https://www.cazypedia.org/api.php?action=feedcontributions&feedformat=atom&user=Guanchen+LiuCAZypedia - User contributions [en-ca]2026-05-05T04:19:14ZUser contributionsMediaWiki 1.35.10https://www.cazypedia.org/index.php?title=User:Guanchen_Liu&diff=18652User:Guanchen Liu2024-12-06T11:56:24Z<p>Guanchen Liu: </p>
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<div>[[File:Photo.jpg|100px|right]]<br />
Guanchen Liu obtained her bachelor's and master's degrees at Kyoto Institute of Technology. She is currently a Ph.D. student at the College of Food Science and Engineering, Ocean University of China, under the instruction of Prof. [[User:Yaoguang Chang|Yaoguang Chang]]. Her research focuses on the gene-mining and characterization of functional domains of [[Carbohydrate-active enzymes|CAZymes]] and [[carbohydrate-binding modules]] <cite>CAZypedia2018</cite>. She discovered and characterized the first member of [[GH174]] <cite>Liu2023a</cite> and [[CBM100]] <cite>Liu2023b</cite>.<br />
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== References ==<br />
<biblio><br />
#CAZypedia2018 pmid=29040563<br />
#Liu2023a pmid=36746582<br />
#Liu2023b pmid=37951443<br />
</biblio><br />
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<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Liu,Guanchen]]</div>Guanchen Liuhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_105&diff=18596Carbohydrate Binding Module Family 1052024-11-07T04:33:47Z<p>Guanchen Liu: </p>
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<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{CuratorApproved}}<br />
* [[Author]]: [[User:Guanchen Liu|Guanchen Liu]]<br />
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]<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}}CBM105.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
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== Ligand specificities ==<br />
The first member of family CBM105 (SoCBM105) was identified in the [[PL29]] multidomain chondroitinase SoChABC29 from ''Segatella oris'' <cite>Liu2024</cite>. SoCBM105 bound specifically to chondroitin sulfates (CSs) including CS-A and CS-C, while it was incapable of binding to other glycosaminoglycans or polyuronic acid substrates <cite>Liu2024</cite>.<br />
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== Structural Features ==<br />
[[File:CBM105 Fig.1.png|thumb|350px|right|'''Figure 1. Domain analysis of SoChABC29, the parent enzyme of SoCBM105 <cite>Jumper2021</cite>.''' The enzyme consists of a signal peptide (1-21 amino acids), a PL29 domain (66-380 amino acids) and a CBM105 domain (viz., SoCBM105; 555-785 amino acids).]]<br />
An AlphaFold2 <cite>Jumper2021</cite> model predicts that SoCBM105 has a β-sandwich fold (Fig.1).<br />
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== Functionalities == <br />
SoCBM105 is at the C-terminus domain of a [[PL29]] enzyme SoChABC29 that displays chondroitin sulfate ABC activity, consistent with the SoCBM105 specificity <cite>Liu2024</cite>. Biochemical characterization of SoChABC29 and the CBM-truncated enzyme revealed that the SoCBM105 enhances the catalytic activity, thermostability, and disaccharide proportion in the final enzymatic products of SoChABC29 <cite>Liu2024</cite>.<br />
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== Family Firsts ==<br />
;First Identified: Binding to chondroitin sulfate in the CBM105 family was first characterized and identified for SoCBM105 from the ''S. oris'' [[PL29]] chondroitinase <cite>Liu2024</cite>.<br />
;First Structural Characterization: No experimentally determined three-dimensional structure has been solved in this CBM family.<br />
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== References ==<br />
<biblio><br />
#Liu2024 pmid=38777025<br />
#Jumper2021 pmid=34265844<br />
</biblio><br />
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<!-- Do not delete this Category tag --><br />
[[Category:Carbohydrate Binding Module Families|CBM105]]<br />
<!-- ATTENTION: Make sure to replace "nnn" with a three digit family number, e.g. "032" or "105" etc., for proper sorting of the page by family number. --></div>Guanchen Liuhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_105&diff=18595Carbohydrate Binding Module Family 1052024-11-07T04:33:22Z<p>Guanchen Liu: </p>
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<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{CuratorApproved}}<br />
* [[Author]]: [[User:Guanchen Liu|Guanchen Liu]]<br />
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]<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}}CBM105.html<br />
|}<br />
</div><br />
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== Ligand specificities ==<br />
The first member of family CBM105 (SoCBM105) was identified in the [[PL29]] multidomain chondroitinase SoChABC29 from ''Segatella oris'' <cite>Liu2024</cite>. SoCBM105 bound specifically to chondroitin sulfates (CSs) including CS-A and CS-C, while it was incapable of binding to other glycosaminoglycans or polyuronic acid substrates <cite>Liu2024</cite>.<br />
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== Structural Features ==<br />
[[File:CBM105 Fig.1.png|thumb|350px|right|'''Figure 1. Domain analysis of SoChABC29, the parent enzyme of SoCBM105. <cite>Jumper2021</cite>''' The enzyme consists of a signal peptide (1-21 amino acids), a PL29 domain (66-380 amino acids) and a CBM105 domain (viz., SoCBM105; 555-785 amino acids).]]<br />
An AlphaFold2 <cite>Jumper2021</cite> model predicts that SoCBM105 has a β-sandwich fold (Fig.1).<br />
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== Functionalities == <br />
SoCBM105 is at the C-terminus domain of a [[PL29]] enzyme SoChABC29 that displays chondroitin sulfate ABC activity, consistent with the SoCBM105 specificity <cite>Liu2024</cite>. Biochemical characterization of SoChABC29 and the CBM-truncated enzyme revealed that the SoCBM105 enhances the catalytic activity, thermostability, and disaccharide proportion in the final enzymatic products of SoChABC29 <cite>Liu2024</cite>.<br />
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== Family Firsts ==<br />
;First Identified: Binding to chondroitin sulfate in the CBM105 family was first characterized and identified for SoCBM105 from the ''S. oris'' [[PL29]] chondroitinase <cite>Liu2024</cite>.<br />
;First Structural Characterization: No experimentally determined three-dimensional structure has been solved in this CBM family.<br />
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== References ==<br />
<biblio><br />
#Liu2024 pmid=38777025<br />
#Jumper2021 pmid=34265844<br />
</biblio><br />
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<!-- Do not delete this Category tag --><br />
[[Category:Carbohydrate Binding Module Families|CBM105]]<br />
<!-- ATTENTION: Make sure to replace "nnn" with a three digit family number, e.g. "032" or "105" etc., for proper sorting of the page by family number. --></div>Guanchen Liuhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_105&diff=18594Carbohydrate Binding Module Family 1052024-11-07T04:31:22Z<p>Guanchen Liu: </p>
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<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{CuratorApproved}}<br />
* [[Author]]: [[User:Guanchen Liu|Guanchen Liu]]<br />
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]<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}}CBM105.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
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== Ligand specificities ==<br />
The first member of family CBM105 (SoCBM105) was identified in the [[PL29]] multidomain chondroitinase SoChABC29 from ''Segatella oris'' <cite>Liu2024</cite>. SoCBM105 bound specifically to chondroitin sulfates (CSs) including CS-A and CS-C, while it was incapable of binding to other glycosaminoglycans or polyuronic acid substrates <cite>Liu2024</cite>.<br />
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== Structural Features ==<br />
[[File:CBM105 Fig.1.png|thumb|350px|right|'''Figure 1. Domain analysis of SoChABC29, the parent enzyme of SoCBM105.''' The enzyme consists of a signal peptide (1-21 amino acids), a PL29 domain (66-380 amino acids) and a CBM105 domain (viz., SoCBM105; 555-785 amino acids).]]<br />
An AlphaFold2 <cite>Jumper2021</cite> model predicts that SoCBM105 has a β-sandwich fold (Fig.1).<br />
