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Literature summary for 4.3.1.18 extracted from

  • Baldassarre, M.; Scire, A.; Tanfani, F.
    Turning pyridoxal-5-phosphate-dependent enzymes into thermostable binding proteins: D-Serine dehydratase from bakers yeast as a case study (2012), Biochimie, 94, 479-486.
    View publication on PubMed

Protein Variants

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

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Temperature Stability [°C]

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

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