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Literature summary for 3.2.1.B26 extracted from

  • Trincone, A.; Giordano, A.; Perugino, G.; Rossi, M.; Moracci, M.
    Highly productive autocondensation and transglycosylation reactions with Sulfolobus solfataricus glycosynthase (2005), Chembiochem, 6, 1431-1437.
    View publication on PubMed
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KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
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 additional information kinetic constants for transglycosylation reactions Saccharolobus solfataricus

Organism

Organism UniProt Comment Textmining
Saccharolobus solfataricus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information mutant enzyme E387G catalyzes transglycosylation reactions. In the transglycosylation reactions, 2-nitrophenyl beta-D-glucopyranoside is used as the donor and different aryl and alkyl mono- and disaccharide substrates containing alpha- and beta-glycosidic linkages are used as acceptors. The formation of the beta-1,3 linkage is observed with acceptors containing the 2-nitrophenyl group, while beta-1,6-disaccharides are predominant with 4-nitrophenyl beta-D-glucoside. When a beta linkage of the acceptor is between two sugars, as for the formation of trisaccharides, the beta-1,3 acceptors possess affinity for the donor active site and are also partially hydrolyzed. The beta-1,4-based acceptor furnish only linear trisaccharides, albeit in very poor yield. The presence of alpha linkages in the acceptors induces beta-1,6 glycosylation despite the nature ofthe aglycons. In these cases, the yield is higher with the increasing lipophilic nature of the aglycon; however, the yield depends on the dimensions and nature of this group. In fact, while maltose as free disaccharide givse very poor yields of trisaccharide products, 33% yield is reached with 4-nitrophenyl alpha-D-glucopyranoside Saccharolobus solfataricus ?
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Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
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 additional information kinetic constants for transglycosylation reactions Saccharolobus solfataricus

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
additional information
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 additional information kinetic constants for transglycosylation reactions Saccharolobus solfataricus