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Literature summary for 1.1.3.6 extracted from

  • Harb, L.H.; Arooj, M.; Vrielink, A.; Mancera, R.L.
    Computational site-directed mutagenesis studies of the role of the hydrophobic triad on substrate binding in cholesterol oxidase (2017), Proteins, 85, 1645-1655 .
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Streptomyces sp. SA-COO P12676
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cholesterol + O2 a combination of molecular docking and molecular dynamics simulations is used to predict the binding interactions of CHL in the active site of ChOx. The hydrophobic triad residues (Y107A, F444 and Y446A) are observed to change conformation upon CHL binding in the wild-type form of the enzyme, leading to an optimal binding mode for catalytic efficiency Streptomyces sp. SA-COO cholest-5-en-3-one + H2O2
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Synonyms

Synonyms Comment Organism
ChOx
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Streptomyces sp. SA-COO