Expanding the Thioglycoligase Strategy to the Synthesis of α-Linked Thioglycosides Allows Structural Investigation of the Parent Enzyme/Substrate Complex

Citations Over TimeTop 10% of 2006 papers

Abstract

For the first time, the thioglycoligase strategy has been successfully applied to alpha-glycosidases. The alpha-thioglycoligases derived from the family 31 glycosidases, alpha-xylosidase from E. coli (YicI) and alpha-glucosidase from Sulfolobus solfataricus, catalyze thioglycoligase reactions using alpha-glycosyl fluorides and deoxythioglycosides as donors and acceptors, respectively, in yields up to 86%. In addition, we describe the Michaelis complex of YicI using one of the thioglycosides as a nonhydrolyzable substrate analogue and discuss the structural insights this yields into the specificity and mechanism of family 31 alpha-glycosidases and the molecular basis of an associated genetic disease.

Related Papers

• → Exo‐glucosidase activity and substrate specificity of the beta‐glycosidase isolated from the extreme thermophile Sulfolobus solfataricus(1993)101 cited
• → A New Archaeal β-Glycosidase from Sulfolobus solfataricus(2010)53 cited
• → The α-l-fucosidase from Sulfolobus solfataricus(2007)16 cited
• → Thermostable β-Glycosidase fromSulfolobus Solfataricus(1994)32 cited
• → Tailoring the substrate specificity of the β‐glycosidase from the thermophilic archaeon Sulfolobus solfataricus(2001)31 cited