Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.1.3.6 extracted from

  • Pollegioni, L.; Wels, G.; Pilone, M.S.; Ghisla, S.
    Kinetic mechanisms of cholesterol oxidase from Streptomyces hygroscopicus and Brevibacterium sterolicum (1999), Eur. J. Biochem., 264, 140-151.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.02
-
cholestanol
-
Brevibacterium sterolicum
0.07
-
cholesterol
-
Brevibacterium sterolicum
0.11
-
cholesterol
-
Brevibacterium sterolicum
0.165
-
O2
-
Brevibacterium sterolicum
0.2
-
cholesterol
-
Streptomyces hygroscopicus
0.2
-
pregnenolone
-
Streptomyces hygroscopicus
0.3
-
3beta-hydroxy-androst-5-en-17-one
-
Streptomyces hygroscopicus
0.4
-
pregnenolone
-
Brevibacterium sterolicum
0.5
-
3beta-hydroxy-androst-5-en-17-one
-
Streptomyces hygroscopicus
0.53
-
O2
-
Streptomyces hygroscopicus
0.7
-
cholestanol
-
Streptomyces hygroscopicus
0.8
-
cholesterol
-
Streptomyces hygroscopicus
0.8
-
3beta-hydroxy-androst-5-en-17-one
-
Brevibacterium sterolicum
1.2
-
3beta-hydroxy-androst-5-en-17-one
-
Brevibacterium sterolicum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
cholesterol + O2 Streptomyces hygroscopicus
-
cholest-5-en-3-one + H2O2
-
?
cholesterol + O2 Brevibacterium sterolicum
-
cholest-5-en-3-one + H2O2
-
?

Organism

Organism UniProt Comment Textmining
Brevibacterium sterolicum
-
-
-
Streptomyces hygroscopicus
-
-
-

Reaction

Reaction Comment Organism Reaction ID
cholesterol + O2 = cholest-5-en-3-one + H2O2 bifunctional enzyme, catalyzes both the oxidation of DELTA5-ene-3beta hydroxysteroids with a trans A-B ring junction to the corresponding DELTA5-3-ketosteroid with the reduction of oxygen to hydrogen peroxide, and the isomerization to the DELTA4-3-ketosteroid Streptomyces hygroscopicus
cholesterol + O2 = cholest-5-en-3-one + H2O2 bifunctional enzyme, catalyzes both the oxidation of DELTA5-ene-3beta hydroxysteroids with a trans A-B ring junction to the corresponding DELTA5-3-ketosteroid with the reduction of oxygen to hydrogen peroxide, and the isomerization to the DELTA4-3-ketosteroid Brevibacterium sterolicum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1-propanol + O2
-
Streptomyces hygroscopicus propanal + H2O2
-
?
cholestanol + O2
-
Streptomyces hygroscopicus ?
-
?
cholestanol + O2
-
Brevibacterium sterolicum ?
-
?
cholesterol + O2 specific for steroid substrates with an OH group in position 3, preference for steroids with at least a C2 chain at position C17 Streptomyces hygroscopicus cholest-4-en-3-one + H2O2
-
?
cholesterol + O2 specific for steroid substrates with an OH group in position 3, preference for steroids with at least a C2 chain at position C17 Brevibacterium sterolicum cholest-4-en-3-one + H2O2
-
?
cholesterol + O2
-
Streptomyces hygroscopicus cholest-5-en-3-one + H2O2
-
?
cholesterol + O2
-
Brevibacterium sterolicum cholest-5-en-3-one + H2O2
-
?
cyclohexanol + O2
-
Streptomyces hygroscopicus cyclohexanal + H2O2
-
?
epiandrosterone + O2
-
Streptomyces hygroscopicus ?
-
?
ethanol + O2
-
Streptomyces hygroscopicus ethanal + H2O2
-
?
methanol + O2
-
Streptomyces hygroscopicus methanal + H2O2
-
?
pregnenolone + O2
-
Streptomyces hygroscopicus ?
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
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 Brevibacterium sterolicum
0.8
-
3beta-hydroxy-5-androsten-17-one H2O2 production assayed, 100 mM phosphate buffer Brevibacterium sterolicum
7
-
epiandrosterone H2O2 production assayed, 100 mM phosphate buffer Streptomyces hygroscopicus
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 Streptomyces hygroscopicus
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 Brevibacterium sterolicum
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 Streptomyces hygroscopicus
28
-
cholesterol 50 mM phosphate buffer, pH 7.5 Streptomyces hygroscopicus
37
-
cholestanol H2O2 production assayed, 100 mM phosphate buffer Streptomyces hygroscopicus
40
-
cholestanol H2O2 production assayed, 100 mM phosphate buffer Brevibacterium sterolicum
48
-
cholesterol 50 mM phosphate buffer, pH 7.5 Brevibacterium sterolicum
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 Brevibacterium sterolicum
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 Streptomyces hygroscopicus
105
-
cholesterol 50 mM phosphate buffer, pH 7.5, 1% thesit, 10% 2-propanol Brevibacterium sterolicum
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 Brevibacterium sterolicum
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 Streptomyces hygroscopicus
345
-
cholesterol 50 mM phosphate buffer, pH 7.5, 1% thesit, 10% 2-propanol Streptomyces hygroscopicus
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 Streptomyces hygroscopicus

Cofactor

Cofactor Comment Organism Structure
FAD non-covalently bound Streptomyces hygroscopicus
FAD covalently bound in His-tagged recombinant enzyme Brevibacterium sterolicum