Carbohydrate esterases of family 2 are 6-O-deacetylases
| Autor: | Paul Christakopoulos, Christina Vafiadi, Peter Biely, Ján Hirsch, Sarantos Kyriakopoulos, Evangelos Topakas |
|---|---|
| Rok vydání: | 2009 |
| Předmět: |
Magnetic Resonance Spectroscopy
Stereochemistry Carbohydrates Biophysics CE-2 family Xylose Biochemistry Esterase Substrate Specificity Clostridium thermocellum Cellvibrio chemistry.chemical_compound Bacterial Proteins Structural Biology Genetics Cellvibrio japonicus Acetylxylan esterase Molecular Biology Hexoses chemistry.chemical_classification Molecular Structure biology Acetyl esterase Monosaccharides Acetylation Cell Biology Carbohydrate 6-O-Deacetylase biology.organism_classification Transesterification Enzyme chemistry Acetylesterase |
| Zdroj: | FEBS Letters. 584:543-548 |
| ISSN: | 0014-5793 |
| Popis: | Three acetyl esterases (AcEs) from the saprophytic bacteria Cellvibrio japonicus and Clostridium thermocellum, members of the carbohydrate esterase (CE) family 2, were tested for their activity against a series of model substrates including partially acetylated gluco-, manno- and xylopyranosides. All three enzymes showed a strong preference for deacetylation of the 6-position in aldohexoses. This regioselectivity is different from that of typical acetylxylan esterases (AcXEs). In aqueous medium saturated with vinyl acetate, the CE-2 enzymes catalyzed transacetylation to the same position, i.e., to the primary hydroxyl group of mono- and disaccharides. Xylose and xylooligosaccharides did not serve as acetyl group acceptors, therefore the CE-2 enzymes appear to be 6-O-deacetylases. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Plný text