Protein Variants | Comment | Organism |
---|---|---|
additional information | reduction of the aldimine linkage tethering PLP to recombinant, tagged D-serine dehydratase by treatment with NaBH4 so as to yield an inactive form of the holoenzyme, DsdR, which is further treated with a protease in order to remove the amino-terminal purification tag. Fourier Transform infrared spectroscopic analysis reveals that both the reduced form DsdR and the reduced/detagged form DsdRD maintain the overall secondary structure of wild-type, but feature a significantly increased thermal stability. The observed Tm values for DsdR and for DsdRD shift to 71.5°C and 73.3°C, respectively, resulting in nearly 11° and 13° higher than the one measured for wild-type. Though catalytically inert, DsdRD retains the ability to enantioselectively bind its natural substrate | Saccharomyces cerevisiae |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | - |
- |
- |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
71.5 | - |
inactive form DsdR of the holoenzyme, obtained by reduction of the aldimine linkage tethering PLP to recombinant, tagged D-serine dehydratase by treatment with NaBH4 | Saccharomyces cerevisiae |
73.3 | - |
inactive form DsdR of the holoenzyme, obtained by reduction of the aldimine linkage tethering PLP to recombinant, tagged D-serine dehydratase by treatment with NaBH4, which is further treated with a protease in order to remove the amino-terminal purification tag | Saccharomyces cerevisiae |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
pyridoxal 5'-phosphate | reduction of the aldimine linkage tethering PLP to recombinant, tagged D-serine dehydratase by treatment with NaBH4 so as to yield an inactive form of the holoenzyme, DsdR, which is further treated with a protease in order to remove the amino-terminal purification tag. Fourier Transform infrared spectroscopic analysis reveals that both the reduced form DsdR and the reduced/detagged form DsdRD maintain the overall secondary structure of wild-type, but feature a significantly increased thermal stability. The observed Tm values for DsdR and for DsdRD shift to 71.5°C and 73.3°C, respectively, resulting in nearly 11° and 13° higher than the one measured for wild-type. Though catalytically inert, DsdRD retains the ability to enantioselectively bind its natural substrate | Saccharomyces cerevisiae |