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The first member of family CBM105 (SoCBM105) was identified in the PL29 multidomain chondroitinase SoChABC29 from Segatella oris [1]. SoCBM105 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 [1].
Structural Features
Figure 1. Domain analysis of SoChABC29, the parent enzyme of SoCBM105 [2]. The enzyme consists of a signal peptide (1-21 amino acids), a PL29 domain (66-380 amino acids) and a CBM105 domain (viz., SoCBM105; 555-785 amino acids).
An AlphaFold2 [2] model predicts that SoCBM105 has a β-sandwich fold (Fig.1).
Functionalities
SoCBM105 is at the C-terminus domain of a PL29 enzyme SoChABC29 that displays chondroitin sulfate ABC activity, consistent with the SoCBM105 specificity [1]. Biochemical characterization of SoChABC29 and the CBM-truncated enzyme revealed that the SoCBM105 enhances the catalytic activity, thermostability, and disaccharide proportion in the final enzymatic products of SoChABC29 [1].
Family Firsts
First Identified
Binding to chondroitin sulfate in the CBM105 family was first characterized and identified for SoCBM105 from the S. orisPL29 chondroitinase [1].
First Structural Characterization
No experimentally determined three-dimensional structure has been solved in this CBM family.