<br />
== Functionalities == <br />
SoCBM105 is at the C-terminus domain of a [[PL29]] enzyme SoChABC29 that displays chondroitin sulfate ABC activity, consistent with the SoCBM105 specificity <cite>Liu2024</cite>. Biochemical characterization of SoChABC29 and the CBM-truncated enzyme revealed that the SoCBM105 enhances the catalytic activity, thermostability, and disaccharide proportion in the final enzymatic products of SoChABC29 <cite>Liu2024</cite>.<br />
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== Family Firsts ==<br />
;First Identified: Binding to chondroitin sulfate in the CBM105 family was first characterized and identified for SoCBM105 from the ''S. oris'' [[PL29]] chondroitinase <cite>Liu2024</cite>.<br />
;First Structural Characterization: No experimentally determined three-dimensional structure has been solved in this CBM family.<br />
<br />
== References ==<br />
<biblio><br />
#Liu2024 pmid=38777025<br />
#Jumper2021 pmid=34265844<br />
</biblio><br />
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<!-- Do not delete this Category tag --><br />
[[Category:Carbohydrate Binding Module Families|CBM105]]<br />
<!-- ATTENTION: Make sure to replace "nnn" with a three digit family number, e.g. "032" or "105" etc., for proper sorting of the page by family number. --></div>Guanchen Liuhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_105&diff=18495Carbohydrate Binding Module Family 1052024-10-28T03:11:03Z<p>Guanchen Liu: </p>
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<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:Guanchen Liu|Guanchen Liu]]<br />
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]<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}}CBM105.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
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== Ligand specificities ==<br />
The first member of family CBM105 (SoCBM) was identified in the [[PL29]] multidomain chondroitinase ChABC29So from ''Segatella oris'' <cite>Liu2024</cite>. SoCBM bound specifically to chondroitin sulfates (CSs) including CS-A and CS-C, while incapable of binding to other glycosaminoglycanss or polyuronic acid substrates.<br />
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== Structural Features ==<br />
[[File:CBM105 Fig.1.png|thumb|350px|right|'''Figure 1. Domain analysis of ChABC29So, the parent enzyme of SoCBM.''' The enzyme consists of a signal peptide (1-21 amino acids), a PL29 domain (66-380 amino acids) and a CBM105 domain (viz., SoCBM; 555-785 amino acids).]]<br />
An AlphaFold2 model predicts that SoCBM has a β-sandwich fold (Fig.1).<br />
<br />
== Functionalities == <br />
SoCBM is the C-terminus domain of a [[PL29]] enzyme ChABC29So that displays chondroitin sulfate ABC activity, consistent with the SoCBM specificity. Biochemical characterization of ChABC29So and the CBM-truncated enzyme revealed that the SoCBM enhances the catalytic activity, thermostability, and disaccharide proportion in the final enzymatic products of ChABC29So.<br />
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== Family Firsts ==<br />
;First Identified<br />
:The chondroitin sulfate binding SoCBM from the ''S. oris'' [[PL29]] chondroitinase was the first member of the family to be identified and characterized<cite>Liu2024</cite>.<br />
;First Structural Characterization<br />
:No experimentally determined three-dimensional structure has been solved in this CBM family.<br />
<br />
== References ==<br />
<biblio><br />
#Liu2024 pmid=38777025<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Carbohydrate Binding Module Families|CBM105]]<br />
<!-- ATTENTION: Make sure to replace "nnn" with a three digit family number, e.g. "032" or "105" etc., for proper sorting of the page by family number. --></div>Guanchen Liuhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_105&diff=18494Carbohydrate Binding Module Family 1052024-10-28T03:09:44Z<p>Guanchen Liu: </p>
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<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:Guanchen Liu|Guanchen Liu]]<br />
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]<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}}CBM105.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
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== Ligand specificities ==<br />
The first member of family CBM105 (SoCBM) was identified in the [[PL29]] multidomain chondroitinase ChABC29So from ''Segatella oris'' <cite>Liu2024</cite>. SoCBM bound specifically to chondroitin sulfates (CSs) including CS-A and CS-C, while incapable of binding to other glycosaminoglycanss or polyuronic acid substrates.<br />
<br />
== Structural Features ==<br />
[[File:CBM105 Fig.1.png|thumb|350px|right|'''Figure 1. Domain analysis of ChABC29So, the parent enzyme of SoCBM.'''The enzyme consists of a signal peptide (1-21 amino acids), a PL29 domain (66-380 amino acids) and a CBM105 domain (viz., SoCBM; 555-785 amino acids).]]<br />
An AlphaFold2 model predicts that SoCBM has a β-sandwich fold (Fig.1).<br />
<br />
== Functionalities == <br />
SoCBM is the C-terminus domain of a [[PL29]] enzyme ChABC29So that displays chondroitin sulfate ABC activity, consistent with the SoCBM specificity. Biochemical characterization of ChABC29So and the CBM-truncated enzyme revealed that the SoCBM enhances the catalytic activity, thermostability, and disaccharide proportion in the final enzymatic products of ChABC29So.<br />
<br />
== Family Firsts ==<br />
;First Identified<br />
:The chondroitin sulfate binding SoCBM from the ''S. oris'' [[PL29]] chondroitinase was the first member of the family to be identified and characterized<cite>Liu2024</cite>.<br />
;First Structural Characterization<br />
:No experimentally determined three-dimensional structure has been solved in this CBM family.<br />
<br />
== References ==<br />
<biblio><br />
#Liu2024 pmid=38777025<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Carbohydrate Binding Module Families|CBM105]]<br />
<!-- ATTENTION: Make sure to replace "nnn" with a three digit family number, e.g. "032" or "105" etc., for proper sorting of the page by family number. --></div>Guanchen Liuhttps://www.cazypedia.org/index.php?title=File:CBM105_Fig.1.png&diff=18493File:CBM105 Fig.1.png2024-10-28T02:59:51Z<p>Guanchen Liu: </p>
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<div></div>Guanchen Liuhttps://www.cazypedia.org/index.php?title=User:Guanchen_Liu&diff=17679User:Guanchen Liu2024-01-05T03:19:28Z<p>Guanchen Liu: </p>
<hr />
<div>[[File:Photo.jpg|100px|right]]<br />
Guanchen Liu obtained her bachelor's and master's degrees at Kyoto Institute of Technology. She is currently a Ph.D. student at the College of Food Science and Engineering, Ocean University of China, under the instruction of Prof. [[User:Yaoguang Chang|Yaoguang Chang]]. Her research focuses on the gene-mining and characterization of functional domains of [[Carbohydrate-active enzymes|CAZymes]] and and [[carbohydrate-binding modules]] <cite>CAZypedia2018</cite>. She discovered and characterized the first member of [[GH174]] <cite>Liu2023a</cite> and [[CBM100]] <cite>Liu2023b</cite>.<br />
<br />
<br />
== References ==<br />
<biblio><br />
#CAZypedia2018 pmid=29040563<br />
#Liu2023a pmid=36746582<br />
#Liu2023b pmid=37951443<br />
</biblio><br />
<br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Liu,Guanchen]]</div>Guanchen Liuhttps://www.cazypedia.org/index.php?title=User:Guanchen_Liu&diff=17678User:Guanchen Liu2024-01-05T03:12:50Z<p>Guanchen Liu: </p>
<hr />
<div>[[File:Photo.jpg|100px|right]]<br />
Guanchen Liu obtained her bachelor's and master's degrees at Kyoto Institute of Technology. She is currently a Ph.D. student at the College of Food Science and Engineering, Ocean University of China, under the instruction of Prof. [[User:Yaoguang Chang|Yaoguang Chang]]. Her research focuses on the gene-mining and characterization of functional domains of [[Carbohydrate-active enzymes|CAZymes]] and and [[carbohydrate-binding modules]]<cite>CAZypedia2018</cite>. She discovered and characterized the first member of [[GH174]] <cite>Liu2023a</cite> and [[CBM100]]<cite>Liu2023b</cite>.<br />
<br />
<br />
== References ==<br />
<biblio><br />
#CAZypedia2018 pmid=29040563<br />
#Liu2023a pmid=36746582<br />
#Liu2023b pmid=37951443<br />
</biblio><br />
