CBM3d, a novel subfamily of family 3 carbohydrate-binding modules identified in Cel48A exoglucanase of Cellulosilyticum ruminicola.
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ABSTRACT: Previously, we found that exoglucanase Cel48A from Cellulosilyticum ruminicola H1 bound intensively to Avicel; however, no known carbohydrate-binding module (CBM) was observed in the protein. Bioinformatics suggested that a C-terminal fragment of 127 amino acids, named the Cellulosilyticum-specific paralogous module (CPM), could function in binding. CPM-appended proteins are all putative (hemi)cellulases from Cellulosilyticum spp. In the present work, we demonstrated that Cel48A without the CPM retained only exoglucanase activity and lost the Avicel-binding ability, while the isolated CPM exhibited a high affinity for Avicel. In addition, the CPM bound to chitin, but not to soluble polysaccharides, making it a type A CBM, which binds only insoluble polysaccharides. Phylogenetic analysis cl
SUBMITTER: Cai S
PROVIDER: S-EPMC3187467 | biostudies-literature | 2011 Oct
REPOSITORIES: biostudies-literature
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