Thioglycoligases: Mutant Glycosidases for Thioglycoside Synthesis

Engineering of the active site of retaining glycosidases in conjunction with the appropriate modification of their substrates has led to the enzymatic synthesis of thioglycosidic linkages in thiooligosaccharides (see scheme).

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Bibliographic Details
Published inAngewandte Chemie (International ed.) Vol. 42; no. 3; pp. 352 - 354
Main Authors Jahn, Michael, Marles, Jennifer, Warren, R. Antony J., Withers, Stephen G.
Format Journal Article
LanguageEnglish
Published Weinheim WILEY-VCH Verlag 20.01.2003
WILEY‐VCH Verlag
Wiley
Subjects
Amino Acid Substitution
Cellulomonas - enzymology
Chemistry
Chemistry, Multidisciplinary
Chromatography, High Pressure Liquid
enzyme catalysis
Glycoside Hydrolases - chemistry
Glycoside Hydrolases - genetics
Glycoside Hydrolases - metabolism
Glycosylation
Mutagenesis, Site-Directed
Nitrobenzenes - chemistry
Physical Sciences
Rhizobium - enzymology
Science & Technology
thioglycosides
Thioglycosides - chemical synthesis
Thioglycosides - metabolism
COMPLEX
REVERSE HYDROLYSIS
ANALOG
THIOHYDROXIMATE S-GLUCOSYLTRANSFERASE
SUBSTRATE
INHIBITORS
ALPHA-L-FUCOSIDASE
THIO-SUGARS
BETA-GLUCOSIDASE
DERIVATIVES
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Summary:Engineering of the active site of retaining glycosidases in conjunction with the appropriate modification of their substrates has led to the enzymatic synthesis of thioglycosidic linkages in thiooligosaccharides (see scheme).
Bibliography:ArticleID:ANIE200390114
M. J. was financed by a DFG fellowship.
ark:/67375/WNG-RW7N857P-H
istex:5787BC6D31782203DB13CE363AEA64F4AA797066
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.200390114