https://www.cazypedia.org/api.php?action=feedcontributions&user=Chihaya+Yamada&feedformat=atomCAZypedia - User contributions [en-ca]2024-03-29T06:15:49ZUser contributionsMediaWiki 1.35.10https://www.cazypedia.org/index.php?title=User:Chihaya_Yamada&diff=17341User:Chihaya Yamada2023-06-20T02:43:38Z<p>Chihaya Yamada: </p>
<hr />
<div>[[Image:chihaya.JPG|200px|right]]<br />
<br />
Chihaya Yamada is a senior assistant professor at the Laboratory of Fermented Foods in the Department of Agricultural Chemistry, Meiji University located in Kanagawa Prefecture, Japan. I obtained Ph.D degree in Agriculture at The University of Tokyo in 2013. I contributed to structural analysis of lacto-''N''-biosidase (LnbX) from ''Bifidobacterium longum'' subsp. ''longum'' belonging to [[GH136]] with Prof. [[User:Shinya Fushinobu|Shinya Fushinobu]] and Prof. [[User:Takane Katayama|Takane Katayama]] <cite>chihaya2017</cite>. My reseach interests are new enzymes from human gut microbiota.<br />
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----<br />
<br />
<biblio><br />
#chihaya2017 pmid=28392148<br />
#Michael2020 pmid=32620774<br />
<br />
</biblio><br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Yamada,Chihaya]]</div>Chihaya Yamadahttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_136&diff=16195Glycoside Hydrolase Family 1362021-03-04T01:02:44Z<p>Chihaya Yamada: </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]]: ^^^Chihaya Yamada^^^<br />
* [[Responsible Curator]]: ^^^Shinya Fushinobu^^^<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 GH136'''<br />
|-<br />
|'''Clan''' <br />
|GH-N<br />
|-<br />
|'''Mechanism'''<br />
|retaining<br />
|-<br />
|'''Active site residues'''<br />
|Asp<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH136.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
This family of glycoside hydrolases contains lacto-''N''-biosidase, as demonstrated for LnbX from ''Bifidobacterium longum'' JCM 1217 <cite>Sakurama2013</cite>. LnbX liberates Galβ1-3GlcNAc(lacto-''N''-biose I, LNB) and lactose from lacto-''N''-tetraose, the main component of human milk oligosaccharides. It hydrolyzed the linkage GlcNAcβ1-3Gal in lacto-''N''-hexaose, lacto-''N''-fucopentaose I, and sialyllacto-''N''-tetraose a of human milk oligosaccharides as substrate of LnbX in the GH136. In addition, LnbX liberates Galβ1-3GalNAc (GNB) from the sugar chains of globo- and ganglio-series glycosphingolipids <cite>Gotoh2015</cite>.<br />
<br />
GH136 lacto-''N''-biosidase required neighboring chaperon gene for folding. Rarely, chaperone-like gene fused to lacto-''N''-biosidase gene in case of ErLnb136<sub>I</sub> and ErLnb136<sub>II</sub>from ''Eubacterium ramulus'' <cite>Michael2020</cite>.<br />
<br />
<br />
== Kinetics and Mechanism ==<br />
LnbX hydrolyzes the glycosidic linkage via a retaining mechanism involving a Grotthuss proton relay. <br />
<br />
== Catalytic Residues ==<br />
The nucleophile is Asp418. The catalytic acid/base is Asp411 via water molecule.<br />
<br />
== Three-dimensional structures ==<br />
[[file:LnbXc.png|thumb|300px|right|'''Figure 1: '''Overall structure of LnbXc with LNB (cyan) and two Ca2+ ions (orange).]]<br />
[[file:ErGH136.png|thumb|300px|right|'''Figure 2: '''Overall structure of ''Er''Lnb136 with LNB (yellow), consisting of an N-terminal domain designated as ''Er''Lnb136<sub>I</sub> (cyan-blue) and a C-terminal β-helix domain (green) -''Er''Lnb136<sub>II</sub>.]]<br />
<br />
The X-ray crystal structure of the catalytic domain, LnbXc(31-625) revealed a right-handed β helix fold that is usually shared by polysaccharide active enzymes. Three forms, ligand free at 2.36 Å resolution (PDB ID 5GQC), LNB complex at 1.82 Å (PDB ID 5GQF), and GNB complex at 2.70 Å (PDB ID 5GQG) were determined <cite>chihaya2017</cite>.<br />
The X-ray crystal structure of'' Er''GH136 in complex with LNB (PDB ID 6KQT) revealed the N-terminal domain (''Er''Lnb136I, from AA 7-224) consists of 8 α-helices (α1-α8) and Y145 of the α6-α7 loop positioned near the active site <cite>Michael2020</cite>.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Content is to be added here.<br />
;First catalytic nucleophile identification: Content is to be added here.<br />
;First general acid/base residue identification: Content is to be added here.<br />
;First 3-D structure: Content is to be added here.<br />
<br />
== References ==<br />
<biblio><br />
#Sakurama2013 pmid=23843461<br />
#Gotoh2015 pmid=25839135<br />
#chihaya2017 pmid=28392148<br />
#Michael2020 pmid=32620774<br />
</biblio><br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH136]]</div>Chihaya Yamadahttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_136&diff=16194Glycoside Hydrolase Family 1362021-03-03T08:26:34Z<p>Chihaya Yamada: </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]]: ^^^Chihaya Yamada^^^<br />
* [[Responsible Curator]]: ^^^Shinya Fushinobu^^^<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 GH136'''<br />
|-<br />
|'''Clan''' <br />
|GH-N<br />
|-<br />
|'''Mechanism'''<br />
|retaining<br />
|-<br />
|'''Active site residues'''<br />
|Asp<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH136.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
