Literature summary for 3.2.1.B26 extracted from

Febbraio, F.; Andolfo, A.; Tanfani, F.; Briante, R.; Gentile, F.; Formisano, S.; Vaccaro, C.; Scire, A.; Bertoli, E.; Pucci, P.; Nucci, R.
Thermal stability and aggregation of Sulfolobus solfataricus beta-glycosidase are dependent upon the N-epsilon-methylation of specific lysyl residues: critical role of in vivo post-translational modifications (2003), J. Biol. Chem., 279, 10185-10194.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Saccharolobus solfataricus

General Stability

General Stability	Organism
in Escherichia coli	Saccharolobus solfataricus
N-epsilon-methylated beta-glycosidase from Sulfolobus solfataricus is characterized by a higher resistance to aggregation and denaturation at physiological pH, in comparison with the unmethylated form recombinantly expressed	Saccharolobus solfataricus

Organism

Organism	UniProt	Comment	Textmining
Saccharolobus solfataricus	-	-	-
Saccharolobus solfataricus MT4	-	-	-

Synonyms

Synonyms	Comment	Organism
SsbetaGly	-	Saccharolobus solfataricus

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
97	98	Tm-value for recombinant enzyme	Saccharolobus solfataricus
98	99	Tm-value for native enzyme	Saccharolobus solfataricus

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Release 2023.1 (January 2023)