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Carbohydrate Binding Module Family 91
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CAZy DB link | |
http://www.cazy.org/CBM91.html |
Ligand specificities
CBM91 bind oat spelt xylan with Ka value of 2.0×10-5 M-1, and can bind birchwood xylan. But it does not bind to cellulosic substrates, carboxymethyl-cellulose, ball-milled cellulose and lichnan. So, CBM91 can recognize and bind to insoluble xylan [1].
Structural Features
- Fold: β-sandwich
- Type: Type B
Functionalities
CBM91 often is found in the β-xylosidases, for example GH43. These seem not to need CBMs because the substrates, xylobiose and/or xylo-oligosaccharides, are soluble. So, it is likely that the binding ability may not be involved in β-xylosidase activity of catalytic domain. β-xylosidases would utilize CBM91 as a tool for efficient saccharification by combination with other enzymes and xylanases which release xylobiose and/or xylo-oligosaccharides from insoluble substrates. CBM91 binds to the substrates and would places the catalytic domain at the vicinity of substrates in which substrate concentration is high.
Family Firsts
- First Identified
- CBM91 from 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 |