Carbohydrate Binding Module Family 105

This page is currently under construction. This means that the Responsible Curator has deemed that the page's content is not quite up to CAZypedia's standards for full public consumption. All information should be considered to be under revision and may be subject to major changes.

• Author: Guanchen Liu
• Responsible Curator: Yaoguang Chang

---

CAZy DB link

http://www.cazy.org/CBM105.html

Ligand specificities

The first member of family CBM105 (SoCBM) 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 incapable of binding to other glycosaminoglycanss or polyuronic acid substrates.

Structural Features

Figure 1. Domain analysis of ChABC29So, the parent enzyme of SoCBM.The enzyme consists of a signal peptide (1-21 amino acids), a PL29 domain (66-380 amino acids) and a CBM105 domain (viz., SoCBM; 555-785 amino acids).

An AlphaFold2 model predicts that SoCBM has a β-sandwich fold (Fig.1).

Functionalities

SoCBM is the C-terminus domain of a PL29 enzyme ChABC29So that displays chondroitin sulfate ABC activity, consistent with the SoCBM specificity. Biochemical characterization of ChABC29So and the CBM-truncated enzyme revealed that the SoCBM enhances the catalytic activity, thermostability, and disaccharide proportion in the final enzymatic products of ChABC29So.

Family Firsts

First Identified

The chondroitin sulfate binding SoCBM 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.

References

1. Liu G, Song L, Li J, Song X, Mei X, Zhang Y, Fan C, Chang Y, and Xue C. (2024). Identification and characterization of a chondroitinase ABC with a novel carbohydrate-binding module. Int J Biol Macromol. 2024;271(Pt 1):132518. DOI:10.1016/j.ijbiomac.2024.132518 |