EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
5.1.99.5 | C181A | no residual activity. The secondary and the tertiary structure of the mutant is not significantly affected. Residue Cys181 is responsible for L-isomer recognition and racemization. Binding thermodynamic parameters of different substrates, thermodynamic parameters of the guanidinium hydrochloride-induced denaturation | Sinorhizobium meliloti |
5.1.99.5 | C76A | no residual activity. The secondary and the tertiary structure of the mutant is not significantly affected. Residue Cys76 is responsible for recognition and proton retrieval of D-isomers. Binding thermodynamic parameters of different substrates, thermodynamic parameters of the guanidinium hydrochloride-induced denaturation | Sinorhizobium meliloti |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
5.1.99.5 | Sinorhizobium meliloti | - |
- |
- |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
5.1.99.5 | D-5-monosubstituted hydantoin = L-5-monosubstituted hydantoin | two-base mechanism for the racemization of 5-monosubstituted hydantoins | Sinorhizobium meliloti |
EC Number | Renatured (Comment) | Organism |
---|---|---|
5.1.99.5 | thermodynamic parameters of the guanidinium hydrochloride-induced denaturation of wild-type and mutants C76A, C181A | Sinorhizobium meliloti |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
5.1.99.5 | L-5-methylthioethylhydantoin | - |
Sinorhizobium meliloti | D-5-methylthioethylhydantoin | - |
r | |
5.1.99.5 | L-ethylhydantoin | - |
Sinorhizobium meliloti | D-ethylhydantoin | - |
r | |
5.1.99.5 | L-isopropylhydantoin | - |
Sinorhizobium meliloti | D-isopropylhydantoin | - |
r |