http://www.cnr.it/ontology/cnr/individuo/prodotto/ID219359

Protein engineering of the beta-glycosidase from the hyperthermophilic archaeon Sulfolobus solfataricus: Special Publication - mechanisms of glycoside hydrolysis (Articolo in rivista)

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Protein engineering of the beta-glycosidase from the hyperthermophilic archaeon Sulfolobus solfataricus: Special Publication - mechanisms of glycoside hydrolysis (Articolo in rivista) (literal)

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Moracci, M.; Perugino, G.; Trincone, A.; Ciaramella, M.; Rossi, M. (1999)
Protein engineering of the beta-glycosidase from the hyperthermophilic archaeon Sulfolobus solfataricus: Special Publication - mechanisms of glycoside hydrolysis
in Special publication - Royal Society of Chemistry; Royal Society of Chemistry, London (Italia)
(literal)

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Titolo

Protein engineering of the beta-glycosidase from the hyperthermophilic archaeon Sulfolobus solfataricus: Special Publication - mechanisms of glycoside hydrolysis (literal)

Abstract

Glycosyl hydrolases follow two reaction mechanisms, one producing overall retention and the other the inversion of the anomeric configuration of the substrate. Both mechanisms involve two carboxylic groups of Issue Recent Advances the active site highly conserved in each family. The modification of kinetic properties of glycosyl hydrolases in Carbohydrate by protein engineering is an interesting challenge for both basic and applied research. With this approach Bioengineering the retaining mechanism of the ?-glycosidase from the Archaeon Sulfolobus solfataricus (Ss?-gly; E.C. 3.2.1.x) has been characterized in detail through the identification of E206 and E387 as the general acid/base and nucleophile of the reaction, resp. (literal)

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