https://www.cazypedia.org/api.php?action=feedcontributions&feedformat=atom&user=Daichi+ItoCAZypedia - User contributions [en-ca]2026-05-05T03:27:27ZUser contributionsMediaWiki 1.35.10https://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_91&diff=19471Carbohydrate Binding Module Family 912025-07-02T14:22:08Z<p>Daichi Ito: </p>
<hr />
<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Daichi Ito|Daichi Ito]]<br />
* [[Responsible Curator]]: [[User:Elizabeth Ficko-Blean|Elizabeth Ficko-Blean]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM91.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
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>.<br />
<br />
== Structural Features ==<br />
[[Image:The_structure_of_PxXyl43A.png|thumb|300px|right|'''Figure 1. The structure of ''Px''Xyl43A and CBM91 <cite>Ito2023</cite>. <br />
'''The prediction structure by Alpha Fold 2 of CBM91(red). This CBM91 is appended to the catalytic domain of ''Px''Xyl43A(green).]]<br />
Alpha Fold 2 structure analysis of ''Px''CBM91 exhibited a β-sandwich fold consisted of 12 β-strands and two opposing antiparallel beta sheets <cite>Ito2023</cite>. The concave surface and loops around it connecting the β-strands possess several hydrophobic amino acid residues, the surface is expected to be the binding site<cite>Ito2023</cite>.<br />
<br />
== Functionalities == <br />
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.<br />
''Paenibacillus xylaniclastuicus'' was isolated from anaerobic digester fed with pineapple waste and grows with xylose as sole carbon source <cite>Tachaapaikoon2012 Ratanakhanockchai2012</cite>. ''P. xylaniclastuicus'' is supposed to degrade xylosic substrates efficiently because it has a lot of genes encoding xylolytic enzymes. Xylosidases, like GH43, which produce xylose from xylan and xylooligosaccharides and connects to CBM91 is one of vial enzymes. Therefore, CBM91 would contribute to produce the carbon sources for the growth of xylolytic bacteria.<br />
<br />
== Family Firsts ==<br />
;First Identified:''Px''CBM91 from ''Px''Xyl43A of ''Paenibacillus xynaniclasticus'' strain TW1 <cite>Ito2022</cite>.<br />
;First Structural Characterization: β-D-xylosidase, a family 43 glycoside hydrolase from ''Clostridium acetobutylicum'' ATCC 824 (Released: 2005-01-25) [{{PDBlink}}1Y7B PDB ID 1Y7B]. <br />
<br />
== References ==<br />
<biblio><br />
#Tachaapaikoon2012 C. Tachaapaikoon, S. Tanasupawat, P. Pason, S. Sornyotha, R. Waeonukul, K.L. Kyu and K. Ratanakhanockchai: ''Paenibacillus xylaniclasticus'' sp. nov., a xylanolytic-cellulolytic bacterium isolated from sludge in an anaerobic digester. J.Microbiol., 50, 394–400 (2012) [https://doi.org/10.1007/s12275-012-1480-3 DOI:10.1007/s12275-012-1480-3]<br />
#Ito2022 pmid=36312872<br />
#Ito2023 Ito, D., 2023. Characterization of plant cell wall degrading enzymes from Paenibacillus sp., 2023, Mie University, Ph. D. thesis. https://dl.ndl.go.jp/pid/12910195/1/1<br />
#Ratanakhanockchai2012 K. Ratanakhanockchai, C. Tachaapaikoon, K.L. Kyu and P. Pason: A novel multienzyme complex from a newly isolated facultative anaerobic bacterium, ''Paenibacillus'' sp. TW1. Act. Biol. Hung., 63, 288–300 (2012) [https://doi.org/10.1556/ABiol.63.2012.2.10 DOI:10.1556/ABiol.63.2012.2.10]<br />
<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Carbohydrate Binding Module Families|CBM091]]</div>Daichi Itohttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_91&diff=19470Carbohydrate Binding Module Family 912025-07-02T13:48:22Z<p>Daichi Ito: </p>
<hr />
<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Daichi Ito|Daichi Ito]]<br />
* [[Responsible Curator]]: [[User:Elizabeth Ficko-Blean|Elizabeth Ficko-Blean]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM91.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
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>.<br />
<br />
== Structural Features ==<br />
[[Image:The_structure_of_PxXyl43A.png|thumb|300px|right|'''Figure 1. The structure of ''Px''Xyl43A and CBM91 <cite>Ito2023</cite>. <br />
'''The prediction structure by Alpha Fold 2 of CBM91(red). This CBM91 is appended to the catalytic domain of ''Px''Xyl43A(green).]]<br />
Alpha Fold 2 structure analysis of ''Px''CBM91 exhibited a β-sandwich fold consisted of 12 β-strands and two opposing antiparallel beta sheets <cite>Ito2023</cite>. The concave surface and loops around it connecting the β-strands possesse several hydrophobic amino acid residues, the surface is expected to be the binding site<cite>Ito2023</cite>.<br />
<br />
== Functionalities == <br />
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.<br />
''Paenibacillus xylaniclastuicus'' was isolated from anaerobic digester fed with pineapple waste and grows with xylose as sole carbon source <cite>Tachaapaikoon2012 Ratanakhanockchai2012</cite>. ''P. xylaniclastuicus'' is supposed to degrade xylosic substrates efficiently because it has a lot of genes encoding xylolytic enzymes. Xylosidases, like GH43, which produce xylose from xylan and xylooligosaccharides and connects to CBM91 is one of vial enzymes. Therefore, CBM91 would contribute to produce the carbon sources for the growth of xylolytic bacteria.<br />
<br />
== Family Firsts ==<br />
;First Identified:''Px''CBM91 from ''Px''Xyl43A of ''Paenibacillus xynaniclasticus'' strain TW1 <cite>Ito2022</cite>.<br />
;First Structural Characterization: β-D-xylosidase, a family 43 glycoside hydrolase from ''Clostridium acetobutylicum'' ATCC 824 (Released: 2005-01-25) [{{PDBlink}}1Y7B PDB ID 1Y7B]. <br />
<br />
== References ==<br />
<biblio><br />
#Tachaapaikoon2012 C. Tachaapaikoon, S. Tanasupawat, P. Pason, S. Sornyotha, R. Waeonukul, K.L. Kyu and K. Ratanakhanockchai: ''Paenibacillus xylaniclasticus'' sp. nov., a xylanolytic-cellulolytic bacterium isolated from sludge in an anaerobic digester. J.Microbiol., 50, 394–400 (2012) [https://doi.org/10.1007/s12275-012-1480-3 DOI:10.1007/s12275-012-1480-3]<br />
#Ito2022 pmid=36312872<br />
#Ito2023 Ito, D., 2023. Characterization of plant cell wall degrading enzymes from Paenibacillus sp., 2023, Mie University, Ph. D. thesis. https://dl.ndl.go.jp/pid/12910195/1/1<br />
#Ratanakhanockchai2012 K. Ratanakhanockchai, C. Tachaapaikoon, K.L. Kyu and P. Pason: A novel multienzyme complex from a newly isolated facultative anaerobic bacterium, ''Paenibacillus'' sp. TW1. Act. Biol. Hung., 63, 288–300 (2012) [https://doi.org/10.1556/ABiol.63.2012.2.10 DOI:10.1556/ABiol.63.2012.2.10]<br />
<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Carbohydrate Binding Module Families|CBM091]]</div>Daichi Itohttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_91&diff=19469Carbohydrate Binding Module Family 912025-07-02T13:42:09Z<p>Daichi Ito: </p>
<hr />
<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Daichi Ito|Daichi Ito]]<br />
* [[Responsible Curator]]: [[User:Elizabeth Ficko-Blean|Elizabeth Ficko-Blean]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM91.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
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>.<br />
<br />
== Structural Features ==<br />
[[Image:The_structure_of_PxXyl43A.png|thumb|300px|right|'''Figure 1. The structure of ''Px''Xyl43A and CBM91 <cite>Ito2023</cite>. <br />
'''The prediction structure by Alpha Fold 2 of CBM91(red). This CBM91 is appended to the catalytic domain of ''Px''Xyl43A(green).]]<br />
Alpha Fold 2 structure analysis of ''Px''CBM91 exhibited a β-sandwich fold consisted of 12 β-strands and two opposing antiparallel beta sheets <cite>Ito2023</cite>. The concave surface and loops around it connecting the β-strands possesse several hydrophobic amino acid residues, the surface is expected to be the binding site<cite>Ito2023</cite>.<br />
<br />
== Functionalities == <br />
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.<br />
''Paenibacillus xylaniclastuicus'' was isolated from anaerobic digester fed with pineapple waste and grows with xylose as sole carbon source <cite>Tachaapaikoon2012 Ratanakhanockchai2012</cite>. ''P. xylaniclastuicus'' is supposed to degrade xylosic substrates efficiently because it has a lot of genes encoding xylolytic enzymes. Xylosidases, like GH43, which produce xylose from xylan and xylooligosaccharides and connects to CBM91 is one of vial enzymes. Therefore, CM91 would contribute to produce the carbon sources for the growth of xylolytic bacteria.<br />
<br />
== Family Firsts ==<br />
;First Identified:''Px''CBM91 from ''Px''Xyl43A of ''Paenibacillus xynaniclasticus'' strain TW1 <cite>Ito2022</cite>.<br />
;First Structural Characterization: β-D-xylosidase, a family 43 glycoside hydrolase from ''Clostridium acetobutylicum'' ATCC 824 (Released: 2005-01-25) [{{PDBlink}}1Y7B PDB ID 1Y7B]. <br />
<br />
== References ==<br />
<biblio><br />
#Tachaapaikoon2012 C. Tachaapaikoon, S. Tanasupawat, P. Pason, S. Sornyotha, R. Waeonukul, K.L. Kyu and K. Ratanakhanockchai: ''Paenibacillus xylaniclasticus'' sp. nov., a xylanolytic-cellulolytic bacterium isolated from sludge in an anaerobic digester. J.Microbiol., 50, 394–400 (2012) [https://doi.org/10.1007/s12275-012-1480-3 DOI:10.1007/s12275-012-1480-3]<br />
#Ito2022 pmid=36312872<br />
#Ito2023 Ito, D., 2023. Characterization of plant cell wall degrading enzymes from Paenibacillus sp., 2023, Mie University, Ph. D. thesis. https://dl.ndl.go.jp/pid/12910195/1/1<br />
#Ratanakhanockchai2012 K. Ratanakhanockchai, C. Tachaapaikoon, K.L. Kyu and P. Pason: A novel multienzyme complex from a newly isolated facultative anaerobic bacterium, ''Paenibacillus'' sp. TW1. Act. Biol. Hung., 63, 288–300 (2012) [https://doi.org/10.1556/ABiol.63.2012.2.10 DOI:10.1556/ABiol.63.2012.2.10]<br />
<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Carbohydrate Binding Module Families|CBM091]]</div>Daichi Itohttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_91&diff=19468Carbohydrate Binding Module Family 912025-07-02T13:35:26Z<p>Daichi Ito: </p>
<hr />
<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Daichi Ito|Daichi Ito]]<br />
* [[Responsible Curator]]: [[User:Elizabeth Ficko-Blean|Elizabeth Ficko-Blean]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM91.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
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>.<br />
<br />
== Structural Features ==<br />
[[Image:The_structure_of_PxXyl43A.png|thumb|300px|right|'''Figure 1. The structure of ''Px''Xyl43A and CBM91 <cite>Ito2023</cite>. <br />
'''The prediction structure by Alpha Fold 2 of CBM91(red). This CBM91 is appended to the catalytic domain of ''Px''Xyl43A(green).]]<br />
Alpha Fold 2 structure analysis of ''Px''CBM91 exhibited a β-sandwich fold consisted of 12 β-strands and two opposing antiparallel beta sheets <cite>Ito2023</cite>. The concave surface and loops around it connecting the β-strands possesse several hydrophobic amino acid residues, the surface is expected to be the binding site.<br />
<br />
== Functionalities == <br />
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.<br />
