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1.1.3.6: cholesterol oxidase

This is an abbreviated version!
For detailed information about cholesterol oxidase, go to the full flat file.

Word Map on EC 1.1.3.6

Reaction

cholesterol
+
O2
=
cholest-5-en-3-one
+
H2O2

Synonyms

3beta-hydroxy steroid oxidoreductase, 3beta-hydroxysteroid: oxygen oxidoreductase, 3beta-hydroxysteroid:oxygen oxidoreductase, 3beta-hydroxysterol oxidase, BsChOx, CgChoA, CHO, CHO-U, ChO3, ChoA, choBb, CHOD, ChoG, ChoL, cholesterol oxidase, cholesterol oxidase I, cholesterol oxidase II, cholesterol-O2 oxidoreductase, CHOLOX, choM, ChoM1, ChoM2, choP, ChoRI, ChoRII, ChoS, ChOx, CO, CO1, COase, COD, COD-B, COX, HCEO-forming enzyme, HMPREF0204_11499, oxidase, cholesterol, PimE, ShChOx, type I ChOx

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.3 With oxygen as acceptor
                1.1.3.6 cholesterol oxidase

Organic Solvent Stability

Organic Solvent Stability on EC 1.1.3.6 - cholesterol oxidase

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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acetone
benzene
Butanol
chloroform
cyclohexane
-
119% activity remaining, pH 7.0, 37°C, 24 h, with mechanical shaking
cyclooctane
dimethyl sulfoxide
DMSO
the enzyme remains stable after incubation in 50% (v/v) for 24 h at 37°C
Emal 20CM
Ethanol
Ethyl acetate
isopropanol
Methanol
n-Butanol
-
well tolerated
p-xylene
propan-2-ol
the activity of the enzyme is rapidly inactivated in the presence of 30% (v/v) propan-2-ol at 25°C
sarcosyl
stable and partially or slightly activated in the presence of 0.5% (w/v) detergent
SDS
the enzyme is relatively tolerant to treatment with SDS after incubation for 1 h at 30°C
sodium cholate
sodium dodecyl sarcosinate
the enzyme is relatively tolerant to treatment with sodium dodecyl sarcosinate even at 60°C
sodium laurylbenzenesulfonate
the enzyme is relatively tolerant to treatment with sodium laurylbenzenesulfonate after incubation for 1 h at 30°C
sodium polyoxyethylene alkyl ether sulfate
toluene
Triton X-100
Triton X-405
Tween 20
urea
-
the apoprotein of the mutant H69A lacks the characteristic tertiary structure of the holoprotein and displays larger hydrophobic surfaces. Its urea-induced unfolding does not occur by a simple two-state mechanism and is largely nonreversible. Minor alterations in the flavin binding region are evident between the native and the refolded proteins, and are likely responsible for the low refolding yield observed
xylene
-
93% the activity remaining, pH 7.0, 37°C, 24 h, with mechanical shaking
additional information