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FEBS Lett. 2010 Feb 5;584(3):543-8. doi: 10.1016/j.febslet.2009.11.095. Epub 2009 Dec 4.

Carbohydrate esterases of family 2 are 6-O-deacetylases.

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Biotechnology Laboratory, School of Chemical Engineering, National Technical University of Athens, Athens, Greece.


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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