''Paenibacillus xylaniclastuicus'' was isolated from anaerobic digester fed with pineapple waste and grows with xylose as sole carbon source <cite>Tachaapaikoon2012 Ratanakhanockchai2012</cite>. ''P. xylaniclastuicus'' is supposed to degrade xylosic substrates efficiently because it has a lot of genes encoding xylolytic enzymes. Xylosidases, like GH43, which produce xylose from xylan and xylooligosaccharides and connects to CBM91 is one of vial enzymes. Therefore, CM91 would contribute to produce the carbon sources for the growth of xylolytic bacteria.<br />
<br />
== Family Firsts ==<br />
;First Identified:''Px''CBM91 from ''Px''Xyl43A of ''Paenibacillus xynaniclasticus'' strain TW1 <cite>Ito2022</cite>.<br />
;First Structural Characterization: β-D-xylosidase, a family 43 glycoside hydrolase from ''Clostridium acetobutylicum'' ATCC 824 (Released: 2005-01-25) [{{PDBlink}}1Y7B PDB ID 1Y7B]. <br />
<br />
== References ==<br />
<biblio><br />
#Tachaapaikoon2012 C. Tachaapaikoon, S. Tanasupawat, P. Pason, S. Sornyotha, R. Waeonukul, K.L. Kyu and K. Ratanakhanockchai: ''Paenibacillus xylaniclasticus'' sp. nov., a xylanolytic-cellulolytic bacterium isolated from sludge in an anaerobic digester. J.Microbiol., 50, 394–400 (2012) [https://doi.org/10.1007/s12275-012-1480-3 DOI:10.1007/s12275-012-1480-3]<br />
#Ito2022 pmid=36312872<br />
#Ito2023 Ito, D., 2023. Characterization of plant cell wall degrading enzymes from Paenibacillus sp. Ph. D. Mie University. https://dl.ndl.go.jp/pid/12910195/1/1<br />
#Ratanakhanockchai2012 K. Ratanakhanockchai, C. Tachaapaikoon, K.L. Kyu and P. Pason: A novel multienzyme complex from a newly isolated facultative anaerobic bacterium, ''Paenibacillus'' sp. TW1. Act. Biol. Hung., 63, 288–300 (2012) [https://doi.org/10.1556/ABiol.63.2012.2.10 DOI:10.1556/ABiol.63.2012.2.10]<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Carbohydrate Binding Module Families|CBM091]]</div>Daichi Itohttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_91&diff=18363Carbohydrate Binding Module Family 912024-08-31T18:35:11Z<p>Daichi Ito: </p>
<hr />
<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Daichi Ito|Daichi Ito]]<br />
* [[Responsible Curator]]: [[User:Elizabeth Ficko-Blean|Elizabeth Ficko-Blean]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM91.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
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>.<br />
<br />
== Structural Features ==<br />
[[Image:The_structure_of_PxXyl43A.png|thumb|300px|right|'''Figure 1. The structure of ''Px''Xyl43A and CBM91 <cite>Ito2023</cite>. <br />
'''The prediction structure by Alpha Fold 2 of CBM91(red). This CBM91 is appended to the catalytic domain of ''Px''Xyl43A(green).]]<br />
Alpha Fold 2 structure analysis of ''Px''CBM91 exhibited a β-sandwich fold consisted of 12 β-strands and two opposing antiparallel beta sheets <cite>Ito2023</cite>. The concave surface and loops around it connecting the β-strands possesse several hydrophobic amino acid residues, the surface is expected to be the binding site.<br />
<br />
== Functionalities == <br />
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.<br />
''Paenibacillus xylaniclastuicus'' was isolated from anaerobic digester fed with pineapple waste and grows with xylose as sole carbon source <cite>Tachaapaikoon2012 Ratanakhanockchai2012</cite>.<br />
Xylosidases, like GH43, which produce xylose from xylan and xylooligosaccharides and connects to CBM91 is one of vial enzymes. Therefore, CM91 would contribute to produce the carbon sources for the growth of xylolytic bacteria.<br />
<br />
== Family Firsts ==<br />
;First Identified:''Px''CBM91 from ''Px''Xyl43A of ''Paenibacillus xynaniclasticus'' strain TW1 <cite>Ito2022</cite>.<br />
;First Structural Characterization: β-D-xylosidase, a family 43 glycoside hydrolase from ''Clostridium acetobutylicum'' ATCC 824 (Released: 2005-01-25) [{{PDBlink}}1Y7B PDB ID 1Y7B]. <br />
<br />
== References ==<br />
<biblio><br />
#Tachaapaikoon2012 C. Tachaapaikoon, S. Tanasupawat, P. Pason, S. Sornyotha, R. Waeonukul, K.L. Kyu and K. Ratanakhanockchai: ''Paenibacillus xylaniclasticus'' sp. nov., a xylanolytic-cellulolytic bacterium isolated from sludge in an anaerobic digester. J.Microbiol., 50, 394–400 (2012) [https://doi.org/10.1007/s12275-012-1480-3 DOI:10.1007/s12275-012-1480-3]<br />
#Ito2022 pmid=36312872<br />
#Ito2023 Ito, D., 2023. Characterization of plant cell wall degrading enzymes from Paenibacillus sp. Ph. D. Mie University. https://dl.ndl.go.jp/pid/12910195/1/1<br />
#Ratanakhanockchai2012 K. Ratanakhanockchai, C. Tachaapaikoon, K.L. Kyu and P. Pason: A novel multienzyme complex from a newly isolated facultative anaerobic bacterium, ''Paenibacillus'' sp. TW1. Act. Biol. Hung., 63, 288–300 (2012) [https://doi.org/10.1556/ABiol.63.2012.2.10 DOI:10.1556/ABiol.63.2012.2.10]<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Carbohydrate Binding Module Families|CBM091]]</div>Daichi Itohttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_91&diff=18362Carbohydrate Binding Module Family 912024-08-31T18:16:44Z<p>Daichi Ito: </p>
<hr />
<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Daichi Ito|Daichi Ito]]<br />
* [[Responsible Curator]]: [[User:Elizabeth Ficko-Blean|Elizabeth Ficko-Blean]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM91.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
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>.<br />
<br />
== Structural Features ==<br />
[[Image:The_structure_of_PxXyl43A.png|thumb|300px|right|'''Figure 1. The structure of ''Px''Xyl43A and CBM91 <cite>Ito2023</cite>. <br />
'''The prediction structure by Alpha Fold 2 of CBM91(red). This CBM91 is appended to the catalytic domain of ''Px''Xyl43A(green).]]<br />
Alpha Fold 2 structure analysis of ''Px''CBM91 exhibited a β-sandwich fold consisted of 12 β-strands and two opposing antiparallel beta sheets <cite>Ito2023</cite>. The concave surface and loops around it connecting the β-strands possesse several hydrophobic amino acid residues, the surface is expected to be the binding site.<br />
<br />
== Functionalities == <br />
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.<br />
''Paenibacillus xylaniclastuicus'' was isolated from anaerobic digester fed with pineapple waste and grows with xylose as sole carbon source <cite>Tachaapaikoon2012 Ratanakhanockchai2012</cite>.<br />
Xylosidases, like GH43, which produce xylose from xylan and xylooligosaccharides and connects to CBM91 is one of vial enzymes. Therefore, CM91 would contribute to produce the carbon sources for the growth of xylolytic bacteria.<br />
<br />
== Family Firsts ==<br />
;First Identified:''Px''CBM91 from ''Px''Xyl43A of ''Paenibacillus xynaniclasticus'' strain TW1 <cite>Ito2022</cite>.<br />
;First Structural Characterization: β-D-xylosidase, a family 43 glycoside hydrolase from ''Clostridium acetobutylicum'' ATCC 824 [{{PDBlink}}1Y7B PDB ID 1Y7B]. <br />
<br />
== References ==<br />
<biblio><br />
#Tachaapaikoon2012 C. Tachaapaikoon, S. Tanasupawat, P. Pason, S. Sornyotha, R. Waeonukul, K.L. Kyu and K. Ratanakhanockchai: ''Paenibacillus xylaniclasticus'' sp. nov., a xylanolytic-cellulolytic bacterium isolated from sludge in an anaerobic digester. J.Microbiol., 50, 394–400 (2012) [https://doi.org/10.1007/s12275-012-1480-3 DOI:10.1007/s12275-012-1480-3]<br />
#Ito2022 pmid=36312872<br />
#Ito2023 Ito, D., 2023. Characterization of plant cell wall degrading enzymes from Paenibacillus sp. Ph. D. Mie University. https://dl.ndl.go.jp/pid/12910195/1/1<br />
#Ratanakhanockchai2012 K. Ratanakhanockchai, C. Tachaapaikoon, K.L. Kyu and P. Pason: A novel multienzyme complex from a newly isolated facultative anaerobic bacterium, ''Paenibacillus'' sp. TW1. Act. Biol. Hung., 63, 288–300 (2012) [https://doi.org/10.1556/ABiol.63.2012.2.10 DOI:10.1556/ABiol.63.2012.2.10]<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Carbohydrate Binding Module Families|CBM091]]</div>Daichi Itohttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_91&diff=18361Carbohydrate Binding Module Family 912024-08-31T18:14:59Z<p>Daichi Ito: </p>
<hr />
<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Daichi Ito|Daichi Ito]]<br />
* [[Responsible Curator]]: [[User:Elizabeth Ficko-Blean|Elizabeth Ficko-Blean]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM91.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
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>.<br />
<br />
== Structural Features ==<br />
[[Image:The_structure_of_PxXyl43A.png|thumb|300px|right|'''Figure 1. The structure of ''Px''Xyl43A and CBM91 <cite>Ito2023</cite>. <br />
'''The prediction structure by Alpha Fold 2 of CBM91(red). This CBM91 is appended to the catalytic domain of ''Px''Xyl43A(green).]]<br />
Alpha Fold 2 structure analysis of ''Px''CBM91 exhibited a β-sandwich fold consisted of 12 β-strands and two opposing antiparallel beta sheets <cite>Ito2023</cite>. The concave surface and loops around it connecting the β-strands possesse several hydrophobic amino acid residues, the surface is expected to be the binding site.<br />
<br />
== Functionalities == <br />
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.<br />
''Paenibacillus xylaniclastuicus'' was isolated from anaerobic digester fed with pineapple waste and grows with xylose as sole carbon source <cite>Tachaapaikoon2012 Ratanakhanockchai2012</cite>.<br />
Xylosidases, like GH43, which produce xylose from xylan and xylooligosaccharides and connects to CBM91 is one of vial enzymes. Therefore, CM91 would contribute to produce the carbon sources for the growth of xylolytic bacteria.<br />
<br />
== Family Firsts ==<br />
;First Identified:''Px''CBM91 from ''Px''Xyl43A of ''Paenibacillus xynaniclasticus'' strain TW1 <cite>Ito2022</cite>.<br />
;First Structural Characterization: β-D-xylosidase, a family 43 glycoside hydrolase from ''Clostridium acetobutylicum'' ATCC 824 [{{PDBlink}}1Y7B PDB ID 1Y7B]. <br />
<br />
== References ==<br />
<biblio><br />
#Tachaapaikoon2012 C. Tachaapaikoon, S. Tanasupawat, P. Pason, S. Sornyotha, R. Waeonukul, K.L. Kyu and K. Ratanakhanockchai: Paenibacillus xylaniclasticus sp. nov., a xylanolytic-cellulolytic bacterium isolated from sludge in an anaerobic digester. J.Microbiol., 50, 394–400 (2012) [https://doi.org/10.1007/s12275-012-1480-3 DOI:10.1007/s12275-012-1480-3]<br />
#Ito2022 pmid=36312872<br />
#Ito2023 Ito, D., 2023. Characterization of plant cell wall degrading enzymes from Paenibacillus sp. Ph. D. Mie University. https://dl.ndl.go.jp/pid/12910195/1/1<br />
#Ratanakhanockchai2012 K. Ratanakhanockchai, C. Tachaapaikoon, K.L. Kyu and P. Pason: A novel multienzyme complex from a newly isolated facultative anaerobic bacterium, Paenibacillus sp. TW1. Act. Biol. Hung., 63, 288–300 (2012) [https://doi.org/10.1556/ABiol.63.2012.2.10 DOI:10.1556/ABiol.63.2012.2.10]<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Carbohydrate Binding Module Families|CBM091]]</div>Daichi Itohttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_91&diff=18360Carbohydrate Binding Module Family 912024-08-31T18:12:44Z<p>Daichi Ito: </p>
<hr />
<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Daichi Ito|Daichi Ito]]<br />
* [[Responsible Curator]]: [[User:Elizabeth Ficko-Blean|Elizabeth Ficko-Blean]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM91.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
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>.<br />
<br />
== Structural Features ==<br />
[[Image:The_structure_of_PxXyl43A.png|thumb|300px|right|'''Figure 1. The structure of ''Px''Xyl43A and CBM91 <cite>Ito2023</cite>. <br />
