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Literature summary for 5.3.3.1 extracted from
- Crystal structure and enzyme mechanism of Delta 5-3-ketosteroid isomerase from Pseudomonas testosteroni (1998), Biochemistry, 37, 8325-8330.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
- |
Comamonas testosteroni |
| crystals are grown at 12°C from1.3 M ammonium sulfate, 3-5% poly(ethylene glycol)400 and 0.1 M HEPES, pH 7.5 in hanging drops. The crystal structure at 2.3 resolution reveals that the active site environment of the Comamonas testosteroni enzyme is nearly identical to that of Pseudomonas putida enzyme | Comamonas testosteroni |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Comamonas testosteroni | P00947 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Comamonas testosteroni |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | the 2.3 A structure indicates that Phe101 is not a catalytic residue and that Tyr14 and Asp99 COOH should be directly involved in the stabilization of the dienolate intermediate | Comamonas testosteroni | ? | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| KSI | - |
Comamonas testosteroni |
| TI | - |
Comamonas testosteroni |
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