This family of glycoside hydrolases contains lacto-''N''-biosidase, as demonstrated for LnbX from ''Bifidobacterium longum'' JCM 1217 <cite>Sakurama2013</cite>. LnbX liberates Galβ1-3GlcNAc(lacto-''N''-biose I, LNB) and lactose from lacto-''N''-tetraose, the main component of human milk oligosaccharides. It hydrolyzed the linkage GlcNAcβ1-3Gal in lacto-''N''-hexaose, lacto-''N''-fucopentaose I, and sialyllacto-''N''-tetraose a of human milk oligosaccharides as substrate of LnbX in the GH136. In addition, LnbX liberates Galβ1-3GalNAc (GNB) from the sugar chains of globo- and ganglio-series glycosphingolipids <cite>Gotoh2015</cite>.<br />
<br />
GH136 lacto-''N''-biosidase required neighboring chaperon gene for folding. Rarely, chaperone-like gene fused to lacto-''N''-biosidase gene in case of ErGH136<sub>I</sub> and ErGH136<sub>II</sub>from ''Eubacterium ramulus'' <cite>Michael2020</cite>.<br />
<br />
<br />
== Kinetics and Mechanism ==<br />
LnbX hydrolyzes the glycosidic linkage via a retaining mechanism involving a Grotthuss proton relay. <br />
<br />
== Catalytic Residues ==<br />
The nucleophile is Asp418. The catalytic acid/base is Asp411 via water molecule.<br />
<br />
== Three-dimensional structures ==<br />
[[file:LnbXc.png|thumb|300px|right|'''Figure 1: '''Overall structure of LnbXc with LNB (cyan) and two Ca2+ ions (orange).]]<br />
[[file:ErGH136.png|thumb|300px|right|'''Figure 2: '''Overall structure of ErGH136 with LNB (yellow).]]<br />
<br />
The X-ray crystal structure of the catalytic domain, LnbXc(31-625) revealed a right-handed β helix fold that is usually shared by polysaccharide active enzymes. Three forms, ligand free at 2.36 Å resolution (PDB ID 5GQC), LNB complex at 1.82 Å (PDB ID 5GQF), and GNB complex at 2.70 Å (PDB ID 5GQG) were determined <cite>chihaya2017</cite>.<br />
The X-ray crystal structure of'' Er''GH136 in complex with LNB (PDB ID 6KQT) revealed the N-terminal domain (''Er''Lnb136I, from AA 7-224) consists of 8 α-helices (α1-α8) and Y145 of the α6-α7 loop positioned near the active site <cite>Michael2020</cite>.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Content is to be added here.<br />
;First catalytic nucleophile identification: Content is to be added here.<br />
;First general acid/base residue identification: Content is to be added here.<br />
;First 3-D structure: Content is to be added here.<br />
<br />
== References ==<br />
<biblio><br />
#Sakurama2013 pmid=23843461<br />
#Gotoh2015 pmid=25839135<br />
#chihaya2017 pmid=28392148<br />
#Michael2020 pmid=32620774<br />
</biblio><br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH136]]</div>Chihaya Yamadahttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_136&diff=16193Glycoside Hydrolase Family 1362021-03-03T08:24:46Z<p>Chihaya Yamada: </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]]: ^^^Chihaya Yamada^^^<br />
* [[Responsible Curator]]: ^^^Shinya Fushinobu^^^<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 GH136'''<br />
|-<br />
|'''Clan''' <br />
|GH-N<br />
|-<br />
|'''Mechanism'''<br />
|retaining<br />
|-<br />
|'''Active site residues'''<br />
|Asp<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH136.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
This family of glycoside hydrolases contains lacto-''N''-biosidase, as demonstrated for LnbX from ''Bifidobacterium longum'' JCM 1217 <cite>Sakurama2013</cite>. LnbX liberates Galβ1-3GlcNAc(lacto-''N''-biose I, LNB) and lactose from lacto-''N''-tetraose, the main component of human milk oligosaccharides. It hydrolyzed the linkage GlcNAcβ1-3Gal in lacto-''N''-hexaose, lacto-''N''-fucopentaose I, and sialyllacto-''N''-tetraose a of human milk oligosaccharides as substrate of LnbX in the GH136. In addition, LnbX liberates Galβ1-3GalNAc (GNB) from the sugar chains of globo- and ganglio-series glycosphingolipids <cite>Gotoh2015</cite>.<br />
<br />
GH136 lacto-''N''-biosidase required neighboring chaperon gene for folding. Rarely, chaperone-like gene fused to lacto-''N''-biosidase gene in case of ErGH136<sub>I</sub> and ErGH136<sub>II</sub>from ''Eubacterium ramulus'' <cite>Michael2020</cite>.<br />
<br />
<br />
== Kinetics and Mechanism ==<br />
LnbXc hydrolyzes the glycosidic linkage via a retaining mechanism involving a Grotthuss proton relay. <br />
<br />
== Catalytic Residues ==<br />
The nucleophile is Asp418. The catalytic acid/base is Asp411 via water molecule.<br />
<br />
== Three-dimensional structures ==<br />
[[file:LnbXc.png|thumb|300px|right|'''Figure 1: '''Overall structure of LnbXc with LNB (cyan) and two Ca2+ ions (orange).]]<br />
[[file:ErGH136.png|thumb|300px|right|'''Figure 2: '''Overall structure of ErGH136 with LNB (yellow).]]<br />
<br />
The X-ray crystal structure of the catalytic domain, LnbXc(31-625) revealed a right-handed β helix fold that is usually shared by polysaccharide active enzymes. Three forms, ligand free at 2.36 Å resolution (PDB ID 5GQC), LNB complex at 1.82 Å (PDB ID 5GQF), and GNB complex at 2.70 Å (PDB ID 5GQG) were determined <cite>chihaya2017</cite>.<br />
The X-ray crystal structure of'' Er''GH136 in complex with LNB (PDB ID 6KQT) revealed the N-terminal domain (''Er''Lnb136I, from AA 7-224) consists of 8 α-helices (α1-α8) and Y145 of the α6-α7 loop positioned near the active site <cite>Michael2020</cite>.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Content is to be added here.<br />
;First catalytic nucleophile identification: Content is to be added here.<br />