'''The prediction structure by Alpha Fold 2 of CBM91(red). This CBM91 is appended to the catalytic domain of ''Px''Xyl43A(green).]]<br />
Alpha Fold 2 structure analysis of ''Px''CBM91 exhibited a β-sandwich fold consisted of 12 β-strands and two opposing antiparallel beta sheets <cite>Ito2023</cite>. The concave surface and loops around it connecting the β-strands possesse several hydrophobic amino acid residues, the surface is expected to be the binding site.<br />
<br />
== Functionalities == <br />
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.<br />
''Paenibacillus xylaniclastuicus'' was isolated from anaerobic digester fed with pineapple waste and grows with xylose as sole carbon source <cite>Tachaapaikoon2012 Ratanakhanockchai2012</cite>.<br />
Xylosidases, like GH43, which produce xylose from xylan and xylooligosaccharides and connects to CBM91 is one of vial enzymes. Therefore, CM91 would contribute to produce the carbon sources for the growth of xylolytic bacteria.<br />
<br />
== Family Firsts ==<br />
;First Identified:''Px''CBM91 from ''Px''Xyl43A of ''Paenibacillus xynaniclasticus'' strain TW1 <cite>Ito2022</cite>.<br />
;First Structural Characterization: β-D-xylosidase, a family 43 glycoside hydrolase from ''Clostridium acetobutylicum'' ATCC 824 [{{PDBlink}}1Y7B PDB ID 1Y7B]. <br />
<br />
== References ==<br />
<biblio><br />
#Tachaapaikoon2012 C. Tachaapaikoon, S. Tanasupawat, P. Pason, S. Sornyotha, R. Waeonukul, K.L. Kyu and K. Ratanakhanockchai: Paenibacillus xylaniclasticus sp. nov., a xylanolytic-cellulolytic bacterium isolated from sludge in an anaerobic digester. J.Microbiol., 50, 394–400 (2012) [https://doi.org/10.1556/ABiol.63.2012.2.10 DOI:10.1007/s12275-012-1480-3]<br />
#Ito2022 pmid=36312872<br />
#Ito2023 Ito, D., 2023. Characterization of plant cell wall degrading enzymes from Paenibacillus sp. Ph. D. Mie University. https://dl.ndl.go.jp/pid/12910195/1/1<br />
#Ratanakhanockchai2012 K. Ratanakhanockchai, C. Tachaapaikoon, K.L. Kyu and P. Pason: A novel multienzyme complex from a newly isolated facultative anaerobic bacterium, Paenibacillus sp. TW1. Act. Biol. Hung., 63, 288–300 (2012) [https://doi.org/10.1556/ABiol.63.2012.2.10 DOI:10.1016/0014-5793(86)80816-X]<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Carbohydrate Binding Module Families|CBM091]]</div>Daichi Itohttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_91&diff=18359Carbohydrate Binding Module Family 912024-08-31T18:11:57Z<p>Daichi Ito: </p>
<hr />
<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Daichi Ito|Daichi Ito]]<br />
* [[Responsible Curator]]: [[User:Elizabeth Ficko-Blean|Elizabeth Ficko-Blean]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM91.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
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>.<br />
<br />
== Structural Features ==<br />
[[Image:The_structure_of_PxXyl43A.png|thumb|300px|right|'''Figure 1. The structure of ''Px''Xyl43A and CBM91 <cite>Ito2023</cite>. <br />
'''The prediction structure by Alpha Fold 2 of CBM91(red). This CBM91 is appended to the catalytic domain of ''Px''Xyl43A(green).]]<br />
Alpha Fold 2 structure analysis of ''Px''CBM91 exhibited a β-sandwich fold consisted of 12 β-strands and two opposing antiparallel beta sheets <cite>Ito2023</cite>. The concave surface and loops around it connecting the β-strands possesse several hydrophobic amino acid residues, the surface is expected to be the binding site.<br />
<br />
== Functionalities == <br />
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.<br />
''Paenibacillus xylaniclastuicus'' was isolated from anaerobic digester fed with pineapple waste and grows with xylose as sole carbon source <cite>Tachaapaikoon2012 Ratanakhanockchai2012</cite>.<br />
Xylosidases, like GH43, which produce xylose from xylan and xylooligosaccharides and connects to CBM91 is one of vial enzymes. Therefore, CM91 would contribute to produce the carbon sources for the growth of xylolytic bacteria.<br />
<br />
== Family Firsts ==<br />
;First Identified:''Px''CBM91 from ''Px''Xyl43A of ''Paenibacillus xynaniclasticus'' strain TW1 <cite>Ito2022</cite>.<br />
;First Structural Characterization: β-D-xylosidase, a family 43 glycoside hydrolase from ''Clostridium acetobutylicum'' ATCC 824 [{{PDBlink}}1Y7B PDB ID 1Y7B]. <br />
<br />
== References ==<br />
<biblio><br />
#Tachaapaikoon2012 C. Tachaapaikoon, S. Tanasupawat, P. Pason, S. Sornyotha, R. Waeonukul, K.L. Kyu and K. Ratanakhanockchai: Paenibacillus xylaniclasticus sp. nov., a xylanolytic-cellulolytic bacterium isolated from sludge in an anaerobic digester. J.Microbiol., 50, 394–400 (2012) DOI 10.1007/s12275-012-1480-3<br />
#Ito2022 pmid=36312872<br />
#Ito2023 Ito, D., 2023. Characterization of plant cell wall degrading enzymes from Paenibacillus sp. Ph. D. Mie University. https://dl.ndl.go.jp/pid/12910195/1/1<br />
#Ratanakhanockchai2012 K. Ratanakhanockchai, C. Tachaapaikoon, K.L. Kyu and P. Pason: A novel multienzyme complex from a newly isolated facultative anaerobic bacterium, Paenibacillus sp. TW1. Act. Biol. Hung., 63, 288–300 (2012) [https://doi.org/10.1556/ABiol.63.2012.2.10 DOI:10.1016/0014-5793(86)80816-X]<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Carbohydrate Binding Module Families|CBM091]]</div>Daichi Itohttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_91&diff=18358Carbohydrate Binding Module Family 912024-08-31T18:09:52Z<p>Daichi Ito: </p>
<hr />
<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Daichi Ito|Daichi Ito]]<br />
* [[Responsible Curator]]: [[User:Elizabeth Ficko-Blean|Elizabeth Ficko-Blean]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM91.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
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>.<br />
<br />
== Structural Features ==<br />
[[Image:The_structure_of_PxXyl43A.png|thumb|300px|right|'''Figure 1. The structure of ''Px''Xyl43A and CBM91 <cite>Ito2023</cite>. <br />
'''The prediction structure by Alpha Fold 2 of CBM91(red). This CBM91 is appended to the catalytic domain of ''Px''Xyl43A(green).]]<br />
Alpha Fold 2 structure analysis of ''Px''CBM91 exhibited a β-sandwich fold consisted of 12 β-strands and two opposing antiparallel beta sheets <cite>Ito2023</cite>. The concave surface and loops around it connecting the β-strands possesse several hydrophobic amino acid residues, the surface is expected to be the binding site.<br />
<br />
== Functionalities == <br />
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.<br />
''Paenibacillus xylaniclastuicus'' was isolated from anaerobic digester fed with pineapple waste and grows with xylose as sole carbon source <cite>Tachaapaikoon2012 Ratanakhanockchai2012</cite>.<br />
Xylosidases, like GH43, which produce xylose from xylan and xylooligosaccharides and connects to CBM91 is one of vial enzymes. Therefore, CM91 would contribute to produce the carbon sources for the growth of xylolytic bacteria.<br />
<br />
== Family Firsts ==<br />
;First Identified:''Px''CBM91 from ''Px''Xyl43A of ''Paenibacillus xynaniclasticus'' strain TW1 <cite>Ito2022</cite>.<br />
;First Structural Characterization: β-D-xylosidase, a family 43 glycoside hydrolase from ''Clostridium acetobutylicum'' ATCC 824 [{{PDBlink}}1Y7B PDB ID 1Y7B]. <br />
<br />
== References ==<br />
<biblio><br />
#Tachaapaikoon2012 C. Tachaapaikoon, S. Tanasupawat, P. Pason, S. Sornyotha, R. Waeonukul, K.L. Kyu and K. Ratanakhanockchai: Paenibacillus xylaniclasticus sp. nov., a xylanolytic-cellulolytic bacterium isolated from sludge in an anaerobic digester. J.Microbiol., 50, 394–400 (2012) DOI 10.1007/s12275-012-1480-3<br />
#Ito2022 pmid=36312872<br />
#Ito2023 Ito, D., 2023. Characterization of plant cell wall degrading enzymes from Paenibacillus sp. Ph. D. Mie University. https://dl.ndl.go.jp/pid/12910195/1/1<br />
#Ratanakhanockchai2012 K. Ratanakhanockchai, C. Tachaapaikoon, K.L. Kyu and P. Pason: A novel multienzyme complex from a newly isolated facultative anaerobic bacterium, Paenibacillus sp. TW1. Act. Biol. Hung., 63, 288–300 (2012) DOI: 10.1556/ABiol.63.2012.2.10<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Carbohydrate Binding Module Families|CBM091]]</div>Daichi Itohttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_91&diff=18357Carbohydrate Binding Module Family 912024-08-31T18:07:51Z<p>Daichi Ito: </p>
<hr />
<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Daichi Ito|Daichi Ito]]<br />
* [[Responsible Curator]]: [[User:Elizabeth Ficko-Blean|Elizabeth Ficko-Blean]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM91.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
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>.<br />
<br />
== Structural Features ==<br />
[[Image:The_structure_of_PxXyl43A.png|thumb|300px|right|'''Figure 1. The structure of ''Px''Xyl43A and CBM91 <cite>Ito2023</cite>. <br />
'''The prediction structure by Alpha Fold 2 of CBM91(red). This CBM91 is appended to the catalytic domain of ''Px''Xyl43A(green).]]<br />
Alpha Fold 2 structure analysis of ''Px''CBM91 exhibited a β-sandwich fold consisted of 12 β-strands and two opposing antiparallel beta sheets <cite>Ito2023</cite>. The concave surface and loops around it connecting the β-strands possesse several hydrophobic amino acid residues, the surface is expected to be the binding site.<br />
<br />
== Functionalities == <br />
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.<br />
''Paenibacillus xylaniclastuicus'' was isolated from anaerobic digester fed with pineapple waste and grows with xylose as sole carbon source <cite>Tachaapaikoon2012 Ratanakhanockchai2012</cite>.<br />
Xylosidases, like GH43, which produce xylose from xylan and xylooligosaccharides and connects to CBM91 is one of vial enzymes. Therefore, CM91 would contribute to produce the carbon sources for the growth of xylolytic bacteria.<br />
<br />
== Family Firsts ==<br />
;First Identified:''Px''CBM91 from ''Px''Xyl43A of ''Paenibacillus xynaniclasticus'' strain TW1 <cite>Ito2022</cite>.<br />
;First Structural Characterization: β-D-xylosidase, a family 43 glycoside hydrolase from ''Clostridium acetobutylicum'' ATCC 824 [{{PDBlink}}1Y7B PDB ID 1Y7B]. <br />
<br />
== References ==<br />
<biblio><br />
#Tachaapaikoon2012 C. Tachaapaikoon, S. Tanasupawat, P. Pason, S. Sornyotha, R. Waeonukul, K.L. Kyu and K. Ratanakhanockchai: Paenibacillus xylaniclasticus sp. nov., a xylanolytic-cellulolytic bacterium isolated from sludge in an anaerobic digester. J.Microbiol., 50, 394–400 (2012)<br />
#Ito2022 pmid=36312872<br />
#Ito2023 Ito, D., 2023. Characterization of plant cell wall degrading enzymes from Paenibacillus sp. Ph. D. Mie University. https://dl.ndl.go.jp/pid/12910195/1/1<br />
#Ratanakhanockchai2012 K. Ratanakhanockchai, C. Tachaapaikoon, K.L. Kyu and P. Pason: A novel multienzyme complex from a newly isolated facultative anaerobic bacterium, Paenibacillus sp. TW1. Act. Biol. Hung., 63, 288–300 (2012)<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Carbohydrate Binding Module Families|CBM091]]</div>Daichi Itohttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_91&diff=18356Carbohydrate Binding Module Family 912024-08-31T18:07:20Z<p>Daichi Ito: </p>
<hr />
