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Appl. Environ. Microbiol. doi:10.1128/AEM.00876-07
Copyright (c) 2007, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

CelAB, a multifunctional cellulase encoded by Teredinibacter turnerae T7902^T, a culturable symbiont isolated from the wood-boring marine bivalve, Lyrodus pedicellatus

Ocean Genome Legacy, Center for Marine Genomic Research and Conservation, 240 County Rd., Ipswich, MA 01938; Department of Biochemistry, Microbiology, and Molecular Biology, University of Maine, 5735 Hitchner Hall, Orono, ME 04469

^* To whom correspondence should be addressed. Email: distel{at}oglf.org.

	Abstract

We characterized a multifunctional cellulase (CelAB) encoded by the endosymbiont Teredinibacter turnerae T7902^T. CelAB contains two catalytic and two carbohydrate-binding domains, each separated by poly-serine linker regions. CelAB binds cellulose and chitin, degrades multiple complex polysaccharides and displays two catalytic activities, cellobiohydrolase (E.C. 3.2.1.91) and -1,4(3) endoglucanase (E.C. 3.2.1.4).