;First general acid/base residue identification: Content is to be added here.<br />
;First 3-D structure: Content is to be added here.<br />
<br />
== References ==<br />
<biblio><br />
#Sakurama2013 pmid=23843461<br />
#Gotoh2015 pmid=25839135<br />
#chihaya2017 pmid=28392148<br />
#Michael2020 pmid=32620774<br />
</biblio><br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH136]]</div>Chihaya Yamadahttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_136&diff=16192Glycoside Hydrolase Family 1362021-03-03T08:23:42Z<p>Chihaya Yamada: </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]]: ^^^Chihaya Yamada^^^<br />
* [[Responsible Curator]]: ^^^Shinya Fushinobu^^^<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 GH136'''<br />
|-<br />
|'''Clan''' <br />
|GH-N<br />
|-<br />
|'''Mechanism'''<br />
|retaining<br />
|-<br />
|'''Active site residues'''<br />
|known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH136.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
This family of glycoside hydrolases contains lacto-''N''-biosidase, as demonstrated for LnbX from ''Bifidobacterium longum'' JCM 1217 <cite>Sakurama2013</cite>. LnbX liberates Galβ1-3GlcNAc(lacto-''N''-biose I, LNB) and lactose from lacto-''N''-tetraose, the main component of human milk oligosaccharides. It hydrolyzed the linkage GlcNAcβ1-3Gal in lacto-''N''-hexaose, lacto-''N''-fucopentaose I, and sialyllacto-''N''-tetraose a of human milk oligosaccharides as substrate of LnbX in the GH136. In addition, LnbX liberates Galβ1-3GalNAc (GNB) from the sugar chains of globo- and ganglio-series glycosphingolipids <cite>Gotoh2015</cite>.<br />
<br />
GH136 lacto-''N''-biosidase required neighboring chaperon gene for folding. Rarely, chaperone-like gene fused to lacto-''N''-biosidase gene in case of ErGH136<sub>I</sub> and ErGH136<sub>II</sub>from ''Eubacterium ramulus'' <cite>Michael2020</cite>.<br />
<br />
<br />
== Kinetics and Mechanism ==<br />
LnbXc hydrolyzes the glycosidic linkage via a retaining mechanism involving a Grotthuss proton relay. <br />
<br />
== Catalytic Residues ==<br />
The nucleophile is Asp418. The catalytic acid/base is Asp411 via water molecule.<br />
<br />
== Three-dimensional structures ==<br />
[[file:LnbXc.png|thumb|300px|right|'''Figure 1: '''Overall structure of LnbXc with LNB (cyan) and two Ca2+ ions (orange).]]<br />
[[file:ErGH136.png|thumb|300px|right|'''Figure 1: '''Overall structure of ErGH136 with LNB (yellow).]]<br />
<br />
The X-ray crystal structure of the catalytic domain, LnbXc(31-625) revealed a right-handed β helix fold that is usually shared by polysaccharide active enzymes. Three forms, ligand free at 2.36 Å resolution (PDB ID 5GQC), LNB complex at 1.82 Å (PDB ID 5GQF), and GNB complex at 2.70 Å (PDB ID 5GQG) were determined <cite>chihaya2017</cite>.<br />
The X-ray crystal structure of'' Er''GH136 in complex with LNB (PDB ID 6KQT) revealed the N-terminal domain (''Er''Lnb136I, from AA 7-224) consists of 8 α-helices (α1-α8) and Y145 of the α6-α7 loop positioned near the active site <cite>Michael2020</cite>.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Content is to be added here.<br />
;First catalytic nucleophile identification: Content is to be added here.<br />
;First general acid/base residue identification: Content is to be added here.<br />
;First 3-D structure: Content is to be added here.<br />
<br />
== References ==<br />
<biblio><br />
#Sakurama2013 pmid=23843461<br />
#Gotoh2015 pmid=25839135<br />
#chihaya2017 pmid=28392148<br />
#Michael2020 pmid=32620774<br />
</biblio><br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH136]]</div>Chihaya Yamadahttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_136&diff=16191Glycoside Hydrolase Family 1362021-03-03T08:22:06Z<p>Chihaya Yamada: </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]]: ^^^Chihaya Yamada^^^<br />
* [[Responsible Curator]]: ^^^Shinya Fushinobu^^^<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 GH136'''<br />
|-<br />
|'''Clan''' <br />
|GH-N<br />
|-<br />
|'''Mechanism'''<br />
|retaining<br />
|-<br />
|'''Active site residues'''<br />
|known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH136.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
This family of glycoside hydrolases contains lacto-''N''-biosidase, as demonstrated for LnbX from ''Bifidobacterium longum'' JCM 1217 <cite>Sakurama2013</cite>. LnbX liberates Galβ1-3GlcNAc(lacto-''N''-biose I, LNB) and lactose from lacto-''N''-tetraose, the main component of human milk oligosaccharides. It hydrolyzed the linkage GlcNAcβ1-3Gal in lacto-''N''-hexaose, lacto-''N''-fucopentaose I, and sialyllacto-''N''-tetraose a of human milk oligosaccharides as substrate of LnbX in the GH136. In addition, LnbX liberates Galβ1-3GalNAc (GNB) from the sugar chains of globo- and ganglio-series glycosphingolipids <cite>Gotoh2015</cite>.<br />
<br />
GH136 lacto-''N''-biosidase required neighboring chaperon gene for folding. Rarely, chaperone-like gene fused to lacto-''N''-biosidase gene in case of ErGH136<sub>I</sub> and ErGH136<sub>II</sub>from ''Eubacterium ramulus'' <cite>Michael2020</cite>.<br />
<br />
<br />
== Kinetics and Mechanism ==<br />
LnbXc hydrolyzes the glycosidic linkage via a retaining mechanism involving a Grotthuss proton relay. <br />
<br />
== Catalytic Residues ==<br />