<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Daichi Ito|Daichi Ito]]<br />
* [[Responsible Curator]]: [[User:Elizabeth Ficko-Blean|Elizabeth Ficko-Blean]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM91.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
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>.<br />
<br />
== Structural Features ==<br />
[[Image:The_structure_of_PxXyl43A.png|thumb|300px|right|'''Figure 1. The structure of ''Px''Xyl43A and CBM91. <br />
'''The prediction structure by Alpha Fold 2 of CBM91(red) <cite>Ito2023</cite>. This CBM91 is appended to the catalytic domain of ''Px''Xyl43A(green).]]<br />
Alpha Fold 2 structure analysis of ''Px''CBM91 exhibited a β-sandwich fold consisted of 12 β-strands and two opposing antiparallel beta sheets <cite>Ito2023</cite>. The concave surface and loops around it connecting the β-strands possesse several hydrophobic amino acid residues, the surface is expected to be the binding site.<br />
<br />
== Functionalities == <br />
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.<br />
''Paenibacillus xylaniclastuicus'' was isolated from anaerobic digester fed with pineapple waste and grows with xylose as sole carbon source <cite>Tachaapaikoon2012 Ratanakhanockchai2012</cite>.<br />
Xylosidases, like GH43, which produce xylose from xylan and xylooligosaccharides and connects to CBM91 is one of vial enzymes. Therefore, CM91 would contribute to produce the carbon sources for the growth of xylolytic bacteria.<br />
<br />
== Family Firsts ==<br />
;First Identified:''Px''CBM91 from ''Px''Xyl43A of ''Paenibacillus xynaniclasticus'' strain TW1 <cite>Ito2022</cite>.<br />
;First Structural Characterization: β-D-xylosidase, a family 43 glycoside hydrolase from ''Clostridium acetobutylicum'' ATCC 824 [{{PDBlink}}1Y7B PDB ID 1Y7B]. <br />
<br />
== References ==<br />
<biblio><br />
#Tachaapaikoon2012 C. Tachaapaikoon, S. Tanasupawat, P. Pason, S. Sornyotha, R. Waeonukul, K.L. Kyu and K. Ratanakhanockchai: Paenibacillus xylaniclasticus sp. nov., a xylanolytic-cellulolytic bacterium isolated from sludge in an anaerobic digester. J.Microbiol., 50, 394–400 (2012)<br />
#Ito2022 pmid=36312872<br />
#Ito2023 Ito, D., 2023. Characterization of plant cell wall degrading enzymes from Paenibacillus sp. Ph. D. Mie University. https://dl.ndl.go.jp/pid/12910195/1/1<br />
#Ratanakhanockchai2012 K. Ratanakhanockchai, C. Tachaapaikoon, K.L. Kyu and P. Pason: A novel multienzyme complex from a newly isolated facultative anaerobic bacterium, Paenibacillus sp. TW1. Act. Biol. Hung., 63, 288–300 (2012)<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Carbohydrate Binding Module Families|CBM091]]</div>Daichi Itohttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_91&diff=18355Carbohydrate Binding Module Family 912024-08-31T18:05:50Z<p>Daichi Ito: </p>
<hr />
<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Daichi Ito|Daichi Ito]]<br />
* [[Responsible Curator]]: [[User:Elizabeth Ficko-Blean|Elizabeth Ficko-Blean]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM91.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
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>.<br />
<br />
== Structural Features ==<br />
[[Image:The_structure_of_PxXyl43A.png|thumb|300px|right|'''Figure 1. The structure of ''Px''Xyl43A and CBM91. <br />
'''The prediction structure by Alpha Fold 2 of CBM91(red). This CBM91 is appended to the catalytic domain of ''Px''Xyl43A(green).]]<br />
Alpha Fold 2 structure analysis of ''Px''CBM91 exhibited a β-sandwich fold consisted of 12 β-strands and two opposing antiparallel beta sheets <cite>Ito2023</cite>. The concave surface and loops around it connecting the β-strands possesse several hydrophobic amino acid residues, the surface is expected to be the binding site.<br />
<br />
== Functionalities == <br />
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.<br />
''Paenibacillus xylaniclastuicus'' was isolated from anaerobic digester fed with pineapple waste and grows with xylose as sole carbon source <cite>Tachaapaikoon2012 Ratanakhanockchai2012</cite>.<br />
Xylosidases, like GH43, which produce xylose from xylan and xylooligosaccharides and connects to CBM91 is one of vial enzymes. Therefore, CM91 would contribute to produce the carbon sources for the growth of xylolytic bacteria.<br />
<br />
== Family Firsts ==<br />
;First Identified:''Px''CBM91 from ''Px''Xyl43A of ''Paenibacillus xynaniclasticus'' strain TW1 <cite>Ito2022</cite>.<br />
;First Structural Characterization: β-D-xylosidase, a family 43 glycoside hydrolase from ''Clostridium acetobutylicum'' ATCC 824 [{{PDBlink}}1Y7B PDB ID 1Y7B]. <br />
<br />
== References ==<br />
<biblio><br />
#Tachaapaikoon2012 C. Tachaapaikoon, S. Tanasupawat, P. Pason, S. Sornyotha, R. Waeonukul, K.L. Kyu and K. Ratanakhanockchai: Paenibacillus xylaniclasticus sp. nov., a xylanolytic-cellulolytic bacterium isolated from sludge in an anaerobic digester. J.Microbiol., 50, 394–400 (2012)<br />
#Ito2022 pmid=36312872<br />
#Ito2023 Ito, D., 2023. Characterization of plant cell wall degrading enzymes from Paenibacillus sp. Ph. D. Mie University. https://dl.ndl.go.jp/pid/12910195/1/1<br />
#Ratanakhanockchai2012 K. Ratanakhanockchai, C. Tachaapaikoon, K.L. Kyu and P. Pason: A novel multienzyme complex from a newly isolated facultative anaerobic bacterium, Paenibacillus sp. TW1. Act. Biol. Hung., 63, 288–300 (2012)<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Carbohydrate Binding Module Families|CBM091]]</div>Daichi Itohttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_91&diff=18354Carbohydrate Binding Module Family 912024-08-31T18:04:51Z<p>Daichi Ito: </p>
<hr />
<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Daichi Ito|Daichi Ito]]<br />
* [[Responsible Curator]]: [[User:Elizabeth Ficko-Blean|Elizabeth Ficko-Blean]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM91.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
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>.<br />
<br />
== Structural Features ==<br />
[[Image:The_structure_of_PxXyl43A.png|thumb|300px|right|'''Figure 1. The structure of ''Px''Xyl43A and CBM91. <br />
'''The prediction structure by Alpha Fold 2 of CBM91(red). This CBM91 is appended to the catalytic domain of ''Px''Xyl43A(green).]]<br />
Alpha Fold 2 structure analysis of ''Px''CBM91 exhibited a β-sandwich fold consisted of 12 β-strands and two opposing antiparallel beta sheets <cite>Ito2023</cite>. The concave surface and loops around it connecting the β-strands possesse several hydrophobic amino acid residues, the surface is expected to be the binding site.<br />
<br />
== Functionalities == <br />
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.<br />
''Paenibacillus xylaniclastuicus'' was isolated from anaerobic digester fed with pineapple waste and grows with xylose as sole carbon source <cite>Tachaapaikoon</cite>.<br />
Xylosidases, like GH43, which produce xylose from xylan and xylooligosaccharides and connects to CBM91 is one of vial enzymes. Therefore, CM91 would contribute to produce the carbon sources for the growth of xylolytic bacteria.<br />
<br />
== Family Firsts ==<br />
;First Identified:''Px''CBM91 from ''Px''Xyl43A of ''Paenibacillus xynaniclasticus'' strain TW1 <cite>Ito2022</cite>.<br />
;First Structural Characterization: β-D-xylosidase, a family 43 glycoside hydrolase from ''Clostridium acetobutylicum'' ATCC 824 [{{PDBlink}}1Y7B PDB ID 1Y7B]. <br />
<br />
== References ==<br />
<biblio><br />
#Tachaapaikoon2012 C. Tachaapaikoon, S. Tanasupawat, P. Pason, S. Sornyotha, R. Waeonukul, K.L. Kyu and K. Ratanakhanockchai: Paenibacillus xylaniclasticus sp. nov., a xylanolytic-cellulolytic bacterium isolated from sludge in an anaerobic digester. J.Microbiol., 50, 394–400 (2012)<br />
#Ito2022 pmid=36312872<br />
#Ito2023 Ito, D., 2023. Characterization of plant cell wall degrading enzymes from Paenibacillus sp. Ph. D. Mie University. https://dl.ndl.go.jp/pid/12910195/1/1<br />
#Ratanakhanockchai2012 K. Ratanakhanockchai, C. Tachaapaikoon, K.L. Kyu and P. Pason: A novel multienzyme complex from a newly isolated facultative anaerobic bacterium, Paenibacillus sp. TW1. Act. Biol. Hung., 63, 288–300 (2012)<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Carbohydrate Binding Module Families|CBM091]]</div>Daichi Itohttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_91&diff=18353Carbohydrate Binding Module Family 912024-08-31T18:03:02Z<p>Daichi Ito: </p>
<hr />
<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Daichi Ito|Daichi Ito]]<br />
* [[Responsible Curator]]: [[User:Elizabeth Ficko-Blean|Elizabeth Ficko-Blean]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM91.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
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>.<br />
<br />
== Structural Features ==<br />
[[Image:The_structure_of_PxXyl43A.png|thumb|300px|right|'''Figure 1. The structure of ''Px''Xyl43A and CBM91. <br />
'''The prediction structure by Alpha Fold 2 of CBM91(red). This CBM91 is appended to the catalytic domain of ''Px''Xyl43A(green).]]<br />
Alpha Fold 2 structure analysis of ''Px''CBM91 exhibited a β-sandwich fold consisted of 12 β-strands and two opposing antiparallel beta sheets <cite>Ito2023</cite>. The concave surface and loops around it connecting the β-strands possesse several hydrophobic amino acid residues, the surface is expected to be the binding site.<br />
<br />
== Functionalities == <br />
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.<br />
''Paenibacillus xylaniclastuicus'' was isolated from anaerobic digester fed with pineapple waste and grows with xylose as sole carbon source <cite>Tachaapaikoon</cite>.<br />
Xylosidases, like GH43, which produce xylose from xylan and xylooligosaccharides and connects to CBM91 is one of vial enzymes. Therefore, CM91 would contribute to produce the carbon sources for the growth of xylolytic bacteria.<br />
<br />
== Family Firsts ==<br />
;First Identified:''Px''CBM91 from ''Px''Xyl43A of ''Paenibacillus xynaniclasticus'' strain TW1 <cite>Ito2022</cite>.<br />
;First Structural Characterization: β-D-xylosidase, a family 43 glycoside hydrolase from ''Clostridium acetobutylicum'' ATCC 824 [{{PDBlink}}1Y7B PDB ID 1Y7B]. <br />
<br />
== References ==<br />
<biblio><br />
#Tachaapaikoon C. Tachaapaikoon, S. Tanasupawat, P. Pason, S. Sornyotha, R. Waeonukul, K.L. Kyu and K. Ratanakhanockchai: Paenibacillus xylaniclasticus sp. nov., a xylanolytic-cellulolytic bacterium isolated from sludge in an anaerobic digester. J.Microbiol., 50, 394–400 (2012)<br />
#Ito2022 pmid=36312872<br />
#Ito2023 Ito, D., 2023. Characterization of plant cell wall degrading enzymes from Paenibacillus sp. Ph. D. Mie University. https://dl.ndl.go.jp/pid/12910195/1/1<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Carbohydrate Binding Module Families|CBM091]]</div>Daichi Itohttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_91&diff=18352Carbohydrate Binding Module Family 912024-08-31T18:01:47Z<p>Daichi Ito: </p>
<hr />
<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Daichi Ito|Daichi Ito]]<br />
* [[Responsible Curator]]: [[User:Elizabeth Ficko-Blean|Elizabeth Ficko-Blean]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM91.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
