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Literature summary extracted from
- Hybrid quantum/classical molecular dynamics simulations of the proton transfer reactions catalyzed by ketosteroid isomerase: Analysis of hydrogen bonding, conformational motions, and electrostatics (2009), Biochemistry, 48, 10608-10619.
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 5.3.3.1 | Comamonas testosteroni | P00947 | - |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.3.3.1 | additional information | the reaction occurs by a two-step general acid-base mechanism involving a dienolate intermediate. Hybrid quantum/classical molecular dynamics simulations elucidating the geometrical, conformational, and electrostatic changes occurring during the isomerization reaction catalyzed by KSI, calculation of rate constants and modeling of the KSI active site, overview. Electrostaic and conformational changes during the proton transfer reactions, rearrangements, overview | Comamonas testosteroni | ? | - |
? |  |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 5.3.3.1 | DELTA5-3-ketosteroid isomerase | - |
Comamonas testosteroni |
| 5.3.3.1 | ketosteroid isomerase | - |
Comamonas testosteroni |
| 5.3.3.1 | KSI | - |
Comamonas testosteroni |
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