The nucleophile is Asp418. The catalytic acid/base is Asp411 via water molecule.<br />
<br />
== Three-dimensional structures ==<br />
[[file:LnbXc.png|thumb|300px|right|'''Figure 1: '''Overall structure of LnbXc with LNB (cyan) and two Ca2+ ions (orange).]]<br />
<br />
The X-ray crystal structure of the catalytic domain, LnbXc(31-625) revealed a right-handed β helix fold that is usually shared by polysaccharide active enzymes. Three forms, ligand free at 2.36 Å resolution (PDB ID 5GQC), LNB complex at 1.82 Å (PDB ID 5GQF), and GNB complex at 2.70 Å (PDB ID 5GQG) were determined <cite>chihaya2017</cite>.<br />
The X-ray crystal structure of'' Er''GH136 in complex with LNB (PDB ID 6KQT) revealed the N-terminal domain (''Er''Lnb136I, from AA 7-224) consists of 8 α-helices (α1-α8) and Y145 of the α6-α7 loop positioned near the active site <cite>Michael2020</cite>.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Content is to be added here.<br />
;First catalytic nucleophile identification: Content is to be added here.<br />
;First general acid/base residue identification: Content is to be added here.<br />
;First 3-D structure: Content is to be added here.<br />
<br />
== References ==<br />
<biblio><br />
#Sakurama2013 pmid=23843461<br />
#Gotoh2015 pmid=25839135<br />
#chihaya2017 pmid=28392148<br />
#Michael2020 pmid=32620774<br />
</biblio><br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH136]]</div>Chihaya Yamadahttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_136&diff=16190Glycoside Hydrolase Family 1362021-03-03T07:49:50Z<p>Chihaya Yamada: </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]]: ^^^Chihaya Yamada^^^<br />
* [[Responsible Curator]]: ^^^Shinya Fushinobu^^^<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 GH136'''<br />
|-<br />
|'''Clan''' <br />
|GH-N<br />
|-<br />
|'''Mechanism'''<br />
|retaining<br />
|-<br />
|'''Active site residues'''<br />
|known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH136.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
This family of glycoside hydrolases contains lacto-''N''-biosidase, as demonstrated for LnbX from ''Bifidobacterium longum'' JCM 1217 <cite>Sakurama2013</cite>. LnbX liberates Galβ1-3GlcNAc(lacto-''N''-biose I, LNB) and lactose from lacto-''N''-tetraose, the main component of human milk oligosaccharides. It hydrolyzed the linkage GlcNAcβ1-3Gal in lacto-''N''-hexaose, lacto-''N''-fucopentaose I, and sialyllacto-''N''-tetraose a of human milk oligosaccharides as substrate of LnbX in the GH136. In addition, LnbX liberates Galβ1-3GalNAc (GNB) from the sugar chains of globo- and ganglio-series glycosphingolipids <cite>Gotoh2015</cite>.<br />
<br />
GH136 lacto-''N''-biosidase required neighboring chaperon gene for folding. Rarely, chaperone-like gene fused to lacto-''N''-biosidase gene in case of ErGH136<sub>I</sub> and ErGH136<sub>II</sub>from ''Eubacterium ramulus'' <cite>Michael2020</cite>.<br />
<br />
<br />
== Kinetics and Mechanism ==<br />
LnbXc hydrolyzes the glycosidic linkage via a retaining mechanism involving a Grotthuss proton relay. <br />
<br />
== Catalytic Residues ==<br />
The nucleophile is Asp418. The catalytic acid/base is Asp411 via water molecule.<br />
<br />
== Three-dimensional structures ==<br />
[[file:LnbXc.png|thumb|300px|right|'''Figure 1: '''Overall structure of LnbXc with LNB (cyan) and two Ca2+ ions (orange).]]<br />
<br />
The X-ray crystal structure of the catalytic domain, LnbXc(31-625) revealed a right-handed β helix fold that is usually shared by polysaccharide active enzymes. Three forms, ligand free at 2.36 Å resolution (PDB ID 5GQC), LNB complex at 1.82 Å (PDB ID 5GQF), and GNB complex at 2.70 Å (PDB ID 5GQG) were determined <cite>chihaya2017</cite>..<br />
The X-ray crystal structure of ErGH136 revealed the N-terminal domain (ErLnb136I, from AA 7-224) consists of 8 α-helices (α1-α8).<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Content is to be added here.<br />
;First catalytic nucleophile identification: Content is to be added here.<br />
;First general acid/base residue identification: Content is to be added here.<br />
;First 3-D structure: Content is to be added here.<br />
<br />
== References ==<br />
<biblio><br />
#Sakurama2013 pmid=23843461<br />
#Gotoh2015 pmid=25839135<br />
#chihaya2017 pmid=28392148<br />
#Michael2020 pmid=32620774<br />
</biblio><br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH136]]</div>Chihaya Yamadahttps://www.cazypedia.org/index.php?title=File:ErGH136.png&diff=16189File:ErGH136.png2021-03-03T07:43:16Z<p>Chihaya Yamada: </p>
<hr />
<div></div>Chihaya Yamadahttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_136&diff=15801Glycoside Hydrolase Family 1362020-08-26T07:15:36Z<p>Chihaya Yamada: </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]]: ^^^Chihaya Yamada^^^<br />
* [[Responsible Curator]]: ^^^Shinya Fushinobu^^^<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 GH136'''<br />
|-<br />
|'''Clan''' <br />
|GH-N<br />
|-<br />
|'''Mechanism'''<br />
|retaining<br />
|-<br />
|'''Active site residues'''<br />
|known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH136.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
