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Literature summary extracted from

  • Sagermann, M.; Ohtaki, A.; Newton, K.; Doukyu, N.
    Structural characterization of the organic solvent-stable cholesterol oxidase from Chromobacterium sp. DS-1 (2010), J. Struct. Biol., 170, 32-40.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.3.6 expressed in Escherichia coli BL21 cells Chromobacterium sp.

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.3.6 crystal screen based on sparse matrix formulation, using 500 mM ammonium sulfate, 1.0 M lithium sulfate and 10 mM sodium citrate Chromobacterium sp.

Organism

EC Number Organism UniProt Comment Textmining
1.1.3.6 Chromobacterium sp. B5MGF8
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.3.6 DEAE-Sepharose column chromatography Chromobacterium sp.

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
-
 Chromobacterium sp. cholest-4-en-3-one + H2O2
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.1.3.6 CHOLOX belongs to the type II cholesterol oxidases Chromobacterium sp.

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.3.6 FAD the FAD cofactor is covalently attached to the protein Chromobacterium sp.