Organism | UniProt | Comment | Textmining |
---|---|---|---|
Streptomyces sp. SA-COO | P12676 | - |
- |
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 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
ChOx | - |
Streptomyces sp. SA-COO |