<br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Liu,Guanchen]]</div>Guanchen Liuhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_100&diff=17677Carbohydrate Binding Module Family 1002024-01-05T03:08:04Z<p>Guanchen Liu: </p>
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<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:Guanchen Liu|Guanchen Liu]]<br />
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]<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}}CBM100.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
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== Ligand specificities ==<br />
[[File:Fig.1 300.png|thumb|250px|right|'''Figure 1. Domain analysis of the parent enzyme of PhCBM100.'''The enzyme consists of a signal peptide (1-23 amino acids), a PL29 domain (68-399 amino acids), a CBM100 domain (viz., PhCBM100; 555-785 amino acids) and a C-terminal sorting domain (786-851 amino acids).]]<br />
The first characterized member of the CBM100 family, PhCBM100<cite>Liu2023</cite>, was found in a PL29 putative chondroitin lyase from ''Polaribacter haliotis''. PhCBM100 bound specifically to chondroitin sulfates (CSs) including CS-A, CS-C and fucosylated chondroitin sulfate from sea cucumber ''Apostichopus japonicus'', whereas incapable of binding to other glycosaminoglycans or polyuronic acids. By affinity electrophoresis assays, PhCBM100 displays high affinity for CS-A and CS-C with the ''K''<sub>a</sub> values of 2.1×10<sup>6</sup> M<sup>-1</sup> and 6.0×10<sup>6</sup> M<sup>-1</sup>, respectively.<br />
<br />
== Structural Features ==<br />
[[File:Fig.2 300.png|thumb|400px|right|'''Figure 2. Structure of PhCBM100.''' (A) Schematic representation of PhCBM100 showing helices in yellow and strands in cyan. (B) Detailed view of the putative PhCBM100 binding site. The surface is colored by electrostatic potential, from blue (positive charge) to red (negative charge).]]<br />
The 1.55 Å resolution X-ray crystal structure of PhCBM100 ([{{PDBlink}}8jiy PDB 8jiy]) exhibited a β-sandwich fold formed by two antiparallel comprised of 10 β-strands and 2 helices.<br />
A groove with both a distinct positive charge and a high degree of conserved residues is proposed as the binding site, enriched with hydrophilic amino acids. As the result of molecular docking, the basic amino acid residues (e.g., Lys-40, Arg-122 and Arg-201) of PhCBM100 may contribute to CS binding through the ionic contacts. <br />
<br />
== Functionalities == <br />
PhCBM100 is a component of a PL29 enzyme that displays chondroitin-sulfate ABC endolyase activity, consistent with the PhCBM100 specificity. The ''in situ'' visualization of chondroitin sulfate in animal tissues (e.g., chicken cartilage, bovine muscle, and porcine laryngeal cartilage) was realized by utilizing a fluorescent probe constructed by fusing PhCBM100 with a green fluorescent protein.<br />
<br />
== Family Firsts ==<br />
;First Identified:The chondroitin sulfate binding PhCBM100 from the ''P. haliotis'' PL29 putative chondroitin lyase was the first member of the family to be identified and characterized.<br />
;First Structural Characterization:PhCBM100 was also the first structurally characterized CBM100.<br />
<br />
== References ==<br />
<biblio><br />
#Liu2023 pmid=37951443<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Carbohydrate Binding Module Families|CBM100]]</div>Guanchen Liuhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_100&diff=17676Carbohydrate Binding Module Family 1002024-01-05T03:01:47Z<p>Guanchen Liu: </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:Guanchen Liu|Guanchen Liu]]<br />
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]<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}}CBM100.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
[[File:Fig.1 300.png|thumb|250px|right|'''Figure 1. Domain analysis of the parent enzyme of PhCBM100.'''The enzyme consists of a signal peptide (1-23 amino acids), a PL29 domain (68-399 amino acids), a CBM100 domain (viz., PhCBM100; 555-785 amino acids) and a C-terminal sorting domain (786-851 amino acids).]]<br />
The first characterized member of the CBM100 family, PhCBM100<cite>Liu2024</cite>, was found in a PL29 putative chondroitin lyase from ''Polaribacter haliotis''. PhCBM100 bound specifically to chondroitin sulfates (CSs) including CS-A, CS-C and fucosylated chondroitin sulfate from sea cucumber ''Apostichopus japonicus'', whereas incapable of binding to other glycosaminoglycans or polyuronic acids. By affinity electrophoresis assays, PhCBM100 displays high affinity for CS-A and CS-C with the ''K''<sub>a</sub> values of 2.1×10<sup>6</sup> M<sup>-1</sup> and 6.0×10<sup>6</sup> M<sup>-1</sup>, respectively.<br />
<br />
== Structural Features ==<br />
[[File:Fig.2 300.png|thumb|400px|right|'''Figure 2. Structure of PhCBM100.''' (A) Schematic representation of PhCBM100 showing helices in yellow and strands in cyan. (B) Detailed view of the putative PhCBM100 binding site. The surface is colored by electrostatic potential, from blue (positive charge) to red (negative charge).]]<br />
The 1.55 Å resolution X-ray crystal structure of PhCBM100 ([{{PDBlink}}8jiy PDB 8jiy]) exhibited a β-sandwich fold formed by two antiparallel comprised of 10 β-strands and 2 helices.<br />
A groove with both a distinct positive charge and a high degree of conserved residues is proposed as the binding site, enriched with hydrophilic amino acids. As the result of molecular docking, the basic amino acid residues (e.g., Lys-40, Arg-122 and Arg-201) of PhCBM100 may contribute to CS binding through the ionic contacts. <br />
<br />
== Functionalities == <br />
PhCBM100 is a component of a PL29 enzyme that displays chondroitin-sulfate ABC endolyase activity, consistent with the PhCBM100 specificity. The ''in situ'' visualization of chondroitin sulfate in animal tissues (e.g., chicken cartilage, bovine muscle, and porcine laryngeal cartilage) was realized by utilizing a fluorescent probe constructed by fusing PhCBM100 with a green fluorescent protein.<br />
<br />
== Family Firsts ==<br />
;First Identified:The chondroitin sulfate binding PhCBM100 from the ''P. haliotis'' PL29 putative chondroitin lyase was the first member of the family to be identified and characterized.<br />
;First Structural Characterization:PhCBM100 was also the first structurally characterized CBM100.<br />
<br />
== References ==<br />
<biblio><br />
#Liu2024 pmid=37951443<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Carbohydrate Binding Module Families|CBM100]]</div>Guanchen Liuhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_100&diff=17675Carbohydrate Binding Module Family 1002024-01-05T03:00:48Z<p>Guanchen Liu: </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:Guanchen Liu|Guanchen Liu]]<br />
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]<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}}CBM100.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
[[File:Fig.1 300.png|thumb|250px|right|'''Figure 1. Domain analysis of the parent enzyme of PhCBM100.'''The enzyme consists of a signal peptide (1-23 amino acids), a PL29 domain (68-399 amino acids), a CBM100 domain (viz., PhCBM100; 555-785 amino acids) and a C-terminal sorting domain (786-851 amino acids).]]<br />
The first characterized member of the CBM100 family, PhCBM100<cite>Liu2024</cite>, was found in a PL29 putative chondroitin lyase from ''Polaribacter haliotis''. PhCBM100 bound specifically to chondroitin sulfates (CSs) including CS-A, CS-C and fucosylated chondroitin sulfate from sea cucumber ''Apostichopus japonicus'', whereas incapable of binding to other glycosaminoglycans or polyuronic acids. By affinity electrophoresis assays, PhCBM100 displays high affinity for CS-A and CS-C with the Ka values of 2.1×10<sup>6</sup> M<sup>-1</sup> and 6.0×10<sup>6</sup> M<sup>-1</sup>, respectively.<br />
<br />
== Structural Features ==<br />
[[File:Fig.2 300.png|thumb|400px|right|'''Figure 2. Structure of PhCBM100.''' (A) Schematic representation of PhCBM100 showing helices in yellow and strands in cyan. (B) Detailed view of the putative PhCBM100 binding site. The surface is colored by electrostatic potential, from blue (positive charge) to red (negative charge).]]<br />
The 1.55 Å resolution X-ray crystal structure of PhCBM100 ([{{PDBlink}}8jiy PDB 8jiy]) exhibited a β-sandwich fold formed by two antiparallel comprised of 10 β-strands and 2 helices.<br />
