AI Article Synopsis
- Three acetyl esterases (AcEs) from the bacteria Cellvibrio japonicus and Clostridium thermocellum were tested for their activity on various sugar substrates.
- These enzymes showed a strong preference for removing acetyl groups from the 6-position of aldohexoses, which is different from how typical acetylxylan esterases operate.
- In a vinyl acetate-saturated solution, the CE-2 enzymes also facilitated transacetylation at the same position, but xylose and xylooligosaccharides did not accept acetyl groups, indicating these enzymes primarily function as 6-O-deacetylases.
Article Abstract
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.
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| http://dx.doi.org/10.1016/j.febslet.2009.11.095 | DOI Listing |
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