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Literature summary for 1.1.3.6 extracted from

  • Volonte, F.; Pollegioni, L.; Molla, G.; Frattini, L.; Marinelli, F.; Piubelli, L.
    Production of recombinant cholesterol oxidase containing covalently bound FAD in Escherichia coli (2010), BMC Biotechnol., 10, 33.
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
biotechnology Cholesterol oxidase has two major biotechnological applications, i.e. in the determination of serum (and food) cholesterol levels and as biocatalyst providing valuable intermediates for industrial steroid drug production Brevibacterium sterolicum

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3)pLysS cells Brevibacterium sterolicum

Organism

Organism UniProt Comment Textmining
Brevibacterium sterolicum
-
-
-

Purification (Commentary)

Purification (Comment) Organism
HiTrap Ni-chelating column chromatography 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
-
?

Cofactor

Cofactor Comment Organism Structure
FAD the type II cholesterol oxidase fully active enzyme contains covalently bound FAD Brevibacterium sterolicum