A groove with both a distinct positive charge and a high degree of conserved residues is proposed as the binding site, enriched with hydrophilic amino acids. As the result of molecular docking, the basic amino acid residues (e.g., Lys-40, Arg-122 and Arg-201) of PhCBM100 may contribute to CS binding through the ionic contacts. <br />
<br />
== Functionalities == <br />
PhCBM100 is a component of a PL29 enzyme that displays chondroitin-sulfate ABC endolyase activity, consistent with the PhCBM100 specificity. The ''in situ'' visualization of chondroitin sulfate in animal tissues (e.g., chicken cartilage, bovine muscle, and porcine laryngeal cartilage) was realized by utilizing a fluorescent probe constructed by fusing PhCBM100 with a green fluorescent protein.<br />
<br />
== Family Firsts ==<br />
;First Identified:The chondroitin sulfate binding PhCBM100 from the ''P. haliotis'' PL29 putative chondroitin lyase was the first member of the family to be identified and characterized.<br />
;First Structural Characterization:PhCBM100 was also the first structurally characterized CBM100.<br />
<br />
== References ==<br />
<biblio><br />
#Liu2024 pmid=37951443<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Carbohydrate Binding Module Families|CBM100]]</div>Guanchen Liuhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_100&diff=17674Carbohydrate Binding Module Family 1002024-01-05T02:59:41Z<p>Guanchen Liu: </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:Guanchen Liu|Guanchen Liu]]<br />
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]<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}}CBM100.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
[[File:Fig.1 300.png|thumb|300px|right|'''Figure 1. Domain analysis of the parent enzyme of PhCBM100.'''The enzyme consists of a signal peptide (1-23 amino acids), a PL29 domain (68-399 amino acids), a CBM100 domain (viz., PhCBM100; 555-785 amino acids) and a C-terminal sorting domain (786-851 amino acids).]]<br />
The first characterized member of the CBM100 family, PhCBM100<cite>Liu2024</cite>, was found in a PL29 putative chondroitin lyase from ''Polaribacter haliotis''. PhCBM100 bound specifically to chondroitin sulfates (CSs) including CS-A, CS-C and fucosylated chondroitin sulfate from sea cucumber ''Apostichopus japonicus'', whereas incapable of binding to other glycosaminoglycans or polyuronic acids. By affinity electrophoresis assays, PhCBM100 displays high affinity for CS-A and CS-C with the Ka values of 2.1×10<sup>6</sup> M<sup>-1</sup> and 6.0×10<sup>6</sup> M<sup>-1</sup>, respectively.<br />
<br />
== Structural Features ==<br />
[[File:Fig.2 300.png|thumb|400px|right|'''Figure 2. Structure of PhCBM100.''' (A) Schematic representation of PhCBM100 showing helices in yellow and strands in cyan. (B) Detailed view of the putative PhCBM100 binding site. The surface is colored by electrostatic potential, from blue (positive charge) to red (negative charge).]]<br />
The 1.55 Å resolution X-ray crystal structure of PhCBM100 ([{{PDBlink}}8jiy PDB 8jiy]) exhibited a β-sandwich fold formed by two antiparallel comprised of 10 β-strands and 2 helices.<br />
A groove with both a distinct positive charge and a high degree of conserved residues is proposed as the binding site, enriched with hydrophilic amino acids. As the result of molecular docking, the basic amino acid residues (e.g., Lys-40, Arg-122 and Arg-201) of PhCBM100 may contribute to CS binding through the ionic contacts. <br />
<br />
== Functionalities == <br />
PhCBM100 is a component of a PL29 enzyme that displays chondroitin-sulfate ABC endolyase activity, consistent with the PhCBM100 specificity. The ''in situ'' visualization of chondroitin sulfate in animal tissues (e.g., chicken cartilage, bovine muscle, and porcine laryngeal cartilage) was realized by utilizing a fluorescent probe constructed by fusing PhCBM100 with a green fluorescent protein.<br />
<br />
== Family Firsts ==<br />
;First Identified:The chondroitin sulfate binding PhCBM100 from the ''P. haliotis'' PL29 putative chondroitin lyase was the first member of the family to be identified and characterized.<br />
;First Structural Characterization:PhCBM100 was also the first structurally characterized CBM100.<br />
<br />
== References ==<br />
<biblio><br />
#Liu2024 pmid=37951443<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Carbohydrate Binding Module Families|CBM100]]</div>Guanchen Liuhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_100&diff=17673Carbohydrate Binding Module Family 1002024-01-05T02:59:09Z<p>Guanchen Liu: </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:Guanchen Liu|Guanchen Liu]]<br />
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]<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}}CBM100.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
[[File:Fig.1 300.png|thumb|300px|right|'''Figure 1. Domain analysis of the parent enzyme of PhCBM100.'''The enzyme consists of a signal peptide (1-23 amino acids), a PL29 domain (68-399 amino acids), a CBM100 domain (viz., PhCBM100; 555-785 amino acids) and a C-terminal sorting domain (786-851 amino acids).]]<br />
The first characterized member of the CBM100 family, PhCBM100<cite>Liu2024</cite>, was found in a PL29 putative chondroitin lyase from ''Polaribacter haliotis''. PhCBM100 bound specifically to chondroitin sulfates (CSs) including CS-A, CS-C and fucosylated chondroitin sulfate from sea cucumber ''Apostichopus japonicus'', whereas incapable of binding to other glycosaminoglycans or polyuronic acids. By affinity electrophoresis assays, PhCBM100 displays high affinity for CS-A and CS-C with the Ka values of 2.1×10<sup>6</sup> M<sup>-1</sup> and 6.0×10<sup>6</sup> M<sup>-1</sup>, respectively.<br />
<br />
== Structural Features ==<br />
[[File:Fig.2 300.png|thumb|600px|right|'''Figure 2. Structure of PhCBM100.''' (A) Schematic representation of PhCBM100 showing helices in yellow and strands in cyan. (B) Detailed view of the putative PhCBM100 binding site. The surface is colored by electrostatic potential, from blue (positive charge) to red (negative charge).]]<br />
The 1.55 Å resolution X-ray crystal structure of PhCBM100 ([{{PDBlink}}8jiy PDB 8jiy]) exhibited a β-sandwich fold formed by two antiparallel comprised of 10 β-strands and 2 helices.<br />
A groove with both a distinct positive charge and a high degree of conserved residues is proposed as the binding site, enriched with hydrophilic amino acids. As the result of molecular docking, the basic amino acid residues (e.g., Lys-40, Arg-122 and Arg-201) of PhCBM100 may contribute to CS binding through the ionic contacts. <br />
<br />
== Functionalities == <br />
PhCBM100 is a component of a PL29 enzyme that displays chondroitin-sulfate ABC endolyase activity, consistent with the PhCBM100 specificity. The ''in situ'' visualization of chondroitin sulfate in animal tissues (e.g., chicken cartilage, bovine muscle, and porcine laryngeal cartilage) was realized by utilizing a fluorescent probe constructed by fusing PhCBM100 with a green fluorescent protein.<br />
<br />
== Family Firsts ==<br />
;First Identified:The chondroitin sulfate binding PhCBM100 from the ''P. haliotis'' PL29 putative chondroitin lyase was the first member of the family to be identified and characterized.<br />
;First Structural Characterization:PhCBM100 was also the first structurally characterized CBM100.<br />
<br />
== References ==<br />
<biblio><br />
#Liu2024 pmid=37951443<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Carbohydrate Binding Module Families|CBM100]]</div>Guanchen Liuhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_100&diff=17672Carbohydrate Binding Module Family 1002024-01-05T02:55:48Z<p>Guanchen Liu: </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:Guanchen Liu|Guanchen Liu]]<br />
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]<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}}CBM100.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
[[File:Fig.1 300.png|thumb|300px|right|'''Figure 1. Domain analysis of the parent enzyme of PhCBM100.'''The enzyme consists of a signal peptide (1-23 amino acids), a PL29 domain (68-399 amino acids), a CBM100 domain (viz., PhCBM100; 555-785 amino acids) and a C-terminal sorting domain (786-851 amino acids).]]<br />
