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Literature summary for 3.2.1.B26 extracted from

  • D'Auria, S.; Rossi, M.; Nucci, R.; Irace, G.; Bismuto, E.
    Perturbation of conformational dynamics, enzymatic activity, and thermostability of beta-glycosidase from archaeon Sulfolobus solfataricus by pH and sodium dodecyl sulfate detergent (1997), Proteins, 27, 71-79.
    View publication on PubMed
Search for more literature for 3.2.1.B26

Activating Compound

Activating Compound Comment Organism Structure
SDS detergent activation, maximal activity in presence of 0.02% SDS. The SDS activation is marked at low temperature; specifically, at 10°C the SDS causes an activation of 140% with respect to the activity observed at the same temperature and in the absence of detergent. At 70°C the increase of enzyme activity is less than 10%. The enzyme activity is not affected by SDS concentration as high as 5% at each temperature Saccharolobus solfataricus

Organism

Organism UniProt Comment Textmining
Saccharolobus solfataricus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Saccharolobus solfataricus

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
Sbetagly
-
 Saccharolobus solfataricus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
 the fluorescence emission is characterized by a bimodal lifetime distribution, suggesting that the enzyme structure contains rigid and flexible regions, properly located in the macromolecule. The enzyme activity and thermostability appear to be related to the dynamic properties of these regions as evidenced by perturbation studies of the enzyme structure at alkaline pH and by addition of detergents such as SDS. The pH increase affects the protein dynamics with a remarkable loss of thermal stability and activity; these changes occur without any significant variation in the secondary structure as revealed by far-UV dichroic measurements. In the presence of 0.02% (w/v) SDS at alkaline pH, the enzymatic activity and thermostability are recovered. Under these conditions, the conformational dynamics appear to be similar to that evidenced at neutral pH. Further inreases in SDS concentration, at alkaline pH, render the activity and thermostability of beta-glycosidase similar to those observed in the absence of detergent Saccharolobus solfataricus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7 10 the increase of pH from 7.0 to 10.0 causes a strong reduction of the catalytic activity of Sbgly that becomes very low at alkaline pH Saccharolobus solfataricus