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

BRENDA support

Literature summary extracted from

  • Motteront, L.; Pilonet, M.S.; Molla, G.; Ghisla, S.; Pollegioni, L.
    Cholesterol oxidase from Brevibacterium sterolicum (2001), J. Biol. Chem., 276, 18024-18030.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.1.3.6 H69A exchange prevents formation of histidyl-FAD bond Brevibacterium sterolicum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.3.6 0.45
-
O2 H69A mutant enzyme, 50 mM phosphate buffer, pH 7.5, 1% thesit, 1% 2-propanol Brevibacterium sterolicum
1.1.3.6 0.47
-
cholesterol H69A mutant enzyme, 50 mM phosphate buffer, pH 7.5, 1% thesit, 1% 2-propanol Brevibacterium sterolicum

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
1.1.3.6 Brevibacterium sterolicum
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.1.3.6 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

Source Tissue

EC Number Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.3.6 cholesterol + O2
-
Brevibacterium sterolicum cholest-4-en-3-one + H2O2
-
?
1.1.3.6 cholesterol + O2
-
Brevibacterium sterolicum cholest-5-en-3-one + H2O2
-
?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.3.6 0.55
-
cholesterol H69A mutant enzyme, steady state, 50 mM phosphate buffer, 1% thesit, 1% 2-propanol Brevibacterium sterolicum
1.1.3.6 1.6
-
cholesterol H69A mutant enzyme, cholesterol oxidation, 50 mM phosphate buffer, 1% thesit, 1% 2-propanol Brevibacterium sterolicum
1.1.3.6 28
-
5-Cholesten-3-one H69A mutant enzyme, 5-cholesten-3-one isomerization, 50 mM phosphate buffer, 1% thesit, 1% 2-propanol Brevibacterium sterolicum

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.3.6 FAD covalently linked to His69 in a second enzyme form Brevibacterium sterolicum