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Carbohydrate Binding Module Family 92
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The first characterized member in the CBM92 family is the Cgk16A-CBM92 from a marine bacterium Wenyingzhuangia aestuarii OF219 . The CBM92 bound specifically to the red algal polysaccharide carrageenan. It was incapable of binding to other polysaccharide components in red algae including agarose, porphyran, and funoran . Meanwhile, the CBM92 displayed no affinity to several anionic polysaccharides, namely pectin, chondroitin sulfates, dermatan sulfate, and sulfated fucans . The Cgk16A-CBM92 showed no significant difference in the affinity to κ- and ι-carrageenan.
No three-dimensional structure has been solved in this CBM family at present. Several conserved residues (e.g., Phe-70, Arg-72, and Phe-75) were discovered through the multiple sequence alignments of Cgk16A-CBM92 and its close homologs , which might be critical for the ligand binding of this CBM.
In the natural context, Cgk16A-CBM92 is a component of the κ-carrageenase Cgk16A  (Fig. 1). It thus might maintain the enzyme near its substrate to improve the enzymatic activity via the proximity effect. To evaluate the feasibility of Cgk16A-CBM92 as a tool in the in situ investigation of carrageenan, a fluorescent probe was constructed by fusing Cgk16A-CBM92 with a green fluorescent protein. The in situ visualization of carrageenan in red alga Kappaphycus alvarezii was realized by utilizing the fluorescent probe .
Members of the CBM92 family are present in different glycoside hydrolase (GH) family sequences, e.g., GH16_17, GH5_54, GH19, and GH95. According to the CAZy database, these GH families comprise enzymes with various substrate specificities, including κ-carrageenase (GH16_17), chitinase (GH19), fucosidase (GH95), and galactosidase (GH95). It indicated that functional diversity might be present within the CBM92 family.
- First Identified
- The first characterized CBM92 member  is a component of the κ-carrageenase Cgk16A , which was discovered from a marine bacterium Wenyingzhuangia aestuarii OF219.
- First Structural Characterization
- No three-dimensional structure has been solved in this CBM family at present.
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