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>.<br />
<br />
== Structural Features ==<br />
[[Image:The_structure_of_PxXyl43A.png|thumb|300px|right|'''Figure 1. The structure of ''Px''Xyl43A and CBM91. <br />
'''The prediction structure by Alpha Fold 2 of CBM91(red). This CBM91 is appended to the catalytic domain of ''Px''Xyl43A(green).]]<br />
Alpha Fold 2 structure analysis of ''Px''CBM91 exhibited a β-sandwich fold consisted of 12 β-strands and two opposing antiparallel beta sheets<cite>Ito2023</cite>. The concave surface and loops around it connecting the β-strands possesse several hydrophobic amino acid residues, the surface is expected to be the binding site.<br />
<br />
== Functionalities == <br />
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.<br />
''Paenibacillus xylaniclastuicus'' was isolated from anaerobic digester fed with pineapple waste and grows with xylose as sole carbon source <cite>Tachaapaikoon</cite>.<br />
Xylosidases, like GH43, which produce xylose from xylan and xylooligosaccharides and connects to CBM91 is one of vial enzymes. Therefore, CM91 would contribute to produce the carbon sources for the growth of xylolytic bacteria.<br />
<br />
== Family Firsts ==<br />
;First Identified:''Px''CBM91 from ''Px''Xyl43A of ''Paenibacillus xynaniclasticus'' strain TW1 <cite>Ito2022</cite>.<br />
;First Structural Characterization: β-D-xylosidase, a family 43 glycoside hydrolase from ''Clostridium acetobutylicum'' ATCC 824 [{{PDBlink}}1Y7B PDB ID 1Y7B]. <br />
<br />
== References ==<br />
<biblio><br />
#Tachaapaikoon C. Tachaapaikoon, S. Tanasupawat, P. Pason, S. Sornyotha, R. Waeonukul, K.L. Kyu and K. Ratanakhanockchai: Paenibacillus xylaniclasticus sp. nov., a xylanolytic-cellulolytic bacterium isolated from sludge in an anaerobic digester. J.Microbiol., 50, 394–400 (2012)<br />
#Ito2022 pmid=36312872<br />
#Ito2023 Ito, D., 2023. Characterization of plant cell wall degrading enzymes from Paenibacillus sp. Ph. D. Mie University.https://dl.ndl.go.jp/pid/12910195/1/1<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Carbohydrate Binding Module Families|CBM091]]</div>Daichi Itohttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_91&diff=18351Carbohydrate Binding Module Family 912024-08-31T17:55:27Z<p>Daichi Ito: </p>
<hr />
<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Daichi Ito|Daichi Ito]]<br />
* [[Responsible Curator]]: [[User:Elizabeth Ficko-Blean|Elizabeth Ficko-Blean]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM91.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
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>.<br />
<br />
== Structural Features ==<br />
[[Image:The_structure_of_PxXyl43A.png|thumb|300px|right|'''Figure 1. The structure of ''Px''Xyl43A and CBM91. <br />
'''The prediction structure by Alpha Fold 2 of CBM91(red). This CBM91 is appended to the catalytic domain of ''Px''Xyl43A(green).]]<br />
Alpha Fold 2 structure analysis of ''Px''CBM91 exhibited a β-sandwich fold consisted of 12 β-strands and two opposing antiparallel beta sheets<cite>Ito2023</cite>. The concave surface and loops around it connecting the β-strands possesse several hydrophobic amino acid residues, the surface is expected to be the binding site.<br />
== Functionalities == <br />
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.<br />
Paenibacillus xylaniclastuicus was isolated from anaerobic digester fed with pineapple waste and grows with xylose as sole carbon source.<br />
Xylosidases, like GH43, which produce xylose from xylan and xylooligosaccharides and connects to CBM91 is one of vial enzymes. Therefore, CM91 would contribute to produce the carbon sources for the growth of xylolytic bacteria.<br />
<br />
<br />
<br />
== Family Firsts ==<br />
;First Identified:''Px''CBM91 from ''Px''Xyl43A of ''Paenibacillus xynaniclasticus'' strain TW1 <cite>Ito2022</cite>.<br />
;First Structural Characterization: β-D-xylosidase, a family 43 glycoside hydrolase from ''Clostridium acetobutylicum'' ATCC 824 [{{PDBlink}}1Y7B PDB ID 1Y7B]. <br />
<br />
== References ==<br />
<biblio><br />
#Ito2022 pmid=36312872<br />
</biblio><br />
<biblio><br />
#Ito2023 Ito, D., 2023. Characterization of plant cell wall degrading enzymes from Paenibacillus sp. Ph. D. Mie University.https://dl.ndl.go.jp/pid/12910195/1/1<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Carbohydrate Binding Module Families|CBM091]]</div>Daichi Itohttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_91&diff=18350Carbohydrate Binding Module Family 912024-08-31T17:54:34Z<p>Daichi Ito: </p>
<hr />
<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Daichi Ito|Daichi Ito]]<br />
* [[Responsible Curator]]: [[User:Elizabeth Ficko-Blean|Elizabeth Ficko-Blean]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM91.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
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>.<br />
<br />
== Structural Features ==<br />
[[Image:The_structure_of_PxXyl43A.png|thumb|300px|right|'''Figure 1. The structure of ''Px''Xyl43A and CBM91. <br />
'''The prediction structure by Alpha Fold 2 of CBM91(red). This CBM91 is appended to the catalytic domain of ''Px''Xyl43A(green).]]<br />
Alpha Fold 2 structure analysis of ''Px''CBM91 exhibited a β-sandwich fold consisted of 12 β-strands and two opposing antiparallel beta sheets<cite>Ito2023</cite>. The concave surface and loops around it connecting the β-strands possesse several hydrophobic amino acid residues, the surface is expected to be the binding site.<br />
== Functionalities == <br />
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.<br />
Paenibacillus xylaniclastuicus was isolated from anaerobic digester fed with pineapple waste and grows with xylose as sole carbon source.<br />
Xylosidases, like GH43, which produce xylose from xylan and xylooligosaccharides and connects to CBM91 is one of vial enzymes. Therefore, CM91 would contribute to produce the carbon sources for the growth of xylolytic bacteria.<br />
<br />
<br />
<br />
== Family Firsts ==<br />
;First Identified:''Px''CBM91 from ''Px''Xyl43A of ''Paenibacillus xynaniclasticus'' strain TW1 <cite>Ito2022</cite>.<br />
;First Structural Characterization: β-D-xylosidase, a family 43 glycoside hydrolase from ''Clostridium acetobutylicum'' ATCC 824 [{{PDBlink}}1Y7B PDB ID 1Y7B]. <br />
<br />
== References ==<br />
<biblio><br />
#Ito2022 pmid=36312872<br />
</biblio><br />
<biblio><br />
#Ito2023 Ito, D., 2023. Characterization of plant cell wall degrading enzymes from Paenibacillus sp. Ph. D. Mie University.<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Carbohydrate Binding Module Families|CBM091]]</div>Daichi Itohttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_91&diff=18349Carbohydrate Binding Module Family 912024-08-31T17:53:50Z<p>Daichi Ito: </p>
<hr />
<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Daichi Ito|Daichi Ito]]<br />
* [[Responsible Curator]]: [[User:Elizabeth Ficko-Blean|Elizabeth Ficko-Blean]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM91.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
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>.<br />
<br />
== Structural Features ==<br />
[[Image:The_structure_of_PxXyl43A.png|thumb|300px|right|'''Figure 1. The structure of ''Px''Xyl43A and CBM91. <br />
'''The prediction structure by Alpha Fold 2 of CBM91(red). This CBM91 is appended to the catalytic domain of ''Px''Xyl43A(green).]]<br />
Alpha Fold 2 structure analysis of ''Px''CBM91 exhibited a β-sandwich fold consisted of 12 β-strands and two opposing antiparallel beta sheets<cite>Ito2023</cite>. The concave surface and loops around it connecting the β-strands possesse several hydrophobic amino acid residues, the surface is expected to be the binding site.<br />
== Functionalities == <br />
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.<br />
Paenibacillus xylaniclastuicus was isolated from anaerobic digester fed with pineapple waste and grows with xylose as sole carbon source.<br />
Xylosidases, like GH43, which produce xylose from xylan and xylooligosaccharides and connects to CBM91 is one of vial enzymes. Therefore, CM91 would contribute to produce the carbon sources for the growth of xylolytic bacteria.<br />
<br />
<br />
<br />
== Family Firsts ==<br />
;First Identified:''Px''CBM91 from ''Px''Xyl43A of ''Paenibacillus xynaniclasticus'' strain TW1 <cite>Ito2022</cite>.<br />
;First Structural Characterization: β-D-xylosidase, a family 43 glycoside hydrolase from ''Clostridium acetobutylicum'' ATCC 824 [{{PDBlink}}1Y7B PDB ID 1Y7B]. <br />
<br />
== References ==<br />
<biblio><br />
#Ito2022 pmid=36312872<br />
</biblio><br />
<biblio><br />
#Ito 2023 Ito, D., 2023. Characterization of plant cell wall degrading enzymes from Paenibacillus sp. Ph. D. Mie University.<br />
<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Carbohydrate Binding Module Families|CBM091]]</div>Daichi Itohttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_91&diff=18348Carbohydrate Binding Module Family 912024-08-31T17:43:17Z<p>Daichi Ito: </p>
<hr />
<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Daichi Ito|Daichi Ito]]<br />
* [[Responsible Curator]]: [[User:Elizabeth Ficko-Blean|Elizabeth Ficko-Blean]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM91.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
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>.<br />
<br />
== Structural Features ==<br />
[[Image:The_structure_of_PxXyl43A.png|thumb|300px|right|'''Figure 1. The structure of ''Px''Xyl43A and CBM91. <br />
'''The prediction structure by Alpha Fold 2 of CBM91(red). This CBM91 is appended to the catalytic domain of ''Px''Xyl43A(green).]]<br />
Alpha Fold 2 structure analysis of ''Px''CBM91 exhibited a β-sandwich fold consisted of 12 β-strands and two opposing antiparallel beta sheets. The concave surface and loops around it connecting the β-strands possesse several hydrophobic amino acid residues, the surface is expected to be the binding site.<br />
== Functionalities == <br />
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.<br />
Paenibacillus xylaniclastuicus was isolated from anaerobic digester fed with pineapple waste and grows with xylose as sole carbon source.<br />
Xylosidases, like GH43, which produce xylose from xylan and xylooligosaccharides and connects to CBM91 is one of vial enzymes. Therefore, CM91 would contribute to produce the carbon sources for the growth of xylolytic bacteria.<br />
<br />
<br />
<br />
== Family Firsts ==<br />
;First Identified:''Px''CBM91 from ''Px''Xyl43A of ''Paenibacillus xynaniclasticus'' strain TW1 <cite>Ito2022</cite>.<br />
;First Structural Characterization: β-D-xylosidase, a family 43 glycoside hydrolase from ''Clostridium acetobutylicum'' ATCC 824 [{{PDBlink}}1Y7B PDB ID 1Y7B]. <br />
<br />
== References ==<br />
<biblio><br />
#Ito2022 pmid=36312872<br />
</biblio><br />
<br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Carbohydrate Binding Module Families|CBM091]]</div>Daichi Itohttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_91&diff=18347Carbohydrate Binding Module Family 912024-08-31T17:42:46Z<p>Daichi Ito: </p>
<hr />
<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Daichi Ito|Daichi Ito]]<br />
