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Literature summary for 3.5.2.2 extracted from
- Stability of immobilized D-hydantoinase from Vigna angularis and repeated cycles of highly enantioenriched production of N-carbamoyl-D-phenylglycines (2004), Amino Acids, 27, 69-74.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Vigna angularis | - |
- |
- |
Storage Stability
| Storage Stability | Organism |
|---|---|
| -5°C, H3BO3/KCl buffer, pH 9.0 | Vigna angularis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| rac-5-p-fluorophenylhydantoin + H2O | immobilized enzyme (linked to aminopropyl glass beads) converts 100% | Vigna angularis | ? | - |
? |  |
| rac-5-p-trifluoromethylphenylhydantoin + H2O | immobilized enzyme (linked to aminopropyl glass beads) converts 87% | Vigna angularis | ? | - |
? | |
| rac-5-phenylhydantoin + H2O | immobilized enzyme (linked to aminopropyl glass beads) converts 100% | Vigna angularis | N-carbamoyl-D-phenylglycine | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| D-hydantoinase | - |
Vigna angularis |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 70 | - |
free enzyme loses 60% of activity in 10 min, immobilized enzyme retains full activity | Vigna angularis |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| additional information | - |
immobilized enzyme is significantly inactivated at pH 10 and pH 8.0 | Vigna angularis |
| 9 | - |
immobilized enzyme is completely stable | Vigna angularis |
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