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Carbohydrate Binding Module Family 105
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| CAZy DB link | |
| https://www.cazy.org/CBM105.html |
Ligand specificities
The first member of family CBM105 (SoCBM105) was identified in the PL29 multidomain chondroitinase ChABC29So from Segatella oris [1]. SoCBM bound specifically to chondroitin sulfates (CSs) including CS-A and CS-C, while it was incapable of binding to other glycosaminoglycans or polyuronic acid substrates.
Structural Features
An AlphaFold2 model predicts that SoCBM105 has a β-sandwich fold (Fig.1).
Functionalities
SoCBM105 is at the C-terminus domain of a PL29 enzyme ChABC29So that displays chondroitin sulfate ABC activity, consistent with the SoCBM105 specificity. Biochemical characterization of ChABC29So and the CBM-truncated enzyme revealed that the SoCBM105 enhances the catalytic activity, thermostability, and disaccharide proportion in the final enzymatic products of ChABC29So.
Family Firsts
- First Identified
- The chondroitin sulfate binding SoCBM105 from the S. oris PL29 chondroitinase was the first member of the family to be identified and characterized[1].
- First Structural Characterization
- No experimentally determined three-dimensional structure has been solved in this CBM family.