* [[Responsible Curator]]: [[User:Elizabeth Ficko-Blean|Elizabeth Ficko-Blean]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM91.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
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>.<br />
<br />
== Structural Features ==<br />
[[Image:The_structure_of_PxXyl43A.png|thumb|300px|right|'''Figure 1. The structure of ''Px''Xyl43A and CBM91. <br />
'''The prediction structure by Alpha Fold 2 of CBM91(red). This CBM91 is appended to the catalytic domain of ''Px''Xyl43A(green).]]<br />
Alpha Fold 2 structure analysis of ''Px''CBM91 exhibited a β-sandwich fold consisted of 12 β-strands and two opposing antiparallel beta sheets. The concave surface and loops around it connecting the β-strands possesse several hydrophobic amino acid residues, the surface is expected to be the binding site.<br />
== Functionalities == <br />
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.<br />
Paenibacillus xylaniclastuicus was isolated from anaerobic digester fed with pineapple waste and grows with xylose as sole carbon source.<br />
Xylosidases, like GH43, which produce xylose from xylan and xylooligosaccharides and connects to CBM91 is one of vial enzymes. Therefore, CM91 would contribute to produce the carbon sources for the growth of xylolytic bacteria.<br />
<br />
<br />
<br />
== Family Firsts ==<br />
;First Identified:''Px''CBM91 from ''Px''Xyl43A of ''Paenibacillus xynaniclasticus'' strain TW1 <cite>Ito2022</cite>.<br />
;First Structural Characterization: β-D-xylosidase, a family 43 glycoside hydrolase from ''Clostridium acetobutylicum'' ATCC 824 [{{PDBlink}}1Y7B PDB ID 1Y7B]. <br />
<br />
== References ==<br />
<biblio><br />
#Ito2022 pmid=36312872<br />
</biblio><br />
<br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Carbohydrate Binding Module Families|CBM091]]</div>Daichi Itohttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_91&diff=18130Carbohydrate Binding Module Family 912024-06-28T16:16:38Z<p>Daichi Ito: </p>
<hr />
<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Daichi Ito|Daichi Ito]]<br />
* [[Responsible Curator]]: [[User:Elizabeth Ficko-Blean|Elizabeth Ficko-Blean]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM91.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
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>.<br />
<br />
== Structural Features ==<br />
[[Image:The_structure_of_PxXyl43A.png|thumb|300px|right|'''Figure 1. The structure of ''Px''Xyl43A and CBM91. <br />
'''The prediction structure by Alpha Fold 2 of CBM91(red). This CBM91 is appended to the catalytic domain of ''Px''Xyl43A(green).]]<br />
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.<br />
== Functionalities == <br />
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.<br />
<br />
<br />
== Family Firsts ==<br />
;First Identified<br />
:''Px''CBM91 from ''Px''Xyl43A of ''Paenibacillus xynaniclasticus'' strain TW1 <cite>Ito2022</cite>.<br />
;First Structural Characterization<br />
: β-D-xylosidase, a family 43 glycoside hydrolase from ''Clostridium acetobutylicum'' ATCC 824 [{{PDBlink}}1Y7B PDB ID 1Y7B]. <br />
<br />
== References ==<br />
<biblio><br />
#Ito2022 pmid=36312872<br />
</biblio><br />
<br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Carbohydrate Binding Module Families|CBM091]]</div>Daichi Itohttps://www.cazypedia.org/index.php?title=User:Daichi_Ito&diff=17956User:Daichi Ito2024-04-23T14:28:43Z<p>Daichi Ito: </p>
<hr />
<div>[[Image:DaichiIto.jpg|200px|right]]<br />
<br />
I am a resarcher in Mie Prefecture Industrial Research Institute in Mie Prefecture, Japan. I recieved Ph.D degree in 2023 from Graduate School of Bioresources, Mie University in Mie, Japan. My home page is [https://sites.google.com/view/hakkou-ito/curriculum-vitae/ here]. My research is about plant cell wall degrading enzymes from bacteria<cite>Ito2022-1</cite>. So far, I studied a glycoside hydrolase, carbohydrate-binding modules and a lytic polysaccharide monooxygenase<cite>Ito2023-1</cite>. I characterized [[CBM91]] <cite>Ito2022-2</cite>.<br />
<br />
<br />
<br />
<br />
<br />
----<br />
<br />
<biblio><br />
#Ito2022-1 pmid=35168167<br />
#Ito2022-2 pmid=36312872<br />
#Ito2023-1 pmid=37033115<br />
<br />
</biblio><br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Ito,Daichi]]</div>Daichi Itohttps://www.cazypedia.org/index.php?title=User:Daichi_Ito&diff=17955User:Daichi Ito2024-04-23T14:28:04Z<p>Daichi Ito: </p>
<hr />
<div>[[Image:DaichiIto.jpg|200px|right]]<br />
<br />
I am a resarcher in Mie Prefecture Industrial Research Institute in Mie Prefecture, Japan. I recieved Ph.D degree in 2023 from Graduate School of Bioresources, Mie University in Mie, Japan. My home page is [https://sites.google.com/view/hakkou-ito/curriculum-vitae/ here]. My research is about plant cell wall degrading enzymes from bacteria. So far, I studied a glycoside hydrolase, carbohydrate-binding modules and a lytic polysaccharide monooxygenase<cite>Ito2023-1</cite>. I characterized [[CBM91]] <cite>Ito2022</cite>.<br />
<br />
<br />
<br />
<br />
<br />
----<br />
<br />
<biblio><br />
#Ito2022-1 pmid=35168167<br />
<br />
#Ito2022-2 pmid=36312872<br />
#Ito2023-1 pmid=37033115<br />
<br />
</biblio><br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Ito,Daichi]]</div>Daichi Itohttps://www.cazypedia.org/index.php?title=User:Daichi_Ito&diff=17954User:Daichi Ito2024-04-23T14:26:59Z<p>Daichi Ito: </p>
<hr />
<div>[[Image:DaichiIto.jpg|200px|right]]<br />
<br />
I am a resarcher in Mie Prefecture Industrial Research Institute in Mie Prefecture, Japan. I recieved Ph.D degree in 2023 from Graduate School of Bioresources, Mie University in Mie, Japan. My home page is [https://sites.google.com/view/hakkou-ito/curriculum-vitae/ here]. My research is about plant cell wall degrading enzymes from bacteria. So far, I studied a glycoside hydrolase, carbohydrate-binding modules and a lytic polysaccharide monooxygenase<cite>Ito2023-1</cite>. I characterized [[CBM91]] <cite>Ito2022</cite>.<br />
<br />
<br />
<br />
<br />
<br />
----<br />
<br />
<biblio><br />
#Ito2022 pmid=36312872<br />
#Ito2023-1 pmid=37033115<br />
<br />
</biblio><br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Ito,Daichi]]</div>Daichi Itohttps://www.cazypedia.org/index.php?title=User:Daichi_Ito&diff=17953User:Daichi Ito2024-04-23T14:26:42Z<p>Daichi Ito: </p>
<hr />
<div>[[Image:DaichiIto.jpg|200px|right]]<br />
<br />
I am a resarcher in Mie Prefecture Industrial Research Institute in Mie Prefecture, Japan. I recieved Ph.D degree in 2023 from Graduate School of Bioresources, Mie University in Mie, Japan. My home page is [https://sites.google.com/view/hakkou-ito/curriculum-vitae/ here]. My research is about plant cell wall degrading enzymes from bacteria. So far, I studied a glycoside hydrolase, carbohydrate-binding modules and a lytic polysaccharide monooxygenase<cite>Ito2022</cite>. I characterized [[CBM91]] <cite>Ito2022</cite>.<br />
<br />
<br />
<br />
<br />
<br />
----<br />
<br />
<biblio><br />
#Ito2022 pmid=36312872<br />
#Ito2023-1 pmid=37033115<br />
<br />
</biblio><br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Ito,Daichi]]</div>Daichi Itohttps://www.cazypedia.org/index.php?title=User:Daichi_Ito&diff=17952User:Daichi Ito2024-04-23T14:21:48Z<p>Daichi Ito: </p>
<hr />
<div>[[Image:DaichiIto.jpg|200px|right]]<br />
<br />
I am a resarcher in Mie Prefecture Industrial Research Institute in Mie Prefecture, Japan. I recieved Ph.D degree in 2023 from Graduate School of Bioresources, Mie University in Mie, Japan. My home page is [https://sites.google.com/view/hakkou-ito/curriculum-vitae/ here]. My research is about plant cell wall degrading enzymes from bacteria. So far, I studied a glycoside hydrolase, carbohydrate-binding modules and a lytic polysaccharide monooxygenase. I characterized [[CBM91]] <cite>Ito2022</cite>.<br />
<br />
<br />
<br />
<br />
<br />
----<br />
<br />
<biblio><br />
#Ito2022 pmid=36312872<br />
<br />
</biblio><br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Ito,Daichi]]</div>Daichi Itohttps://www.cazypedia.org/index.php?title=User:Daichi_Ito&diff=17951User:Daichi Ito2024-04-23T14:20:57Z<p>Daichi Ito: </p>
<hr />
<div>[[Image:DaichiIto.jpg|200px|right]]<br />
<br />
I am a resarcher in Mie Prefecture Industrial Research Institute in Mie Prefecture, Japan. I recieved Ph.D degree in Graduate School of Bioresources, Mie University in Mie, Japan. My home page is [https://sites.google.com/view/hakkou-ito/curriculum-vitae/ here]. My research is about plant cell wall degrading enzymes from bacteria. So far, I studied a glycoside hydrolase, carbohydrate-binding modules and a lytic polysaccharide monooxygenase. I characterized [[CBM91]] <cite>Ito2022</cite>.<br />
<br />
<br />
<br />
<br />
<br />
----<br />
<br />
<biblio><br />
#Ito2022 pmid=36312872<br />
<br />
</biblio><br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Ito,Daichi]]</div>Daichi Itohttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_91&diff=17950Carbohydrate Binding Module Family 912024-04-23T14:11:48Z<p>Daichi Ito: </p>
<hr />
<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Daichi Ito|Daichi Ito]]<br />
* [[Responsible Curator]]: [[User:Elizabeth Ficko-Blean|Elizabeth Ficko-Blean]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM91.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
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>.<br />
<br />
== Structural Features ==<br />
[[Image:The_structure_of_PxXyl43A.png|thumb|300px|right|'''Figure 1. The structure of ''Px''Xyl43A and CBM91. <br />
'''The prediction structure by Alpha Fold 2 of CBM91(red). This CBM91 is appended to the catalytic domain of ''Px''Xyl43A(green).]]<br />
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.<br />
== Functionalities == <br />
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.<br />
<br />
<br />
== Family Firsts ==<br />
;First Identified<br />
:''Px''CBM91 from ''Px''Xyl43A of ''Paenibacillus xynaniclasticus'' strain TW1 <cite>Ito2022</cite>.<br />
;First Structural Characterization<br />
: β-D-xylosidase, a family 43 glycoside hydrolase from ''Clostridium acetobutylicum'' ATCC 824 [{{PDBlink}}1Y7B PDB ID 1Y7B]. <br />
<br />
== References ==<br />
<biblio><br />
#Ito2022 pmid=36312872<br />
</biblio><br />
<br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Carbohydrate Binding Module Families|CBM091]]</div>Daichi Itohttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_91&diff=17949Carbohydrate Binding Module Family 912024-04-23T14:10:55Z<p>Daichi Ito: </p>
<hr />
<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Daichi Ito|Daichi Ito]]<br />
* [[Responsible Curator]]: [[User:Elizabeth Ficko-Blean|Elizabeth Ficko-Blean]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM91.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
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>.<br />
<br />
== Structural Features ==<br />
[[Image:The_structure_of_PxXyl43A.png|thumb|300px|right|'''Figure 1. The structure of CBM91. <br />
'''The prediction structure by Alpha Fold 2 of CBM91(red). This CBM91 is appended to the catalytic domain of ''Px''Xyl43A(green).]]<br />
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.<br />
== Functionalities == <br />
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.<br />
