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Difference between revisions of "Carbohydrate Binding Module Family 91"
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== Structural Features == | == Structural Features == | ||
− | '' | + | [[Image:The_structure_of_PxXyl43A.png|thumb|300px|right|'''Figure. The structure of CBM91. '''The prediction structure by Alpha Fold 2 of CBM91(red). This CBM91 is appended to the catalytic domain of''Px''Xyl43A(green).]] |
* '''Fold: β-sandwich ''' | * '''Fold: β-sandwich ''' | ||
* '''Type: Type B ''' | * '''Type: Type B ''' | ||
− | == Functionalities == | + | == Functionalities == | |
− | |||
== Family Firsts == | == Family Firsts == | ||
;First Identified | ;First Identified |
Revision as of 05:35, 20 October 2023
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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 == |
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 |