This family of glycoside hydrolases contains lacto-''N''-biosidase, as demonstrated for LnbX from ''Bifidobacterium longum'' JCM 1217 <cite>Sakurama2013</cite>. LnbX liberates Galβ1-3GlcNAc(lacto-''N''-biose I, LNB) and lactose from lacto-''N''-tetraose, the main component of human milk oligosaccharides. It hydrolyzed the linkage GlcNAcβ1-3Gal in lacto-''N''-hexaose, lacto-''N''-fucopentaose I, and sialyllacto-''N''-tetraose a of human milk oligosaccharides as substrate of LnbX in the GH136. In addition, LnbX liberates Galβ1-3GalNAc (GNB) from the sugar chains of globo- and ganglio-series glycosphingolipids <cite>Gotoh2015</cite>.<br />
<br />
GH136 lacto-''N''-biosidase required neighboring chaperon gene for folding. Rarely, chaperone-like gene fused to lacto-''N''-biosidase gene in case of ErGH136<sub>I</sub> and ErGH136<sub>II</sub>from ''Eubacterium ramulus'' <cite>Michael2020</cite>.<br />
<br />
<br />
== Kinetics and Mechanism ==<br />
LnbXc hydrolyzes the glycosidic linkage via a retaining mechanism involving a Grotthuss proton relay. <br />
<br />
== Catalytic Residues ==<br />
The nucleophile is Asp418. The catalytic acid/base is Asp411 via water molecule.<br />
<br />
== Three-dimensional structures ==<br />
[[file:LnbXc.png|thumb|300px|right|'''Figure 1: '''Overall structure of LnbXc with LNB (cyan) and two Ca2+ ions (orange).]]<br />
<br />
The X-ray crystal structure of the catalytic domain, LnbXc(31-625) revealed a right-handed β helix fold that is usually shared by polysaccharide active enzymes. Three forms, ligand free (2.36 Å resolution), LNB complex (1.82 Å), and GNB complex (2.70 Å) were determined.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Content is to be added here.<br />
;First catalytic nucleophile identification: Content is to be added here.<br />
;First general acid/base residue identification: Content is to be added here.<br />
;First 3-D structure: Content is to be added here.<br />
<br />
== References ==<br />
<biblio><br />
#Sakurama2013 pmid=23843461<br />
#Gotoh2015 pmid=25839135<br />
#chihaya2017 pmid=28392148<br />
#Michael2020 pmid=32620774<br />
</biblio><br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH136]]</div>Chihaya Yamadahttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_136&diff=15787Glycoside Hydrolase Family 1362020-08-13T07:47:35Z<p>Chihaya Yamada: </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]]: ^^^Chihaya Yamada^^^<br />
* [[Responsible Curator]]: ^^^Shinya Fushinobu^^^<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 GH136'''<br />
|-<br />
|'''Clan''' <br />
|GH-N<br />
|-<br />
|'''Mechanism'''<br />
|retaining<br />
|-<br />
|'''Active site residues'''<br />
|known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH136.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
This family of glycoside hydrolases contains lacto-''N''-biosidase, as demonstrated for LnbX from ''Bifidobacterium longum'' JCM 1217 <cite>Sakurama2013</cite>. LnbX liberates Galβ1-3GlcNAc(lacto-''N''-biose I, LNB) and lactose from lacto-''N''-tetraose, the main component of human milk oligosaccharides. It hydrolyzed the linkage GlcNAcβ1-3Gal in lacto-''N''-hexaose, lacto-''N''-fucopentaose I, and sialyllacto-''N''-tetraose a of human milk oligosaccharides as substrate of LnbX in the GH136. In addition, LnbX liberates Galβ1-3GalNAc (GNB) from the sugar chains of globo- and ganglio-series glycosphingolipids <cite>Gotoh2015</cite>.<br />
<br />
GH136 lacto-''N''-biosidase required neighboring chaperon gene for folding. Rarely, chaperone-like gene fused to lacto-''N''-biosidase gene in case of ErGH136<sub>I</sub> and ErGH136<sub>II</sub>from ''Eubacterium ramulus'' <cite>Michael2020</cite>.<br />
<br />
<br />
== Kinetics and Mechanism ==<br />
Content is to be added here.<br />
<br />
== Catalytic Residues ==<br />
The nucleophile is Asp418. The catalytic acid/base is Asp411 via water molecule.<br />
<br />
== Three-dimensional structures ==<br />
The X-ray crystal structure of the catalytic domain, LnbXc(31-625) revealed a right-handed β helix fold.<br />
Three forms, ligand free (2.36 Å resolution), LNB complex (1.82 Å), and GNB complex (2.70 Å) were determined.<br />
[[file:LnbXc.png|200px|right|'''Figure 1: '''Overall structure of LnbXc with LNB (cyan) and two Ca2+ ions (orange).]]<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Content is to be added here.<br />
;First catalytic nucleophile identification: Content is to be added here.<br />
;First general acid/base residue identification: Content is to be added here.<br />
;First 3-D structure: Content is to be added here.<br />
<br />
== References ==<br />
<biblio><br />
#Sakurama2013 pmid=23843461<br />
#Gotoh2015 pmid=25839135<br />
#chihaya2017 pmid=28392148<br />
#Michael2020 pmid=32620774<br />
</biblio><br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH136]]</div>Chihaya Yamadahttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_136&diff=15786Glycoside Hydrolase Family 1362020-08-13T07:46:12Z<p>Chihaya Yamada: </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]]: ^^^Chihaya Yamada^^^<br />
* [[Responsible Curator]]: ^^^Shinya Fushinobu^^^<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 GH136'''<br />
|-<br />
|'''Clan''' <br />
|GH-N<br />
|-<br />
|'''Mechanism'''<br />
|retaining<br />
|-<br />
|'''Active site residues'''<br />
|known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH136.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
