamma proteobacterium Y-134
-
analytic tool for determining cholesterol in various samples
-