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Carbohydrate Binding Module Family 101
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| CAZy DB link | |
| http://www.cazy.org/CBM101.html |
Ligand specificities
The first characterized member in the CBM101 family is WfCBM101 [1]. The CBM WfCBM101 could bind to agarose and displayed a weak affinity to porphyran (Fig. 1). While it was incapable of binding to the other examined polysaccharides, including κ-carrageenan, ι-carrageenan, alginate, sulfated fucan, chondroitin sulfate A sodium salt, hyaluronic acid, or pectin. Furthermore, WfCBM101 could bind to agarose tetrasaccharide, but not to porphyran tetrasaccharide. It was reported that the backbone of porphyran consists of approximately 30% characteristic structural units of agarose [2]. It was thus speculated that the weak affinity of WfCBM101 to porphyran was attributed to the structural heterogeneity of porphyran.
Structural Features
The predicted structure by AlphaFold2 showed that WfCBM101 displays a typical β-sandwich fold.
Functionalities
To evaluate the feasibility of WfCBM101 as a tool in the in situ investigation of porphyran, a fluorescent probe was constructed by fusing WfCBM101 with a green fluorescent protein. The in situ visualization of agarose in red alga Gelidium amansii was realized by utilizing the fluorescent probe [1]. Taking WfCBM101 as the query sequence, 15 modules were retrieved from the NCBI database by the BLASTP program (E-value < e-5). There are eight modules adjacent to catalytic domains which are divided into the GH16_16 subfamily or GH86 family respectively. According to the CAZy database, the GH16_16 subfamily and GH86 family members exhibit the activity for degrading agarose. It was thus implied that these eight modules might bind to agarose, which requires further investigation.
Family Firsts
- First Identified
The first member WfCBM101 is a component of a GH86 β-agarase (unpublished data) from a marine bacterium Wenyingzhuangia fucanilytica CZ1127T [3].
- First Structural Characterization
No three-dimensional structure has been solved in this CBM family at present.
References
- Mei X, Zhang Y, Jiang X, Liu G, Shen J, Xue C, Xiao H, and Chang Y. (2024). Discovery and characterization of a novel carbohydrate-binding module: a favorable tool for investigating agarose. J Sci Food Agric. 2024;104(5):2792-2797. DOI:10.1002/jsfa.13164 |
- Chi WJ, Chang YK, and Hong SK. (2012). Agar degradation by microorganisms and agar-degrading enzymes. Appl Microbiol Biotechnol. 2012;94(4):917-30. DOI:10.1007/s00253-012-4023-2 |
- Chen F, Chang Y, Dong S, and Xue C. (2016). Wenyingzhuangia fucanilytica sp. nov., a sulfated fucan utilizing bacterium isolated from shallow coastal seawater. Int J Syst Evol Microbiol. 2016;66(9):3270-3275. DOI:10.1099/ijsem.0.001184 |