Inhibitors | Comment | Organism | Structure |
---|---|---|---|
coumarin 183 | binds tightly in the oxyanion hole of the enzyme and chemically resemble the intermediate in the catalytic cycle. Upon photoexcitation, the pKa of the hydroxyl group changes substantially. This light-activated change in electron density around the photoacid hydroxyl group simulates the change in substrate pKa during the catalytic cycle. When the light-driven reaction analog occurs in the KSI active site, the electrostatic environment changes little | Pseudomonas putida | |
equilenin | binds tightly in the oxyanion hole of the enzyme and chemically resemble the intermediate in the catalytic cycle. Upon photoexcitation, the pKa of the hydroxyl group changes substantially. This light-activated change in electron density around the photoacid hydroxyl group simulates the change in substrate pKa during the catalytic cycle. When the light-driven reaction analog occurs in the KSI active site, the electrostatic environment changes little | Pseudomonas putida |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pseudomonas putida | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | the enzyme catalyzes a C-H bond cleavage and formation through an enolate intermediate. Conversion of the ketone substrate to the enolate intermediate is simulated by a photoacid bound to the active site oxyanion hole. The lack of a significant solvation response in KSI suggests a preorganized active site | Pseudomonas putida | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
DELTA5-3-ketosteroid isomerase | - |
Pseudomonas putida |
ketosteroid isomerase | - |
Pseudomonas putida |
KSI | - |
Pseudomonas putida |