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Literature summary for 1.1.3.6 extracted from

  • Yu, L.J.; Golden, E.; Chen, N.; Zhao, Y.; Vrielink, A.; Karton, A.
    Computational insights for the hydride transfer and distinctive roles of key residues in cholesterol oxidase (2017), Sci. Rep., 7, 17265 .
    View publication on PubMedView publication on EuropePMC
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Protein Variants

Protein Variants Comment Organism
His447Gln/H447N mutations cause notable decreases in the catalytic activity Streptomyces sp. SA-COO

Organism

Organism UniProt Comment Textmining
Streptomyces sp. SA-COO P12676
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cholesterol + O2 the enzyme catalyzes the oxidation of the substrate via a hydride transfer mechanism and concomitant reduction of the FAD cofactor. The Glu361 residue acts as a catalytic base facilitating the hydride transfer from the substrate to the cofactor Streptomyces sp. SA-COO cholest-5-en-3-one + H2O2
-
 ?

Synonyms

Synonyms Comment Organism
ChOx
-
 Streptomyces sp. SA-COO

Cofactor

Cofactor Comment Organism Structure
FAD
-
 Streptomyces sp. SA-COO