<br />
<br />
== Family Firsts ==<br />
;First Identified<br />
:''Px''CBM91 from ''Px''Xyl43A of ''Paenibacillus xynaniclasticus'' strain TW1 <cite>Ito2022</cite>.<br />
;First Structural Characterization<br />
: β-D-xylosidase, a family 43 glycoside hydrolase from ''Clostridium acetobutylicum'' ATCC 824 [{{PDBlink}}1Y7B PDB ID 1Y7B]. <br />
<br />
== References ==<br />
<biblio><br />
#Ito2022 pmid=36312872<br />
</biblio><br />
<br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Carbohydrate Binding Module Families|CBM091]]</div>Daichi Itohttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_91&diff=17948Carbohydrate Binding Module Family 912024-04-23T14:10:24Z<p>Daichi Ito: </p>
<hr />
<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Daichi Ito|Daichi Ito]]<br />
* [[Responsible Curator]]: [[User:Elizabeth Ficko-Blean|Elizabeth Ficko-Blean]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM91.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
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>.<br />
<br />
== Structural Features ==<br />
[[Image:The_structure_of_PxXyl43A.png|thumb|300px|right|'''Figure 1. The structure of CBM91. <br />
'''The prediction structure by Alpha Fold 2 of CBM91(red). This CBM91 is appended to the catalytic domain of ''Px''Xyl43A(green).]]<br />
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.<br />
== Functionalities == <br />
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.<br />
<br />
<br />
== Family Firsts ==<br />
;First Identified<br />
:''Px''CBM91 from ''Px''xyl43A of ''Paenibacillus xynaniclasticus'' strain TW1 <cite>Ito2022</cite>.<br />
;First Structural Characterization<br />
: β-D-xylosidase, a family 43 glycoside hydrolase from ''Clostridium acetobutylicum'' ATCC 824 [{{PDBlink}}1Y7B PDB ID 1Y7B]. <br />
<br />
== References ==<br />
<biblio><br />
#Ito2022 pmid=36312872<br />
</biblio><br />
<br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Carbohydrate Binding Module Families|CBM091]]</div>Daichi Itohttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_91&diff=17947Carbohydrate Binding Module Family 912024-04-23T14:08:59Z<p>Daichi Ito: </p>
<hr />
<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Daichi Ito|Daichi Ito]]<br />
* [[Responsible Curator]]: [[User:Elizabeth Ficko-Blean|Elizabeth Ficko-Blean]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM91.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
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>.<br />
<br />
== Structural Features ==<br />
[[Image:The_structure_of_PxXyl43A.png|thumb|300px|right|'''Figure 1. The structure of CBM91. <br />
'''The prediction structure by Alpha Fold 2 of CBM91(red). This CBM91 is appended to the catalytic domain of ''Px''Xyl43A(green).]]<br />
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.<br />
== Functionalities == <br />
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.<br />
<br />
<br />
== Family Firsts ==<br />
;First Identified<br />
:''Px''CBM91 from ''Paenibacillus xynaniclasticus'' strain TW1 <cite>Ito2022</cite>.<br />
;First Structural Characterization<br />
: β-D-xylosidase, a family 43 glycoside hydrolase from ''Clostridium acetobutylicum'' ATCC 824 [{{PDBlink}}1Y7B PDB ID 1Y7B]. <br />
<br />
== References ==<br />
<biblio><br />
#Ito2022 pmid=36312872<br />
</biblio><br />
<br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Carbohydrate Binding Module Families|CBM091]]</div>Daichi Itohttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_91&diff=17946Carbohydrate Binding Module Family 912024-04-23T14:08:12Z<p>Daichi Ito: </p>
<hr />
<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Daichi Ito|Daichi Ito]]<br />
* [[Responsible Curator]]: [[User:Elizabeth Ficko-Blean|Elizabeth Ficko-Blean]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM91.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
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>.<br />
<br />
== Structural Features ==<br />
[[Image:The_structure_of_PxXyl43A.png|thumb|300px|right|'''Figure. The structure of CBM91. <br />
'''The prediction structure by Alpha Fold 2 of CBM91(red). This CBM91 is appended to the catalytic domain of ''Px''Xyl43A(green).]]<br />
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.<br />
== Functionalities == <br />
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.<br />
<br />
<br />
== Family Firsts ==<br />
;First Identified<br />
:''Px''CBM91 from ''Paenibacillus xynaniclasticus'' strain TW1 <cite>Ito2022</cite>.<br />
;First Structural Characterization<br />
: β-D-xylosidase, a family 43 glycoside hydrolase from ''Clostridium acetobutylicum'' ATCC 824 [{{PDBlink}}1Y7B PDB ID 1Y7B]. <br />
<br />
== References ==<br />
<biblio><br />
#Ito2022 pmid=36312872<br />
</biblio><br />
<br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Carbohydrate Binding Module Families|CBM091]]</div>Daichi Itohttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_91&diff=17945Carbohydrate Binding Module Family 912024-04-23T13:14:01Z<p>Daichi Ito: </p>
<hr />
<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Daichi Ito|Daichi Ito]]<br />
* [[Responsible Curator]]: [[User:Elizabeth Ficko-Blean|Elizabeth Ficko-Blean]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM91.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
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>.<br />
<br />
== Structural Features ==<br />
[[Image:The_structure_of_PxXyl43A.png|thumb|300px|right|'''Figure. The structure of CBM91. <br />
'''The prediction structure by Alpha Fold 2 of CBM91(red). This CBM91 is appended to the catalytic domain of ''Px''Xyl43A(green).]]<br />
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.<br />
== Functionalities == <br />
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.<br />
<br />
<br />
== Family Firsts ==<br />
;First Identified<br />
:''Px''CBM91 from ''Paenibacillus xynaniclasticus'' strain TW1 <cite>Ito2022</cite>.<br />
;First Structural Characterization<br />
: β-D-xylosidase, a family 43 glycoside hydrolase from ''Clostridium acetobutylicum'' ATCC 824 [{{PDBlink}}1Y7B PDB ID 1Y7B]. <br />
<br />
== References ==<br />
<biblio><br />
#Ito2022 pmid=36312872<br />
</biblio><br />
<br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Carbohydrate Binding Module Families|CBM091]]</div>Daichi Itohttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_91&diff=17944Carbohydrate Binding Module Family 912024-04-23T13:11:31Z<p>Daichi Ito: </p>
<hr />
<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Daichi Ito|Daichi Ito]]<br />
* [[Responsible Curator]]: [[User:Elizabeth Ficko-Blean|Elizabeth Ficko-Blean]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM91.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
CBM91 bind oat spelt xylan with ''K''<sub>a</sub> value of 2.0×10<sup>-5</sup> M<sup>-1</sup>, 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 <cite>Ito2022</cite>.<br />
<br />
== Structural Features ==<br />
[[Image:The_structure_of_PxXyl43A.png|thumb|300px|right|'''Figure. The structure of CBM91. <br />
'''The prediction structure by Alpha Fold 2 of CBM91(red). This CBM91 is appended to the catalytic domain of ''Px''Xyl43A(green).]]<br />
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.<br />
== Functionalities == <br />
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.<br />
<br />
<br />
== Family Firsts ==<br />
;First Identified<br />
:''Px''CBM91 from ''Paenibacillus xynaniclasticus'' strain TW1 <cite>Ito2022</cite>.<br />
;First Structural Characterization<br />
: β-D-xylosidase, a family 43 glycoside hydrolase from ''Clostridium acetobutylicum'' ATCC 824 [{{PDBlink}}1Y7B PDB ID 1Y7B]. <br />
<br />
== References ==<br />
<biblio><br />
#Ito2022 pmid=36312872<br />
</biblio><br />
<br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Carbohydrate Binding Module Families|CBM091]]</div>Daichi Itohttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_91&diff=17943Carbohydrate Binding Module Family 912024-04-23T12:37:25Z<p>Daichi Ito: </p>
<hr />
<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Daichi Ito|Daichi Ito]]<br />
* [[Responsible Curator]]: [[User:Elizabeth Ficko-Blean|Elizabeth Ficko-Blean]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM91.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
CBM91 bind oat spelt xylan with ''K''<sub>a</sub> value of 2.0×10<sup>-5</sup> M<sup>-1</sup>, 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 <cite>Ito2022</cite>.<br />
<br />
== Structural Features ==<br />
[[Image:The_structure_of_PxXyl43A.png|thumb|300px|right|'''Figure. The structure of CBM91. <br />
'''The prediction structure by Alpha Fold 2 of CBM91(red). This CBM91 is appended to the catalytic domain of ''Px''Xyl43A(green).]]<br />
* '''Fold: β-sandwich '''<br />
* '''Type: Type B ''' <br />
<br />
== Functionalities == <br />
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.<br />
<br />
<br />
== Family Firsts ==<br />
;First Identified<br />
:''Px''CBM91 from ''Paenibacillus xynaniclasticus'' strain TW1 <cite>Ito2022</cite>.<br />
;First Structural Characterization<br />
: β-D-xylosidase, a family 43 glycoside hydrolase from ''Clostridium acetobutylicum'' ATCC 824 [{{PDBlink}}1Y7B PDB ID 1Y7B]. <br />
<br />
== References ==<br />
<biblio><br />
#Ito2022 pmid=36312872<br />
</biblio><br />
<br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Carbohydrate Binding Module Families|CBM091]]</div>Daichi Itohttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_91&diff=17563Carbohydrate Binding Module Family 912023-10-20T13:13:57Z<p>Daichi Ito: </p>
<hr />
<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Daichi Ito|Daichi Ito]]<br />
* [[Responsible Curator]]: [[User:Elizabeth Ficko-Blean|Elizabeth Ficko-Blean]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM91.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
CBM91 bind oat spelt xylan with ''K''<sub>a</sub> value of 2.0×10<sup>-5</sup> M<sup>-1</sup>, 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 <cite>Ito2022</cite>.<br />
<br />
== Structural Features ==<br />
[[Image:The_structure_of_PxXyl43A.png|thumb|300px|right|'''Figure. The structure of CBM91. <br />
'''The prediction structure by Alpha Fold 2 of CBM91(red). This CBM91 is appended to the catalytic domain of ''Px''Xyl43A(green).]]<br />
* '''Fold: β-sandwich '''<br />
* '''Type: Type B ''' <br />
<br />
== Functionalities == <br />
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.<br />
<br />
<br />
== Family Firsts ==<br />
;First Identified<br />
:CBM91 from ''Paenibacillus xynaniclasticus'' strain TW1 <cite>Ito2022</cite>.<br />
;First Structural Characterization<br />
: β-D-xylosidase, a family 43 glycoside hydrolase from ''Clostridium acetobutylicum'' ATCC 824 [{{PDBlink}}1Y7B PDB ID 1Y7B]. <br />
<br />
== References ==<br />
<biblio><br />
#Ito2022 pmid=36312872<br />
</biblio><br />
<br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Carbohydrate Binding Module Families|CBM091]]</div>Daichi Itohttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_91&diff=17562Carbohydrate Binding Module Family 912023-10-20T12:36:12Z<p>Daichi Ito: </p>
<hr />
<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Daichi Ito|Daichi Ito]]<br />