The first characterized member of the CBM100 family, PhCBM100<cite>Liu2024</cite>, was found in a PL29 putative chondroitin lyase from ''Polaribacter haliotis''. PhCBM100 bound specifically to chondroitin sulfates (CSs) including CS-A, CS-C and fucosylated chondroitin sulfate from sea cucumber ''Apostichopus japonicus'', whereas incapable of binding to other glycosaminoglycans or polyuronic acids. By affinity electrophoresis assays, PhCBM100 displays high affinity for CS-A and CS-C with the Ka values of 2.1×10<sup>6</sup> M<sup>-1</sup> and 6.0×10<sup>6</sup> M<sup>-1</sup>, respectively.<br />
<br />
== Structural Features ==<br />
[[File:Fig.2 300.png|thumb|300px|right|'''Figure 2. Structure of PhCBM100.''' (A) Schematic representation of PhCBM100 showing helices in yellow and strands in cyan. (B) Detailed view of the putative PhCBM100 binding site. The surface is colored by electrostatic potential, from blue (positive charge) to red (negative charge).]]<br />
The 1.55 Å resolution X-ray crystal structure of PhCBM100 ([{{PDBlink}}8jiy PDB 8jiy]) exhibited a β-sandwich fold formed by two antiparallel comprised of 10 β-strands and 2 helices.<br />
A groove with both a distinct positive charge and a high degree of conserved residues is proposed as the binding site, enriched with hydrophilic amino acids. As the result of molecular docking, the basic amino acid residues (e.g., Lys-40, Arg-122 and Arg-201) of PhCBM100 may contribute to CS binding through the ionic contacts. <br />
<br />
== Functionalities == <br />
PhCBM100 is a component of a PL29 enzyme that displays chondroitin-sulfate ABC endolyase activity, consistent with the PhCBM100 specificity. The ''in situ'' visualization of chondroitin sulfate in animal tissues (e.g., chicken cartilage, bovine muscle, and porcine laryngeal cartilage) was realized by utilizing a fluorescent probe constructed by fusing PhCBM100 with a green fluorescent protein.<br />
<br />
== Family Firsts ==<br />
;First Identified:The chondroitin sulfate binding PhCBM100 from the ''P. haliotis'' PL29 putative chondroitin lyase was the first member of the family to be identified and characterized.<br />
;First Structural Characterization:PhCBM100 was also the first structurally characterized CBM100.<br />
<br />
== References ==<br />
<biblio><br />
#Liu2024 pmid=37951443<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Carbohydrate Binding Module Families|CBM100]]</div>Guanchen Liuhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_100&diff=17671Carbohydrate Binding Module Family 1002024-01-05T02:53:47Z<p>Guanchen Liu: </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:Guanchen Liu|Guanchen Liu]]<br />
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]<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}}CBM100.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
[[File:Fig.1 300.png|thumb|300px|right|'''Figure 1. Domain analysis of the parent enzyme of PhCBM100.'''The enzyme consists of a signal peptide (1-23 amino acids), a PL29 domain (68-399 amino acids), a CBM100 domain (viz., PhCBM100; 555-785 amino acids) and a C-terminal sorting domain (786-851 amino acids).]]<br />
The first characterized member of the CBM100 family, PhCBM100<cite>Liu2024</cite>, was found in a PL29 putative chondroitin lyase from ''Polaribacter haliotis''. PhCBM100 bound specifically to chondroitin sulfates (CSs) including CS-A, CS-C and fucosylated chondroitin sulfate from sea cucumber ''Apostichopus japonicus'', whereas incapable of binding to other glycosaminoglycans or polyuronic acids. By affinity electrophoresis assays, PhCBM100 displays high affinity for CS-A and CS-C with the Ka values of 2.1×10<sup>6</sup> M<sup>-1</sup> and 6.0×10<sup>6</sup> M<sup>-1</sup>, respectively.<br />
<br />
== Structural Features ==<br />
[[File:Fig.2 300.png|thumb|300px|right|'''Figure 2. Structure of PhCBM100.''' (A) Schematic representation of PhCBM100 showing helices in yellow and strands in cyan. (B) Detailed view of the putative PhCBM100 binding site. The surface is colored by electrostatic potential, from blue (positive charge) to red (negative charge).]]<br />
The 1.55 Å resolution X-ray crystal structure of PhCBM100 (PDB ID 8JIY) exhibited a β-sandwich fold formed by two antiparallel comprised of 10 β-strands and 2 helices.<br />
A groove with both a distinct positive charge and a high degree of conserved residues is proposed as the binding site, enriched with hydrophilic amino acids. As the result of molecular docking, the basic amino acid residues (e.g., Lys-40, Arg-122 and Arg-201) of PhCBM100 may contribute to CS binding through the ionic contacts. <br />
<br />
== Functionalities == <br />
PhCBM100 is a component of a PL29 enzyme that displays chondroitin-sulfate ABC endolyase activity, consistent with the PhCBM100 specificity. The ''in situ'' visualization of chondroitin sulfate in animal tissues (e.g., chicken cartilage, bovine muscle, and porcine laryngeal cartilage) was realized by utilizing a fluorescent probe constructed by fusing PhCBM100 with a green fluorescent protein.<br />
<br />
== Family Firsts ==<br />
;First Identified:The chondroitin sulfate binding PhCBM100 from the ''P. haliotis'' PL29 putative chondroitin lyase was the first member of the family to be identified and characterized.<br />
;First Structural Characterization:PhCBM100 was also the first structurally characterized CBM100.<br />
<br />
== References ==<br />
<biblio><br />
#Liu2024 pmid=37951443<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Carbohydrate Binding Module Families|CBM100]]</div>Guanchen Liuhttps://www.cazypedia.org/index.php?title=File:Fig.2_300.png&diff=17670File:Fig.2 300.png2024-01-05T02:52:12Z<p>Guanchen Liu: </p>
<hr />
<div>Structure of PhCBM100. (A) Schematic representation of PhCBM100 showing helices in yellow and strands in cyan. (B) Detailed view of the putative PhCBM100 binding site. The surface is colored by electrostatic potential, from blue (positive charge) to red (negative charge).</div>Guanchen Liuhttps://www.cazypedia.org/index.php?title=File:Fig.1_300.png&diff=17669File:Fig.1 300.png2024-01-05T02:34:02Z<p>Guanchen Liu: </p>
<hr />
<div>Domain analysis of the parent enzyme of PhCBM100. The enzyme consists of a signal peptide (1-23 amino acids), a PL29 domain (68-399 amino acids), a CBM100 domain (viz., PhCBM100; 555-785 amino acids) and a C-terminal sorting domain (786-851 amino acids).</div>Guanchen Liuhttps://www.cazypedia.org/index.php?title=User:Guanchen_Liu&diff=17288User:Guanchen Liu2023-06-16T02:24:39Z<p>Guanchen Liu: </p>
<hr />
<div>[[File:Photo.jpg|100px|right]]<br />
Guanchen Liu obtained her bachelor's and master's degrees at Kyoto Institute of Technology. She is currently a Ph.D. student at the College of Food Science and Engineering, Ocean University of China, under the instruction of Prof. [[User:Yaoguang Chang|Yaoguang Chang]]. Her research focuses on the gene-mining and characterization of functional domains of [[Carbohydrate-active enzymes|CAZymes]]<cite>CAZypedia2018</cite>. She discovered and characterized the first member of [[GH174]] <cite>Liu2023</cite><br />
<br />
<br />
== References ==<br />
<biblio><br />
#CAZypedia2018 pmid=29040563<br />
#Liu2023 pmid=36746582<br />
</biblio><br />
<br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Liu,Guanchen]]</div>Guanchen Liuhttps://www.cazypedia.org/index.php?title=User:Guanchen_Liu&diff=17287User:Guanchen Liu2023-06-16T02:23:32Z<p>Guanchen Liu: </p>
<hr />
<div>[[File:Photo.jpg|thumb]]<br />
Guanchen Liu obtained her bachelor's and master's degrees at Kyoto Institute of Technology. She is currently a Ph.D. student at the College of Food Science and Engineering, Ocean University of China, under the instruction of Prof. [[User:Yaoguang Chang|Yaoguang Chang]]. Her research focuses on the gene-mining and characterization of functional domains of [[Carbohydrate-active enzymes|CAZymes]]<cite>CAZypedia2018</cite>. She discovered and characterized the first member of [[GH174]] <cite>Liu2023</cite><br />
<br />
<br />
== References ==<br />
<biblio><br />
#CAZypedia2018 pmid=29040563<br />
#Liu2023 pmid=36746582<br />
<biblio><br />
<br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Liu,Guanchen]]</div>Guanchen Liuhttps://www.cazypedia.org/index.php?title=File:Photo.jpg&diff=17286File:Photo.jpg2023-06-16T01:44:50Z<p>Guanchen Liu: </p>
<hr />
<div>Guanchen Liu</div>Guanchen Liuhttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_174&diff=17266Glycoside Hydrolase Family 1742023-05-26T01:42:46Z<p>Guanchen Liu: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Guanchen Liu|Guanchen Liu]]<br />
