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Carbohydrate Binding Module Family 91
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http://www.cazy.org/CBM91.html |
Ligand specificities
CBM91 from Paenibacillus xynaniclasticus bound to oat spelt xylan with Ka value of 2.0×10-5 M-1, and bound birchwood xylan. But it did not bind to cellulosic substrates (carboxymethyl-cellulose, ball-milled cellulose and lichnan). Therefore, CBM91 can recognize and bind to insoluble xylan [1].
Structural Features
Alpha Fold 2 structure analysis of PxCBM91 exhibited a β-sandwich fold consisted of 12 β-strands. The concave surface and loops around it connecting the β-strands possesses several hydrophobic amino acid residues, the surface is expected to be the binding site.
Functionalities
CBM91 often is connected to the β-xylosidases belonging to glycoside hydrolase family 43 ([GH43]). CBM91 binds to the substrates and would place the catalytic domain in the vicinity of substrates in which substrate concentration is high. These enzymes would utilize CBM91 as a tool for efficient saccharification in combination with other xylanases which release xylobiose and/or xylo-oligosaccharides from insoluble substrates.
Family Firsts
- First Identified
- PxCBM91 from PxXyl43A of Paenibacillus xynaniclasticus strain TW1 [1].
- First Structural Characterization
- β-D-xylosidase, a family 43 glycoside hydrolase from Clostridium acetobutylicum ATCC 824 PDB ID 1Y7B.
References
- Ito D, Nakano E, Karita S, Umekawa M, Ratanakhanokchai K, and Tachaapaikoon C. (2022). Characterization of a GH Family 43 β-Xylosidase Having a Novel Carbohydrate-binding Module from Paenibacillus xylaniclasticus Strain TW1. J Appl Glycosci (1999). 2022;69(3):65-71. DOI:10.5458/jag.jag.JAG-2022_0001 |