This family of glycoside hydrolases contains lacto-''N''-biosidase, as demonstrated for LnbX from ''Bifidobacterium longum'' JCM 1217 <cite>Sakurama2013</cite>. LnbX liberates Galβ1-3GlcNAc(lacto-''N''-biose I, LNB) and lactose from lacto-''N''-tetraose, the main component of human milk oligosaccharides. It hydrolyzed the linkage GlcNAcβ1-3Gal in lacto-''N''-hexaose, lacto-''N''-fucopentaose I, and sialyllacto-''N''-tetraose a of human milk oligosaccharides as substrate of LnbX in the GH136. In addition, LnbX liberates Galβ1-3GalNAc (GNB) from the sugar chains of globo- and ganglio-series glycosphingolipids <cite>Gotoh2015</cite>.<br />
<br />
GH136 lacto-''N''-biosidase required neighboring chaperon gene for folding. Rarely, chaperone-like gene fused to lacto-''N''-biosidase gene in case of ErGH136<sub>I</sub> and ErGH136<sub>II</sub>from ''Eubacterium ramulus'' <cite>Michael2020</cite>.<br />
<br />
<br />
== Kinetics and Mechanism ==<br />
Content is to be added here.<br />
<br />
== Catalytic Residues ==<br />
The nucleophile is Asp418. The catalytic acid/base is Asp411 via water molecule.<br />
<br />
== Three-dimensional structures ==<br />
The X-ray crystal structure of the catalytic domain, LnbXc(31-625) revealed a right-handed β helix fold.<br />
Three forms, ligand free (2.36 Å resolution), LNB complex (1.82 Å), and GNB complex (2.70 Å) were determined.<br />
[[file:LnbXc.png|200px|right'''Figure 1: '''Overall structure of LnbXc with LNB (cyan) and two Ca2+ ions (orange).]]<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Content is to be added here.<br />
;First catalytic nucleophile identification: Content is to be added here.<br />
;First general acid/base residue identification: Content is to be added here.<br />
;First 3-D structure: Content is to be added here.<br />
<br />
== References ==<br />
<biblio><br />
#Sakurama2013 pmid=23843461<br />
#Gotoh2015 pmid=25839135<br />
#chihaya2017 pmid=28392148<br />
#Michael2020 pmid=32620774<br />
</biblio><br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH136]]</div>Chihaya Yamadahttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_136&diff=15785Glycoside Hydrolase Family 1362020-08-13T07:45:28Z<p>Chihaya Yamada: </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]]: ^^^Chihaya Yamada^^^<br />
* [[Responsible Curator]]: ^^^Shinya Fushinobu^^^<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 GH136'''<br />
|-<br />
|'''Clan''' <br />
|GH-N<br />
|-<br />
|'''Mechanism'''<br />
|retaining<br />
|-<br />
|'''Active site residues'''<br />
|known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH136.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
This family of glycoside hydrolases contains lacto-''N''-biosidase, as demonstrated for LnbX from ''Bifidobacterium longum'' JCM 1217 <cite>Sakurama2013</cite>. LnbX liberates Galβ1-3GlcNAc(lacto-''N''-biose I, LNB) and lactose from lacto-''N''-tetraose, the main component of human milk oligosaccharides. It hydrolyzed the linkage GlcNAcβ1-3Gal in lacto-''N''-hexaose, lacto-''N''-fucopentaose I, and sialyllacto-''N''-tetraose a of human milk oligosaccharides as substrate of LnbX in the GH136. In addition, LnbX liberates Galβ1-3GalNAc (GNB) from the sugar chains of globo- and ganglio-series glycosphingolipids <cite>Gotoh2015</cite>.<br />
<br />
GH136 lacto-''N''-biosidase required neighboring chaperon gene for folding. Rarely, chaperone-like gene fused to lacto-''N''-biosidase gene in case of ErGH136<sub>I</sub> and ErGH136<sub>II</sub>from ''Eubacterium ramulus'' <cite>Michael2020</cite>.<br />
<br />
<br />
== Kinetics and Mechanism ==<br />
Content is to be added here.<br />
<br />
== Catalytic Residues ==<br />
The nucleophile is Asp418. The catalytic acid/base is Asp411 via water molecule.<br />
<br />
== Three-dimensional structures ==<br />
The X-ray crystal structure of the catalytic domain, LnbXc(31-625) revealed a right-handed β helix fold.<br />
Three forms, ligand free (2.36 Å resolution), LNB complex (1.82 Å), and GNB complex (2.70 Å) were determined.<br />
[[file:LnbXc.png|200px|right|'''Figure 1: '''Overall structure of LnbXc with LNB (cyan) and two Ca2+ ions (orange).]]<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Content is to be added here.<br />
;First catalytic nucleophile identification: Content is to be added here.<br />
;First general acid/base residue identification: Content is to be added here.<br />
;First 3-D structure: Content is to be added here.<br />
<br />
== References ==<br />
<biblio><br />
#Sakurama2013 pmid=23843461<br />
#Gotoh2015 pmid=25839135<br />
#chihaya2017 pmid=28392148<br />
#Michael2020 pmid=32620774<br />
</biblio><br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH136]]</div>Chihaya Yamadahttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_136&diff=15783Glycoside Hydrolase Family 1362020-08-13T05:04:04Z<p>Chihaya Yamada: </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]]: ^^^Chihaya Yamada^^^<br />
* [[Responsible Curator]]: ^^^Shinya Fushinobu^^^<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 GH136'''<br />
|-<br />
|'''Clan''' <br />
|GH-N<br />
|-<br />
|'''Mechanism'''<br />
|retaining<br />
|-<br />
|'''Active site residues'''<br />
|known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH136.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