<br />
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]<br />
<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" |'''Glycoside Hydrolase Family GH174'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|retaining/inverting<br />
|-<br />
|'''Active site residues'''<br />
|known/not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH174.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Members of [[GH174|glycoside hydrolase family 174]] have been shown to exhibit α-1,3-L-fucanase activity. The first member of this family, Fun174A from a marine bacterium ''Wenyingzhuangia aestuarii'' OF219, specifically hydrolyze the α-1,3- L-fucoside bonds between 2-O-sulfated and non-sulfated fucose residues in the sulfated fucan from sea cucumber ''Isostichopus badionotus'' in a processive endo-acting manner.<cite>Liu2023</cite> Meanwhile, three homologs of Fun174A from ''Rubritalea marina'', ''Spartobacteria bacterium'' and ''Wenyingzhuangia fucanilytica'', display activities toward sulfated fucan from ''Isostichopus badionotus''.<cite>Liu2023</cite> All 92 members (up to May,2023) of GH174 are bacterial enzymes.<br />
[[File:Tree.png|thumb|'''Figure 1. The phylogenetic tree of GH174 homologs.''' Sequences comfirmed to exhibit α-1,3-L-fucanase activity were in red.]]<br />
<br />
== Kinetics and Mechanism ==<br />
The catalytic mechanism of GH174 has not been identified. As mentioned in the report, Fun174A showed no transglycosylating activity in the tested acceptor substrates, such as glycerin, methanol, L-fucose, D-glucose, D-galactose, D-fructose, D-mannose, D-glucosamine and N-acetyl- D-glucosamine.<cite>Liu2023</cite><br />
<br />
== Catalytic Residues ==<br />
Multiple sequence alignments of GH174 homologs showed that D119, E120 and E218 in Fun174A were highly conserved in all sequences. Three single-site mutants D119E, E120A and E218Q were established, expressed and identified in the report. Mutant D119E, E120A and E218Q resulted in 100.0%, 85.7% and 88.3% loss of activity on sulfated fucan from ''Isostichopus badionotus'' respectively. It indicated that D119, E120 and E218 were critical for the functioning of Fun174A.<cite>Liu2023</cite><br />
[[File:Weblogo.jpg|thumb|'''Figure 2. Multiple sequence alignments of residues in GH174 homologs.''' The highly conserved acidic amino acids in all sequences were indicated with black triangles.]]<br />
== Three-dimensional structures ==<br />
No three-dimensional structure has been solved in this glycoside hydrolase family at present. <br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Not yet identified.<br />
;First catalytic nucleophile identification: Not yet identified.<br />
;First general acid/base residue identification: Not yet identified.<br />
;First 3-D structure: Not yet identified.<br />
<br />
== References ==<br />
<biblio><br />
#Liu2023 pmid=36746582<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Glycoside Hydrolase Families|GH174]]</div>Guanchen Liuhttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_174&diff=17265Glycoside Hydrolase Family 1742023-05-26T01:39:20Z<p>Guanchen Liu: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Guanchen Liu|Guanchen Liu]]<br />
<br />
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]<br />
<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" |'''Glycoside Hydrolase Family GH174'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|retaining/inverting<br />
|-<br />
|'''Active site residues'''<br />
|known/not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH174.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Members of [[GH174|glycoside hydrolase family 174]] have been shown to exhibit α-1,3-L-fucanase activity. The first member of this family, Fun174A from a marine bacterium ''Wenyingzhuangia aestuarii'' OF219, specifically hydrolyze the α-1,3- L-fucoside bonds between 2-O-sulfated and non-sulfated fucose residues in the sulfated fucan from sea cucumber ''Isostichopus badionotus'' in a processive endo-acting manner.<ref>Liu2023</ref> Meanwhile, three homologs of Fun174A from ''Rubritalea marina'', ''Spartobacteria bacterium'' and ''Wenyingzhuangia fucanilytica'', display activities toward sulfated fucan from ''Isostichopus badionotus''.<ref>Liu2023</ref> All 92 members (up to May,2023) of GH174 are bacterial enzymes.<br />
[[File:Tree.png|thumb]]<br />
<br />
== Kinetics and Mechanism ==<br />
The catalytic mechanism of GH174 has not been identified. As mentioned in the report, Fun174A showed no transglycosylating activity in the tested acceptor substrates, such as glycerin, methanol, L-fucose, D-glucose, D-galactose, D-fructose, D-mannose, D-glucosamine and N-acetyl- D-glucosamine.<ref>Liu2023</ref><br />
<br />
== Catalytic Residues ==<br />
Multiple sequence alignments of GH174 homologs showed that D119, E120 and E218 in Fun174A were highly conserved in all sequences. Three single-site mutants D119E, E120A and E218Q were established, expressed and identified in the report. Mutant D119E, E120A and E218Q resulted in 100.0%, 85.7% and 88.3% loss of activity on sulfated fucan from ''Isostichopus badionotus'' respectively. It indicated that D119, E120 and E218 were critical for the functioning of Fun174A.<ref>Liu2023</ref><br />
[[File:Weblogo.jpg|thumb]]<br />
== Three-dimensional structures ==<br />
No three-dimensional structure has been solved in this glycoside hydrolase family at present. <br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Not yet identified.<br />
;First catalytic nucleophile identification: Not yet identified.<br />
;First general acid/base residue identification: Not yet identified.<br />
;First 3-D structure: Not yet identified.<br />
<br />
== References ==<br />
<biblio><br />
#Liu2023 pmid=36746582<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Glycoside Hydrolase Families|GH174]]</div>Guanchen Liuhttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_174&diff=17264Glycoside Hydrolase Family 1742023-05-26T01:37:32Z<p>Guanchen Liu: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Guanchen Liu|Guanchen Liu]]<br />
<br />
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]<br />
<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" |'''Glycoside Hydrolase Family GH174'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|retaining/inverting<br />
|-<br />
|'''Active site residues'''<br />
|known/not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH174.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Members of [[GH174|glycoside hydrolase family 174]] have been shown to exhibit α-1,3-L-fucanase activity. The first member of this family, Fun174A from a marine bacterium ''Wenyingzhuangia aestuarii'' OF219, specifically hydrolyze the α-1,3- L-fucoside bonds between 2-O-sulfated and non-sulfated fucose residues in the sulfated fucan from sea cucumber ''Isostichopus badionotus'' in a processive endo-acting manner. Meanwhile, three homologs of Fun174A from ''Rubritalea marina'', ''Spartobacteria bacterium'' and ''Wenyingzhuangia fucanilytica'', display activities toward sulfated fucan from ''Isostichopus badionotus''. All 92 members (up to May,2023) of GH174 are bacterial enzymes.<br />
[[File:Tree.png|thumb]]<br />
<br />
== Kinetics and Mechanism ==<br />
The catalytic mechanism of GH174 has not been identified. As mentioned in the report, Fun174A showed no transglycosylating activity in the tested acceptor substrates, such as glycerin, methanol, L-fucose, D-glucose, D-galactose, D-fructose, D-mannose, D-glucosamine and N-acetyl- D-glucosamine.<br />
<br />
== Catalytic Residues ==<br />
Multiple sequence alignments of GH174 homologs showed that D119, E120 and E218 in Fun174A were highly conserved in all sequences. Three single-site mutants D119E, E120A and E218Q were established, expressed and identified in the report. Mutant D119E, E120A and E218Q resulted in 100.0%, 85.7% and 88.3% loss of activity on sulfated fucan from ''Isostichopus badionotus'' respectively. It indicated that D119, E120 and E218 were critical for the functioning of Fun174A.<br />
[[File:Weblogo.jpg|thumb]]<br />
== Three-dimensional structures ==<br />
No three-dimensional structure has been solved in this glycoside hydrolase family at present. <br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Not yet identified.<br />
;First catalytic nucleophile identification: Not yet identified.<br />
;First general acid/base residue identification: Not yet identified.<br />
