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Literature summary for 3.2.1.B26 extracted from

  • D'Auria, S.; Nucci, R.; Rossi, M.; Gryczynski, I.; Gryczynski, Z.; Lakowicz, J.R.
    The beta-glycosidase from the hyperthermophilic archaeon Sulfolobus solfataricus: enzyme activity and conformational dynamics at temperatures above 100 degrees C (1999), Biophys. Chem., 81, 23-31.
    View publication on PubMed
Search for more literature for 3.2.1.B26

Organism

Organism UniProt Comment Textmining
Saccharolobus solfataricus
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-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-nitrophenyl beta-D-galactopyranoside + H2O
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 Saccharolobus solfataricus 2-nitrophenol + beta-D-galactopyranose
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 ?

Synonyms

Synonyms Comment Organism
Sbetagly
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 Saccharolobus solfataricus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
125
-
-
 Saccharolobus solfataricus

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
95 145 95°C: about 45% of maximal activity, 145°C: about 50% of maximal activity Saccharolobus solfataricus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
100
-
 investigation of the activity and conformational dynamics above 100°C. The data indicate a strong correlation between enzyme activity and protein flexibility. In particular, the time-resolved fluorescence data point out that some regions of the protein structure are very sensitive to the temperature increases, gaining a high flexibility degree with temperature. On the other hand, it is also possible to identify local environments of the enzyme structure that still possess a relatively high rigidity at 125°C Saccharolobus solfataricus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.8
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 assay at Saccharolobus solfataricus