This family of glycoside hydrolases contains lacto-''N''-biosidase, as demonstrated for LnbX from ''Bifidobacterium longum'' JCM 1217 <cite>Sakurama2013</cite>. LnbX liberates Galβ1-3GlcNAc(lacto-''N''-biose I, LNB) and lactose from lacto-''N''-tetraose, the main component of human milk oligosaccharides. It hydrolyzed the linkage GlcNAcβ1-3Gal in lacto-''N''-hexaose, lacto-''N''-fucopentaose I, and sialyllacto-''N''-tetraose a of human milk oligosaccharides as substrate of LnbX in the GH136. In addition, LnbX liberates Galβ1-3GalNAc (GNB) from the sugar chains of globo- and ganglio-series glycosphingolipids <cite>Gotoh2015</cite>.<br />
<br />
GH136 lacto-''N''-biosidase required neighboring chaperon gene for folding. Rarely, chaperone-like gene fused to lacto-''N''-biosidase gene in case of ErGH136<sub>I</sub> and ErGH136<sub>II</sub>from ''Eubacterium ramulus'' <cite>Michael2020</cite>.<br />
<br />
<br />
== Kinetics and Mechanism ==<br />
Content is to be added here.<br />
<br />
== Catalytic Residues ==<br />
The nucleophile is Asp418. The catalytic acid/base is Asp411 via water molecule.<br />
<br />
== Three-dimensional structures ==<br />
The X-ray crystal structure of the catalytic domain, LnbXc(31-625) revealed a right-handed β helix fold.<br />
Three forms, ligand free (2.36 Å resolution), LNB complex (1.82 Å), and GNB complex (2.70 Å) were determined.<br />
[[file:LnbXc.png|200px|right]]<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Content is to be added here.<br />
;First catalytic nucleophile identification: Content is to be added here.<br />
;First general acid/base residue identification: Content is to be added here.<br />
;First 3-D structure: Content is to be added here.<br />
<br />
== References ==<br />
<biblio><br />
#Sakurama2013 pmid=23843461<br />
#Gotoh2015 pmid=25839135<br />
#chihaya2017 pmid=28392148<br />
#Michael2020 pmid=32620774<br />
</biblio><br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH136]]</div>Chihaya Yamadahttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_136&diff=15782Glycoside Hydrolase Family 1362020-08-13T05:00:49Z<p>Chihaya Yamada: </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]]: ^^^Chihaya Yamada^^^<br />
* [[Responsible Curator]]: ^^^Shinya Fushinobu^^^<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 GH136'''<br />
|-<br />
|'''Clan''' <br />
|GH-N<br />
|-<br />
|'''Mechanism'''<br />
|retaining<br />
|-<br />
|'''Active site residues'''<br />
|known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH136.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
This family of glycoside hydrolases contains lacto-''N''-biosidase, as demonstrated for LnbX from ''Bifidobacterium longum'' JCM 1217 <cite>Sakurama2013</cite>. LnbX liberates Galβ1-3GlcNAc(lacto-''N''-biose I, LNB) and lactose from lacto-''N''-tetraose, the main component of human milk oligosaccharides. It hydrolyzed the linkage GlcNAcβ1-3Gal in lacto-''N''-hexaose, lacto-''N''-fucopentaose I, and sialyllacto-''N''-tetraose a of human milk oligosaccharides as substrate of LnbX in the GH136. In addition, LnbX liberates Galβ1-3GalNAc (GNB) from the sugar chains of globo- and ganglio-series glycosphingolipids <cite>Gotoh2015</cite>.<br />
<br />
GH136 lacto-''N''-biosidase required neighboring chaperon gene for folding. Rarely, chaperone-like gene fused to lacto-''N''-biosidase gene in case of ErGH136<sub>I</sub> and ErGH136<sub>II</sub>from ''Eubacterium ramulus'' <cite>Michael2020</cite>.<br />
<br />
<br />
== Kinetics and Mechanism ==<br />
Content is to be added here.<br />
<br />
== Catalytic Residues ==<br />
The nucleophile is Asp418. The catalytic acid/base is Asp411 via water molecule.<br />
<br />
== Three-dimensional structures ==<br />
The X-ray crystal structure of the catalytic domain, LnbXc(31-625) revealed a right-handed β helix fold.<br />
Three forms, ligand free (2.36 Å resolution), LNB complex (1.82 Å), and GNB complex (2.70 Å) were determined.<br />
[[Image:LnbXc.JPG|200px|right]]<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Content is to be added here.<br />
;First catalytic nucleophile identification: Content is to be added here.<br />
;First general acid/base residue identification: Content is to be added here.<br />
;First 3-D structure: Content is to be added here.<br />
<br />
== References ==<br />
<biblio><br />
#Sakurama2013 pmid=23843461<br />
#Gotoh2015 pmid=25839135<br />
#chihaya2017 pmid=28392148<br />
#Michael2020 pmid=32620774<br />
</biblio><br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH136]]</div>Chihaya Yamadahttps://www.cazypedia.org/index.php?title=File:LnbXc.png&diff=15781File:LnbXc.png2020-08-13T04:58:02Z<p>Chihaya Yamada: </p>
<hr />
<div></div>Chihaya Yamadahttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_136&diff=15780Glycoside Hydrolase Family 1362020-08-13T04:39:18Z<p>Chihaya Yamada: </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]]: ^^^Chihaya Yamada^^^<br />
* [[Responsible Curator]]: ^^^Shinya Fushinobu^^^<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 GH136'''<br />
|-<br />
|'''Clan''' <br />
|GH-N<br />
|-<br />
|'''Mechanism'''<br />
|retaining<br />
|-<br />
|'''Active site residues'''<br />
|known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH136.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
