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Difference between revisions of "Carbohydrate Binding Module Family 91"
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== Ligand specificities == | == Ligand specificities == | ||
| − | CBM91 bound to oat spelt xylan with ''K''<sub>a</sub> value of 2.0×10<sup>-5</sup> M<sup>-1</sup>, 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 <cite>Ito2022</cite>. | + | CBM91 from ''Paenibacillus xynaniclasticus'' bound to oat spelt xylan with ''K''<sub>a</sub> value of 2.0×10<sup>-5</sup> M<sup>-1</sup>, 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 <cite>Ito2022</cite>. |
== Structural Features == | == Structural Features == | ||
[[Image:The_structure_of_PxXyl43A.png|thumb|300px|right|'''Figure 1. The structure of ''Px''Xyl43A and CBM91. | [[Image:The_structure_of_PxXyl43A.png|thumb|300px|right|'''Figure 1. The structure of ''Px''Xyl43A and CBM91. | ||
'''The prediction structure by Alpha Fold 2 of CBM91(red). This CBM91 is appended to the catalytic domain of ''Px''Xyl43A(green).]] | '''The prediction structure by Alpha Fold 2 of CBM91(red). This CBM91 is appended to the catalytic domain of ''Px''Xyl43A(green).]] | ||
| − | Alpha Fold 2 structure analysis of ''Px''CBM91 exhibited a β-sandwich fold consisted of 12 β-strands | + | Alpha Fold 2 structure analysis of ''Px''CBM91 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 == | == Functionalities == | ||
| − | CBM91 often is connected to the β-xylosidases belonging to glycoside hydrolase family 43 | + | 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 == | == Family Firsts == | ||
| − | ;First Identified | + | ;First Identified:''Px''CBM91 from ''Px''Xyl43A of ''Paenibacillus xynaniclasticus'' strain TW1 <cite>Ito2022</cite>. |
| − | :''Px''CBM91 from ''Px''Xyl43A of ''Paenibacillus xynaniclasticus'' strain TW1 <cite>Ito2022</cite>. | + | ;First Structural Characterization: β-D-xylosidase, a family 43 glycoside hydrolase from ''Clostridium acetobutylicum'' ATCC 824 [{{PDBlink}}1Y7B PDB ID 1Y7B]. |
| − | ;First Structural Characterization | ||
| − | : β-D-xylosidase, a family 43 glycoside hydrolase from ''Clostridium acetobutylicum'' ATCC 824 [{{PDBlink}}1Y7B PDB ID 1Y7B]. | ||
== References == | == References == | ||
Revision as of 01:02, 20 August 2024
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| CAZy DB link | |
| https://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 |