- Abstract:
-
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 - Publication status:
- Published
- Publisher copy:
- 10.1002/cbic.200400341
-
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- Journal:
- Chembiochem : a European journal of chemical biology
- Volume:
- 6
- Issue:
- 5
- Pages:
- 866-875
- Publication date:
- 2005-05-05
- DOI:
- EISSN:
-
1439-7633
- ISSN:
-
1439-4227
- URN:
-
uuid:588c3e1a-51c0-4aa8-bec6-6921622cb5c5
- Source identifiers:
-
33071
- Local pid:
- pubs:33071
- Copyright date:
- 2005
Journal article
Developing promiscuous glycosidases for glycoside synthesis: residues W433 and E432 in Sulfolobus solfataricus beta-glycosidase are important glucoside- and galactoside-specificity determinants.
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