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Literature summary for 3.2.1.B26 extracted from

  • Bismuto, E.; Febbraio, F.; Limongelli, S.; Briante, R.; Nucci, R.
    Dynamic fluorescence studies of β-glycosidase mutants from Sulfolobus solfataricus: Effects of single mutations on protein thermostability (2003), Proteins, 51, 10-20.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Saccharolobus solfataricus

Protein Variants

Protein Variants Comment Organism
N97C mutation causes some changes in the structural and dynamic properties as observed by circular dichroism in far- and near-UV light, as well as by frequency domain fluorometry, with a simultaneous loss of thermostability Saccharolobus solfataricus
S101C mutation causes some changes in the structural and dynamic properties as observed by circular dichroism in far- and near-UV light, as well as by frequency domain fluorometry, with a simultaneous loss of thermostability 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-galactopyranose
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
-
Saccharolobus solfataricus 4-nitrophenol + D-glucopyranose
-
?

Synonyms

Synonyms Comment Organism
Sbetagly
-
Saccharolobus solfataricus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
an important role of the sequence segment present only in hyperthermophilic beta-glycosidases, in the thermal adaptation of archaea beta-glycosidases is hypothesized. The thermostabilization mechanism could occur as a consequence of numerous favorable ionic interactions of the 83–124 sequence with the other part of protein matrix that becomes more rigid and less accessible to the insult of thermal-activated solvent molecules Saccharolobus solfataricus