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Literature summary extracted from
- Binding studies of hydantoin racemase from Sinorhizobium meliloti by calorimetric and fluorescence analysis (2006), Biochim. Biophys. Acta, 1764, 292-298.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 5.1.99.5 | expression in Escherichia coli | Sinorhizobium meliloti |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 5.1.99.5 | C181A | no residual activity | Sinorhizobium meliloti |
| 5.1.99.5 | C181S | less than 1% of wild-type activity | Sinorhizobium meliloti |
| 5.1.99.5 | C76A | no residual activity | Sinorhizobium meliloti |
| 5.1.99.5 | C76S | less than 0.5% of wild-type activity | Sinorhizobium meliloti |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.1.99.5 | D-5-methylthioethyl-hydantoin | determination of thermodynamic binding parameters. Binding of the inhibitor is entropically and thermodynamically favoured | Sinorhizobium meliloti |  |
| 5.1.99.5 | L-5-methylthioethyl-hydantoin | determination of thermodynamic binding parameters. Binding of the inhibitor is entropically and thermodynamically favoured | Sinorhizobium meliloti | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 5.1.99.5 | Sinorhizobium meliloti | - |
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Release 2023.1 (January 2023)
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