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Difference between revisions of "Carbohydrate Binding Module Family 91"

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|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
 
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== Ligand specificities ==
 
== Ligand specificities ==
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Mention here all major natural ligand specificities that are found within a given family (also plant or mammalian origin). Certain linkages and promiscuity would also be mentioned here if biologically relevant.
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CBM91 bound to oat spelt xylan with ''K''<sub>a</sub> value of 2.0×10<sup>-5</sup> M<sup>-1</sup>, 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 <cite>Ito2022</cite>.
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''Note: Here is an example of how to insert references in the text, together with the "biblio" section below:'' Please see these references for an essential introduction to the CAZy classification system: <cite>DaviesSinnott2008 Cantarel2009</cite>. CBMs, in particular, have been extensively reviewed <cite>Boraston2004 Hashimoto2006 Shoseyov2006 Guillen2010 Armenta2017</cite>.
 
  
 
== Structural Features ==
 
== Structural Features ==
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''Content in this section should include, in paragraph form, a description of:''
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[[Image:The_structure_of_PxXyl43A.png|thumb|300px|right|'''Figure 1. The structure of ''Px''Xyl43A and CBM91.
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* '''Fold:''' Structural fold (beta trefoil, beta sandwich, etc.)
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'''The prediction structure by Alpha Fold 2 of  CBM91(red).  This CBM91 is appended to the catalytic domain of ''Px''Xyl43A(green).]]
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* '''Type:''' Include here Type A, B, or C and properties
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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.
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* '''Features of ligand binding:''' Describe CBM binding pocket location (Side or apex) important residues for binding (W, Y, F, subsites), interact with reducing end, non-reducing end, planar surface or within polysaccharide chains. Include examples pdb codes. Metal ion dependent. Etc.
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== Functionalities ==
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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.
  
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== Functionalities ==
 
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''Content in this section should include, in paragraph form, a description of:''
 
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* '''Functional role of CBM:''' Describe common functional roles such as targeting, disruptive, anchoring, proximity/position on substrate.
 
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* '''Most Common Associated Modules:''' 1. Glycoside Hydrolase Activity; 2. Additional Associated Modules (other CBM, FNIII, cohesin, dockerins, expansins, etc.)
 
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* '''Novel Applications:'''  Include here if CBM has been used to modify another enzyme, or if a CBM was used to label plant/mammalian tissues? Etc.
 
  
 
== Family Firsts ==
 
== Family Firsts ==
 
;First Identified
 
;First Identified
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:Insert archetype here, possibly including ''very brief'' synopsis.
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:''Px''CBM91 from ''Px''Xyl43A of ''Paenibacillus xynaniclasticus'' strain TW1 <cite>Ito2022</cite>.
 
;First Structural Characterization
 
;First Structural Characterization
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:Insert archetype here, possibly including ''very brief'' synopsis.
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: β-D-xylosidase, a family 43 glycoside hydrolase from ''Clostridium acetobutylicum'' ATCC 824 [{{PDBlink}}1Y7B PDB ID 1Y7B].  
  
 
== References ==
 
== References ==
 
<biblio>
 
<biblio>
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#Cantarel2009 pmid=18838391
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#Ito2022 pmid=36312872
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#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [https://doi.org/10.1042/BIO03004026 Download PDF version].
 
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#Boraston2004 pmid=15214846
 
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#Hashimoto2006 pmid=17131061
 
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#Shoseyov2006 pmid=16760304
 
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#Guillen2010 pmid=19908036
 
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#Armenta2017 pmid=28547780
 
 
</biblio>
 
</biblio>
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<!-- Do not delete this Category tag -->
 
<!-- Do not delete this Category tag -->
 
[[Category:Carbohydrate Binding Module Families|CBM091]]
 
[[Category:Carbohydrate Binding Module Families|CBM091]]
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<!-- ATTENTION: Make sure to replace "nnn" with a three digit family number, e.g. "032" or "105" etc., for proper sorting of the page by family number. -->
 

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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