;First 3-D structure: Not yet identified.<br />
<br />
== References ==<br />
<biblio><br />
#Liu2023 pmid=36746582<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Glycoside Hydrolase Families|GH174]]</div>Guanchen Liuhttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_174&diff=17263Glycoside Hydrolase Family 1742023-05-26T01:33:16Z<p>Guanchen Liu: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Guanchen Liu|Guanchen Liu]]<br />
<br />
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]<br />
<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" |'''Glycoside Hydrolase Family GH174'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|retaining/inverting<br />
|-<br />
|'''Active site residues'''<br />
|known/not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH174.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Members of glycoside hydrolase family 174 have been shown to exhibit α-1,3-L-fucanase activity. The first member of this family, Fun174A from a marine bacterium Wenyingzhuangia aestuarii OF219, specifically hydrolyze the α-1,3- L-fucoside bonds between 2-O-sulfated and non-sulfated fucose residues in the sulfated fucan from sea cucumber Isostichopus badionotus in a processive endo-acting manner. Meanwhile, three homologs of Fun174A from Rubritalea marina, Spartobacteria bacterium and Wenyingzhuangia fucanilytica, display activities toward sulfated fucan from Isostichopus badionotus. All 92 members (up to May,2023) of GH174 are bacterial enzymes.<br />
[[File:Tree.png|thumb]]<br />
<br />
== Kinetics and Mechanism ==<br />
The catalytic mechanism of GH174 has not been identified. As mentioned in the report, Fun174A showed no transglycosylating activity in the tested acceptor substrates, such as glycerin, methanol, L-fucose, D-glucose, D-galactose, D-fructose, D-mannose, D-glucosamine and N-acetyl- D-glucosamine.<br />
<br />
== Catalytic Residues ==<br />
Multiple sequence alignments of GH174 homologs showed that D119, E120 and E218 in Fun174A were highly conserved in all sequences. Three single-site mutants D119E, E120A and E218Q were established, expressed and identified in the report. Mutant D119E, E120A and E218Q resulted in 100.0%, 85.7% and 88.3% loss of activity on sulfated fucan from Isostichopus badionotus respectively. It indicated that D119, E120 and E218 were critical for the functioning of Fun174A.<br />
[[File:Weblogo.jpg|thumb]]<br />
== Three-dimensional structures ==<br />
No three-dimensional structure has been solved in this glycoside hydrolase family at present. <br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Not yet identified.<br />
;First catalytic nucleophile identification: Not yet identified.<br />
;First general acid/base residue identification: Not yet identified.<br />
;First 3-D structure: Not yet identified.<br />
<br />
== References ==<br />
<biblio><br />
#Liu2023 pmid=36746582<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Glycoside Hydrolase Families|GH174]]</div>Guanchen Liuhttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_174&diff=17262Glycoside Hydrolase Family 1742023-05-26T01:32:28Z<p>Guanchen Liu: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Guanchen Liu|Guanchen Liu]]<br />
<br />
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]<br />
<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" |'''Glycoside Hydrolase Family GH174'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|retaining/inverting<br />
|-<br />
|'''Active site residues'''<br />
|known/not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH174.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Members of glycoside hydrolase family 174 have been shown to exhibit α-1,3-L-fucanase activity. The first member of this family, Fun174A from a marine bacterium Wenyingzhuangia aestuarii OF219, specifically hydrolyze the α-1,3- L-fucoside bonds between 2-O-sulfated and non-sulfated fucose residues in the sulfated fucan from sea cucumber Isostichopus badionotus in a processive endo-acting manner. Meanwhile, three homologs of Fun174A from Rubritalea marina, Spartobacteria bacterium and Wenyingzhuangia fucanilytica, display activities toward sulfated fucan from Isostichopus badionotus. All 92 members (up to May,2023) of GH174 are bacterial enzymes.<br />
[[File:Tree.png|thumb]]<br />
Authors may get an idea of what to put in each field from ''Curator Approved'' [[Glycoside Hydrolase Families]]. ''(TIP: Right click with your mouse and open this link in a new browser window...)''<br />
<br />
In the meantime, please see these references for an essential introduction to the CAZy classification system: <cite>DaviesSinnott2008 Cantarel2009</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
The catalytic mechanism of GH174 has not been identified. As mentioned in the report, Fun174A showed no transglycosylating activity in the tested acceptor substrates, such as glycerin, methanol, L-fucose, D-glucose, D-galactose, D-fructose, D-mannose, D-glucosamine and N-acetyl- D-glucosamine.<br />
<br />
== Catalytic Residues ==<br />
Multiple sequence alignments of GH174 homologs showed that D119, E120 and E218 in Fun174A were highly conserved in all sequences. Three single-site mutants D119E, E120A and E218Q were established, expressed and identified in the report. Mutant D119E, E120A and E218Q resulted in 100.0%, 85.7% and 88.3% loss of activity on sulfated fucan from Isostichopus badionotus respectively. It indicated that D119, E120 and E218 were critical for the functioning of Fun174A.<br />
[[File:Weblogo.jpg|thumb]]<br />
== Three-dimensional structures ==<br />
No three-dimensional structure has been solved in this glycoside hydrolase family at present. <br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Not yet identified.<br />
;First catalytic nucleophile identification: Not yet identified.<br />
;First general acid/base residue identification: Not yet identified.<br />
;First 3-D structure: Not yet identified.<br />
<br />
== References ==<br />
<biblio><br />
#Liu2023 pmid=36746582<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Glycoside Hydrolase Families|GH174]]</div>Guanchen Liuhttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_174&diff=17261Glycoside Hydrolase Family 1742023-05-26T01:31:35Z<p>Guanchen Liu: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Guanchen Liu|Guanchen Liu]]<br />
<br />
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]<br />
<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" |'''Glycoside Hydrolase Family GH174'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|retaining/inverting<br />
|-<br />
|'''Active site residues'''<br />
|known/not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH174.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Members of glycoside hydrolase family 174 have been shown to exhibit α-1,3-L-fucanase activity. The first member of this family, Fun174A from a marine bacterium Wenyingzhuangia aestuarii OF219, specifically hydrolyze the α-1,3- L-fucoside bonds between 2-O-sulfated and non-sulfated fucose residues in the sulfated fucan from sea cucumber Isostichopus badionotus in a processive endo-acting manner. Meanwhile, three homologs of Fun174A from Rubritalea marina, Spartobacteria bacterium and Wenyingzhuangia fucanilytica, display activities toward sulfated fucan from Isostichopus badionotus. All 92 members (up to May,2023) of GH174 are bacterial enzymes.<br />
[[File:Tree.png|'''Figure 1. The phylogenetic tree of GH174 homologs.''' Sequences comfirmed to exhibit α-1,3-L-fucanase activity were in red.]]<br />
Authors may get an idea of what to put in each field from ''Curator Approved'' [[Glycoside Hydrolase Families]]. ''(TIP: Right click with your mouse and open this link in a new browser window...)''<br />
<br />
In the meantime, please see these references for an essential introduction to the CAZy classification system: <cite>DaviesSinnott2008 Cantarel2009</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
The catalytic mechanism of GH174 has not been identified. As mentioned in the report, Fun174A showed no transglycosylating activity in the tested acceptor substrates, such as glycerin, methanol, L-fucose, D-glucose, D-galactose, D-fructose, D-mannose, D-glucosamine and N-acetyl- D-glucosamine.<br />
<br />
== Catalytic Residues ==<br />
