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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.

Author information

1
Biotechnology Laboratory, School of Chemical Engineering, National Technical University of Athens, Athens, Greece. vtopakas@central.ntua.gr

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.

PMID:
19968989
DOI:
10.1016/j.febslet.2009.11.095
[Indexed for MEDLINE]
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