Developing promiscuous glycosidases for glycoside synthesis: residues W433 and E432 in Sulfolobus solfataricus beta-glycosidase are important glucoside- and galactoside-specificity determinants.

Journal article

Two residues that have been implicated in determining the substrate specificity of the thermophilic beta-glycosidase from the archaeon Sulfolobus solfataricus (SsbetaG), a member of the glycosyl hydrolase family 1, have been mutated by site-directed mutagenesis so as to create more versatile catalysts for carbohydrate chemistry. The wild-type and mutated sequences were expressed in E. coli with a His(7)-tag to allow one-step chromatographic purification. The E432C and W433C mutations removed ...

Expand abstract

Authors: Hancock, S; Corbett, K; Fordham-Skelton, A; Gatehouse, J; Davis, B

• Publication status: Published
• Journal: Chembiochem : a European journal of chemical biology
• Volume: 6
• Issue: 5
• Pages: 866-875
• Publication date: 2005-05-01
• DOI: 10.1002/cbic.200400341
• EISSN: 1439-7633
• ISSN: 1439-4227
• Language: English
• Keywords: Methylation; Glutamic Acid; Amino Acid Sequence; Glucosidases; Sequence Alignment; Galactose; Alkylation; Molecular Sequence Data; Glycosylation; Kinetics; Protein Structure, Tertiary; Glucose; Mutation; Substrate Specificity; Tryptophan; Sulfolobus solfataricus