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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.  
+
[[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 curving in the one direction. The concave and loops around it connecting each β-strands possesses several hydrophobic amino acid residues and the surface would be the binding site.
 
Alpha Fold 2 structure analysis of ''Px''CBM91 exhibited a β-sandwich fold consisted of 12 β-strands curving in the one direction. The concave and loops around it connecting each β-strands possesses several hydrophobic amino acid residues and the surface would be the binding site.
 
== Functionalities ==  
 
== 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.
+
CBM91 often is connected to the β-xylosidases belonging to glycoside hydrolase family 43, for example. CBM91 binds to the substrates and would places the catalytic domain at the vicinity of substrates in which substrate concentration is high. These emzymes would utilize CBM91 as a tool for efficient saccharification by 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 ''Paenibacillus xynaniclasticus'' strain TW1 <cite>Ito2022</cite>.
+
:''Px''CBM91 from ''Px''Xyl43A of ''Paenibacillus xynaniclasticus'' strain TW1 <cite>Ito2022</cite>.
 
;First Structural Characterization
 
;First Structural Characterization
 
: β-D-xylosidase, a family 43 glycoside hydrolase from ''Clostridium acetobutylicum'' ATCC 824 [{{PDBlink}}1Y7B PDB ID 1Y7B].  
 
: β-D-xylosidase, a family 43 glycoside hydrolase from ''Clostridium acetobutylicum'' ATCC 824 [{{PDBlink}}1Y7B PDB ID 1Y7B].  

Latest revision as of 07:11, 23 April 2024

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This page is currently under construction. This means that the Responsible Curator has deemed that the page's content is not quite up to CAZypedia's standards for full public consumption. All information should be considered to be under revision and may be subject to major changes.

CAZy DB link
http://www.cazy.org/CBM91.html

Ligand specificities

CBM91 bound to oat spelt xylan with Ka value of 2.0×10-5 M-1, and 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

Figure 1. The structure of PxXyl43A and CBM91. The prediction structure by Alpha Fold 2 of CBM91(red). This CBM91 is appended to the catalytic domain of PxXyl43A(green).

Alpha Fold 2 structure analysis of PxCBM91 exhibited a β-sandwich fold consisted of 12 β-strands curving in the one direction. The concave and loops around it connecting each β-strands possesses several hydrophobic amino acid residues and the surface would be the binding site.

Functionalities

CBM91 often is connected to the β-xylosidases belonging to glycoside hydrolase family 43, for example. CBM91 binds to the substrates and would places the catalytic domain at the vicinity of substrates in which substrate concentration is high. These emzymes would utilize CBM91 as a tool for efficient saccharification by 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

  1. 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 | PubMed ID:36312872 [Ito2022]
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