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Literature summary for 1.1.3.6 extracted from

  • Croteau, N.; Vrielink, A.
    Crystallization and preliminary x-ray analysis of cholesterol oxidase from Brevibacterium sterolicum containing covalently bound FAD (1996), J. Struct. Biol., 116, 317-319.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli, His-tagged enzyme Brevibacterium sterolicum

Crystallization (Commentary)

Crystallization (Comment) Organism
crystals of recombinant His-tagged enzyme, vapor diffusion by hanging drop, space group P21 Brevibacterium sterolicum

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Brevibacterium sterolicum
-
-
-

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 Brevibacterium sterolicum

Substrates and Products (Substrate)

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

Cofactor

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