Multiple sequence alignments of GH174 homologs showed that D119, E120 and E218 in Fun174A were highly conserved in all sequences. Three single-site mutants D119E, E120A and E218Q were established, expressed and identified in the report. Mutant D119E, E120A and E218Q resulted in 100.0%, 85.7% and 88.3% loss of activity on sulfated fucan from Isostichopus badionotus respectively. It indicated that D119, E120 and E218 were critical for the functioning of Fun174A.<br />
[[File:Weblogo.jpg|'''Figure 2. Multiple sequence alignments of residues in GH174 homologs.''' The highly conserved acidic amino acids in all sequences were indicated with black triangles.]]<br />
== Three-dimensional structures ==<br />
No three-dimensional structure has been solved in this glycoside hydrolase family at present. <br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Not yet identified.<br />
;First catalytic nucleophile identification: Not yet identified.<br />
;First general acid/base residue identification: Not yet identified.<br />
;First 3-D structure: Not yet identified.<br />
<br />
== References ==<br />
<biblio><br />
#Liu2023 pmid=36746582<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Glycoside Hydrolase Families|GH174]]</div>Guanchen Liuhttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_174&diff=17260Glycoside Hydrolase Family 1742023-05-26T01:21:04Z<p>Guanchen Liu: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Guanchen Liu|Guanchen Liu]]<br />
<br />
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]<br />
<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" |'''Glycoside Hydrolase Family GH174'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|retaining/inverting<br />
|-<br />
|'''Active site residues'''<br />
|known/not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH174.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Members of glycoside hydrolase family 174 have been shown to exhibit α-1,3-L-fucanase activity. The first member of this family, Fun174A from a marine bacterium Wenyingzhuangia aestuarii OF219, specifically hydrolyze the α-1,3- L-fucoside bonds between 2-O-sulfated and non-sulfated fucose residues in the sulfated fucan from sea cucumber Isostichopus badionotus in a processive endo-acting manner. Meanwhile, three homologs of Fun174A from Rubritalea marina, Spartobacteria bacterium and Wenyingzhuangia fucanilytica, display activities toward sulfated fucan from Isostichopus badionotus. All 92 members (up to May,2023) of GH174 are bacterial enzymes.<br />
[[File:Tree.png|thumb]]<br />
Authors may get an idea of what to put in each field from ''Curator Approved'' [[Glycoside Hydrolase Families]]. ''(TIP: Right click with your mouse and open this link in a new browser window...)''<br />
<br />
In the meantime, please see these references for an essential introduction to the CAZy classification system: <cite>DaviesSinnott2008 Cantarel2009</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
The catalytic mechanism of GH174 has not been identified. As mentioned in the report, Fun174A showed no transglycosylating activity in the tested acceptor substrates, such as glycerin, methanol, L-fucose, D-glucose, D-galactose, D-fructose, D-mannose, D-glucosamine and N-acetyl- D-glucosamine.<br />
<br />
== Catalytic Residues ==<br />
Multiple sequence alignments of GH174 homologs showed that D119, E120 and E218 in Fun174A were highly conserved in all sequences. Three single-site mutants D119E, E120A and E218Q were established, expressed and identified in the report. Mutant D119E, E120A and E218Q resulted in 100.0%, 85.7% and 88.3% loss of activity on sulfated fucan from Isostichopus badionotus respectively. It indicated that D119, E120 and E218 were critical for the functioning of Fun174A.<br />
[[File:Weblogo.jpg|thumb]]<br />
== Three-dimensional structures ==<br />
No three-dimensional structure has been solved in this glycoside hydrolase family at present. <br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Not yet identified.<br />
;First catalytic nucleophile identification: Not yet identified.<br />
;First general acid/base residue identification: Not yet identified.<br />
;First 3-D structure: Not yet identified.<br />
<br />
== References ==<br />
<biblio><br />
#Liu2023 pmid=36746582<br />
<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Glycoside Hydrolase Families|GH174]]</div>Guanchen Liuhttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_174&diff=17259Glycoside Hydrolase Family 1742023-05-26T00:59:32Z<p>Guanchen Liu: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Guanchen Liu|Guanchen Liu]]<br />
<br />
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]<br />
<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" |'''Glycoside Hydrolase Family GH174'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|retaining/inverting<br />
|-<br />
|'''Active site residues'''<br />
|known/not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH174.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Members of glycoside hydrolase family 174 have been shown to exhibit α-1,3-L-fucanase activity. The first member of this family, Fun174A from a marine bacterium Wenyingzhuangia aestuarii OF219, specifically hydrolyze the α-1,3- L-fucoside bonds between 2-O-sulfated and non-sulfated fucose residues in the sulfated fucan from sea cucumber Isostichopus badionotus in a processive endo-acting manner. Meanwhile, three homologs of Fun174A from Rubritalea marina, Spartobacteria bacterium and Wenyingzhuangia fucanilytica, display activities toward sulfated fucan from Isostichopus badionotus. All 92 members (up to May,2023) of GH174 are bacterial enzymes.<br />
[[File:Tree|thumb]]<br />
Authors may get an idea of what to put in each field from ''Curator Approved'' [[Glycoside Hydrolase Families]]. ''(TIP: Right click with your mouse and open this link in a new browser window...)''<br />
<br />
In the meantime, please see these references for an essential introduction to the CAZy classification system: <cite>DaviesSinnott2008 Cantarel2009</cite>.<br />
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== Kinetics and Mechanism ==<br />
The catalytic mechanism of GH174 has not been identified. As mentioned in the report, Fun174A showed no transglycosylating activity in the tested acceptor substrates, such as glycerin, methanol, L-fucose, D-glucose, D-galactose, D-fructose, D-mannose, D-glucosamine and N-acetyl- D-glucosamine.<br />
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== Catalytic Residues ==<br />
Multiple sequence alignments of GH174 homologs showed that D119, E120 and E218 in Fun174A were highly conserved in all sequences. Three single-site mutants D119E, E120A and E218Q were established, expressed and identified in the report. Mutant D119E, E120A and E218Q resulted in 100.0%, 85.7% and 88.3% loss of activity on sulfated fucan from Isostichopus badionotus respectively. It indicated that D119, E120 and E218 were critical for the functioning of Fun174A.<br />
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== Three-dimensional structures ==<br />
No three-dimensional structure has been solved in this glycoside hydrolase family at present. <br />
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== Family Firsts ==<br />
;First stereochemistry determination: Not yet identified.<br />
;First catalytic nucleophile identification: Not yet identified.<br />
;First general acid/base residue identification: Not yet identified.<br />
;First 3-D structure: Not yet identified.<br />
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== References ==<br />
<biblio><br />
#Liu2023 pmid=36746582<br />
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</biblio><br />
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[[Category:Glycoside Hydrolase Families|GH174]]</div>Guanchen Liuhttps://www.cazypedia.org/index.php?title=File:Weblogo.jpg&diff=17258File:Weblogo.jpg2023-05-26T00:57:55Z<p>Guanchen Liu: </p>
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<div>Figure 2. Multiple sequence alignments of residues in GH174 homologs. The highly conserved acidic amino acids in all sequences were indicated with black triangles.</div>Guanchen Liuhttps://www.cazypedia.org/index.php?title=File:Tree.png&diff=17257File:Tree.png2023-05-26T00:53:27Z<p>Guanchen Liu: </p>
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<div>Figure 1. The phylogenetic tree of GH174 homologs. Sequences comfirmed to exhibit α-1,3-L-fucanase activity were in red.</div>Guanchen Liu