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

BRENDA support

Literature summary extracted from

  • Uwajima, T.; Yagi, H.; Nakamura, S.; Terada, O.
    Isolation and crystallization of extracellular 3beta-hydroxysteroid oxidase of Brevibacterium sterolicum nov. Sp. (1973), Agric. Biol. Chem., 37, 2345-2350.
No PubMed abstract available

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.3.6 rod shaped crystals with bright yellow color 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
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
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
a

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.3.6 17
-
-
 Brevibacterium sterolicum

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
-
 ?

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.3.6 FAD flavoprotein Brevibacterium sterolicum