* [[Responsible Curator]]: [[User:Elizabeth Ficko-Blean|Elizabeth Ficko-Blean]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM91.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
CBM91 bind oat spelt xylan with ''K''<sub>a</sub> value of 2.0×10<sup>-5</sup> M<sup>-1</sup>, 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 <cite>Ito2022</cite>.<br />
<br />
== Structural Features ==<br />
[[Image:The_structure_of_PxXyl43A.png|thumb|300px|right|'''Figure. The structure of CBM91. <br />
'''The prediction structure by Alpha Fold 2 of CBM91(red). This CBM91 is appended to the catalytic domain of ''Px''Xyl43A(green).]]<br />
* '''Fold: β-sandwich '''<br />
* '''Type: Type B ''' <br />
<br />
== Functionalities == <br />
== Family Firsts ==<br />
;First Identified<br />
:CBM91 from ''Paenibacillus xynaniclasticus'' strain TW1 <cite>Ito2022</cite>.<br />
;First Structural Characterization<br />
: β-D-xylosidase, a family 43 glycoside hydrolase from ''Clostridium acetobutylicum'' ATCC 824 [{{PDBlink}}1Y7B PDB ID 1Y7B]. <br />
<br />
== References ==<br />
<biblio><br />
#Ito2022 pmid=36312872<br />
</biblio><br />
<br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Carbohydrate Binding Module Families|CBM091]]</div>Daichi Itohttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_91&diff=17561Carbohydrate Binding Module Family 912023-10-20T12:35:18Z<p>Daichi Ito: </p>
<hr />
<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Daichi Ito|Daichi Ito]]<br />
* [[Responsible Curator]]: [[User:Elizabeth Ficko-Blean|Elizabeth Ficko-Blean]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM91.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
CBM91 bind oat spelt xylan with ''K''<sub>a</sub> value of 2.0×10<sup>-5</sup> M<sup>-1</sup>, 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 <cite>Ito2022</cite>.<br />
<br />
== Structural Features ==<br />
[[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).]]<br />
* '''Fold: β-sandwich '''<br />
* '''Type: Type B ''' <br />
<br />
== Functionalities == |<br />
== Family Firsts ==<br />
;First Identified<br />
:CBM91 from ''Paenibacillus xynaniclasticus'' strain TW1 <cite>Ito2022</cite>.<br />
;First Structural Characterization<br />
: β-D-xylosidase, a family 43 glycoside hydrolase from ''Clostridium acetobutylicum'' ATCC 824 [{{PDBlink}}1Y7B PDB ID 1Y7B]. <br />
<br />
== References ==<br />
<biblio><br />
#Ito2022 pmid=36312872<br />
</biblio><br />
<br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Carbohydrate Binding Module Families|CBM091]]</div>Daichi Itohttps://www.cazypedia.org/index.php?title=File:The_structure_of_PxXyl43A.png&diff=17560File:The structure of PxXyl43A.png2023-10-20T12:13:32Z<p>Daichi Ito: </p>
<hr />
<div></div>Daichi Itohttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_91&diff=17017Carbohydrate Binding Module Family 912023-01-15T14:44:44Z<p>Daichi Ito: </p>
<hr />
<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Daichi Ito|Daichi Ito]]<br />
* [[Responsible Curator]]: [[User:Elizabeth Ficko-Blean|Elizabeth Ficko-Blean]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM91.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
CBM91 bind oat spelt xylan with ''K''<sub>a</sub> value of 2.0×10<sup>-5</sup> M<sup>-1</sup>, 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 <cite>Ito2022</cite>.<br />
<br />
== Structural Features ==<br />
''Content in this section should include, in paragraph form, a description of:''<br />
* '''Fold: β-sandwich '''<br />
* '''Type: Type B ''' <br />
<br />
== Functionalities == <br />
<br />
== Family Firsts ==<br />
;First Identified<br />
:CBM91 from ''Paenibacillus xynaniclasticus'' strain TW1 <cite>Ito2022</cite>.<br />
;First Structural Characterization<br />
: β-D-xylosidase, a family 43 glycoside hydrolase from ''Clostridium acetobutylicum'' ATCC 824 [{{PDBlink}}1Y7B PDB ID 1Y7B]. <br />
<br />
== References ==<br />
<biblio><br />
#Ito2022 pmid=36312872<br />
</biblio><br />
<br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Carbohydrate Binding Module Families|CBM091]]</div>Daichi Itohttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_91&diff=17016Carbohydrate Binding Module Family 912023-01-15T14:42:17Z<p>Daichi Ito: </p>
<hr />
<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Daichi Ito|Daichi Ito]]<br />
* [[Responsible Curator]]: [[User:Elizabeth Ficko-Blean|Elizabeth Ficko-Blean]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM91.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
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 <cite>Ito2022</cite>.<br />
<br />
== Structural Features ==<br />
''Content in this section should include, in paragraph form, a description of:''<br />
* '''Fold: β-sandwich '''<br />
* '''Type: Type B ''' <br />
<br />
== Functionalities == <br />
<br />
== Family Firsts ==<br />
;First Identified<br />
:CBM91 from ''Paenibacillus xynaniclasticus'' strain TW1 <cite>Ito2022</cite>.<br />
;First Structural Characterization<br />
: β-D-xylosidase, a family 43 glycoside hydrolase from ''Clostridium acetobutylicum'' ATCC 824 [{{PDBlink}}1Y7B PDB ID 1Y7B]. <br />
<br />
== References ==<br />
<biblio><br />
#Ito2022 pmid=36312872<br />
</biblio><br />
<br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Carbohydrate Binding Module Families|CBM091]]</div>Daichi Itohttps://www.cazypedia.org/index.php?title=User:Daichi_Ito&diff=17013User:Daichi Ito2023-01-12T12:32:30Z<p>Daichi Ito: </p>
<hr />
<div>[[Image:DaichiIto.jpg|200px|right]]<br />
<br />
I am a Ph.D student at Laboratory of Fermentation Biology in Department of Life Sciences, Graduate School of Bioresources, Mie University in Mie, Japan. My home page is [https://sites.google.com/view/hakkou-ito/curriculum-vitae/ here]. My research is about plant cell wall degrading enzymes from bacteria. So far, I studied a glycoside hydrolase, carbohydrate-binding modules and a lytic polysaccharide monooxygenase. I characterized [[CBM91]] <cite>Ito2022</cite>.<br />
<br />
<br />
<br />
<br />
<br />
----<br />
<br />
<biblio><br />
#Ito2022 pmid=36312872<br />
<br />
</biblio><br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Ito,Daichi]]</div>Daichi Itohttps://www.cazypedia.org/index.php?title=User:Daichi_Ito&diff=16968User:Daichi Ito2023-01-07T11:05:26Z<p>Daichi Ito: </p>
<hr />
<div>[[Image:DaichiIto.jpg|200px|right]]<br />
<br />
I am a Ph.D student at Laboratory of Fermentation Biology in Department of Life Sciences, Graduate School of Bioresources, Mie University in Mie, Japan. My home page is [https://sites.google.com/view/hakkou-ito/ here] (Sorry. Japanese only). My research is about plant cell wall degrading enzymes from bacteria. So far, I studied a glycoside hydrolase, carbohydrate-binding modules and a lytic polysaccharide monooxygenase. I characterized CBM91 <cite>Ito2022</cite>.<br />
<br />
<br />
<br />
<br />
<br />
----<br />
<br />
<biblio><br />
#Ito2022 pmid=36312872<br />
<br />
</biblio><br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Ito,Daichi]]</div>Daichi Itohttps://www.cazypedia.org/index.php?title=User:Daichi_Ito&diff=16967User:Daichi Ito2023-01-07T08:33:08Z<p>Daichi Ito: </p>
<hr />
<div>[[Image:DaichiIto.jpg|200px|right]]<br />
<br />
I am a Ph.D student at Laboratory of Fermentation Biology in Department of Life Sciences, Graduate School of Bioresources, Mie University in Mie, Japan. My home page is here (Sorry. Japanese only).My research is about plant cell wall degrading enzymes from bacteria. So far, I studied a glycoside hydrolase, carbohydrate-binding modules and a lytic polysaccharide monooxygenase. I characterized CBM91 <cite>Ito2022</cite>.<br />
<br />
<br />
<br />
<br />
<br />
----<br />
<br />
<biblio><br />
#Ito2022 pmid=36312872<br />
<br />
</biblio><br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Ito,Daichi]]</div>Daichi Itohttps://www.cazypedia.org/index.php?title=File:DaichiIto.jpg&diff=16966File:DaichiIto.jpg2023-01-07T08:32:24Z<p>Daichi Ito: </p>
<hr />
<div>DaichiIto</div>Daichi Itohttps://www.cazypedia.org/index.php?title=User:Daichi_Ito&diff=16965User:Daichi Ito2023-01-07T08:26:49Z<p>Daichi Ito: </p>
<hr />
<div>I am a Ph.D student at Laboratory of Fermentation Biology in Department of Life Sciences, Graduate School of Bioresources, Mie University in Mie, Japan. My home page is here (Sorry. Japanese only).My research is about plant cell wall degrading enzymes from bacteria. So far, I studied a glycoside hydrolase, carbohydrate-binding modules and a lytic polysaccharide monooxygenase. I characterized CBM91 <cite>Ito2022</cite>.<br />
<br />
<br />
<br />
<br />
<br />
<br />
<br />
----<br />
<br />
<biblio><br />
#Ito2022 pmid=36312872<br />
<br />
</biblio><br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Ito,Daichi]]</div>Daichi Itohttps://www.cazypedia.org/index.php?title=User:Daichi_Ito&diff=16964User:Daichi Ito2023-01-07T07:47:36Z<p>Daichi Ito: </p>
<hr />
<div>[[Image:Blank_user-200px.png|200px|right]]<br />
''This is an empty template to help you get started with composing your User page.''<br />
<br />
You should begin by opening this page for editing by clicking on the Edit tab above. Your biography goes in this area of the page.<br />
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* See [[User:Gerlind_Sulzenbacher]] for an example. You may copy text from this example by opening the page in another browser window and clicking the "Edit" tab.<br />
* Add your publications in the list below using PubMed IDs and cite them in the text like this <cite>Gilbert2008</cite>.<br />
* Please upload a picture of yourself using the "Upload file" link in the Toolbox section of the left menu, and then replace the Image filename with your own.<br />
<br />
''More specific help on these steps is available from the links under the "For contributors" section of the left page menu.''<br />
<br />
I characterized CBM91 <cite>Ito2022</cite>.<br />
<br />
<br />
<br />
----<br />
<br />
<biblio><br />
#Gilbert2008 pmid=18430603<br />
#Ito2022 pmid=36312872<br />
<br />
</biblio><br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Ito,Daichi]]</div>Daichi Itohttps://www.cazypedia.org/index.php?title=User:Daichi_Ito&diff=16963User:Daichi Ito2023-01-07T07:45:01Z<p>Daichi Ito: </p>
<hr />
<div>[[Image:Blank_user-200px.png|200px|right]]<br />
''This is an empty template to help you get started with composing your User page.''<br />
<br />
You should begin by opening this page for editing by clicking on the Edit tab above. Your biography goes in this area of the page.<br />
<br />
* See [[User:Gerlind_Sulzenbacher]] for an example. You may copy text from this example by opening the page in another browser window and clicking the "Edit" tab.<br />
* Add your publications in the list below using PubMed IDs and cite them in the text like this <cite>Gilbert2008</cite>.<br />
* Please upload a picture of yourself using the "Upload file" link in the Toolbox section of the left menu, and then replace the Image filename with your own.<br />
<br />
''More specific help on these steps is available from the links under the "For contributors" section of the left page menu.''<br />
<br />
<br />
<br />
----<br />
<br />
<biblio><br />
#Gilbert2008 pmid=18430603<br />
<br />
</biblio><br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Ito,Daichi]]</div>Daichi Ito