This family of glycoside hydrolases contains lacto-''N''-biosidase, as demonstrated for LnbX from ''Bifidobacterium longum'' JCM 1217 <cite>Sakurama2013</cite>. LnbX liberates Galβ1-3GlcNAc(lacto-''N''-biose I, LNB) and lactose from lacto-''N''-tetraose, the main component of human milk oligosaccharides. It hydrolyzed the linkage GlcNAcβ1-3Gal in lacto-''N''-hexaose, lacto-''N''-fucopentaose I, and sialyllacto-''N''-tetraose a of human milk oligosaccharides as substrate of LnbX in the GH136. In addition, LnbX liberates Galβ1-3GalNAc (GNB) from the sugar chains of globo- and ganglio-series glycosphingolipids <cite>Gotoh2015</cite>.<br />
<br />
GH136 lacto-''N''-biosidase required neighboring chaperon gene for folding. Rarely, chaperone-like gene fused to lacto-''N''-biosidase gene in case of ErGH136<sub>I</sub> and ErGH136<sub>II</sub>from ''Eubacterium ramulus'' <cite>Michael2020</cite>.<br />
<br />
<br />
== Kinetics and Mechanism ==<br />
Content is to be added here.<br />
<br />
== Catalytic Residues ==<br />
The nucleophile is Asp418. The catalytic acid/base is Asp411 via water molecule.<br />
<br />
== Three-dimensional structures ==<br />
The X-ray crystal structure of the catalytic domain, LnbXc(31-625) revealed a right-handed β helix fold.<br />
Three forms, ligand free (2.36 Å resolution), LNB complex (1.82 Å), and GNB complex (2.70 Å) were determined.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Content is to be added here.<br />
;First catalytic nucleophile identification: Content is to be added here.<br />
;First general acid/base residue identification: Content is to be added here.<br />
;First 3-D structure: Content is to be added here.<br />
<br />
== References ==<br />
<biblio><br />
#Sakurama2013 pmid=23843461<br />
#Gotoh2015 pmid=25839135<br />
#chihaya2017 pmid=28392148<br />
#Michael2020 pmid=32620774<br />
</biblio><br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH136]]</div>Chihaya Yamadahttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_136&diff=15779Glycoside Hydrolase Family 1362020-08-13T04:16:14Z<p>Chihaya Yamada: </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]]: ^^^Chihaya Yamada^^^<br />
* [[Responsible Curator]]: ^^^Shinya Fushinobu^^^<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 GH136'''<br />
|-<br />
|'''Clan''' <br />
|GH-N<br />
|-<br />
|'''Mechanism'''<br />
|retaining<br />
|-<br />
|'''Active site residues'''<br />
|known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH136.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
This family of glycoside hydrolases contains lacto-''N''-biosidase, as demonstrated for LnbX from ''Bifidobacterium longum'' JCM 1217 <cite>Sakurama2013</cite>. LnbX liberates Galβ1-3GlcNAc(lacto-''N''-biose I, LNB) and lactose from lacto-''N''-tetraose, the main component of human milk oligosaccharides. It hydrolyzed the linkage GlcNAcβ1-3Gal in lacto-''N''-hexaose, lacto-''N''-fucopentaose I, and sialyllacto-''N''-tetraose a of human milk oligosaccharides as substrate of LnbX in the GH136. In addition, LnbX liberates Galβ1-3GalNAc (GNB) from the sugar chains of globo- and ganglio-series glycosphingolipids <cite>Gotoh2015</cite>.<br />
<br />
GH136 lacto-''N''-biosidase required neighboring chaperon gene for folding. Rarely, chaperone-like gene fused to lacto-''N''-biosidase gene in case of ErGH136<sub>I</sub> and ErGH136<sub>II</sub>from ''Eubacterium ramulus'' <cite>Michael2020</cite>.<br />
<br />
<br />
== Kinetics and Mechanism ==<br />
Content is to be added here.<br />
<br />
== Catalytic Residues ==<br />
The nucleophile is Asp418. The catalytic acid/base is Asp411 via water molecule.<br />
<br />
== Three-dimensional structures ==<br />
Content is to be added here.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Content is to be added here.<br />
;First catalytic nucleophile identification: Content is to be added here.<br />
;First general acid/base residue identification: Content is to be added here.<br />
;First 3-D structure: Content is to be added here.<br />
<br />
== References ==<br />
<biblio><br />
#Sakurama2013 pmid=23843461<br />
#Gotoh2015 pmid=25839135<br />
#chihaya2017 pmid=28392148<br />
#Michael2020 pmid=32620774<br />
</biblio><br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH136]]</div>Chihaya Yamadahttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_136&diff=15778Glycoside Hydrolase Family 1362020-08-13T04:08:22Z<p>Chihaya Yamada: </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]]: ^^^Chihaya Yamada^^^<br />
* [[Responsible Curator]]: ^^^Shinya Fushinobu^^^<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 GH136'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|retaining<br />
|-<br />
|'''Active site residues'''<br />
|known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH136.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
This family of glycoside hydrolases contains lacto-''N''-biosidase, as demonstrated for LnbX from ''Bifidobacterium longum'' JCM 1217 <cite>Sakurama2013</cite>. LnbX liberates Galβ1-3GlcNAc(lacto-''N''-biose I, LNB) and lactose from lacto-''N''-tetraose, the main component of human milk oligosaccharides. It hydrolyzed the linkage GlcNAcβ1-3Gal in lacto-''N''-hexaose, lacto-''N''-fucopentaose I, and sialyllacto-''N''-tetraose a of human milk oligosaccharides as substrate of LnbX in the GH136. In addition, LnbX liberates Galβ1-3GalNAc (GNB) from the sugar chains of globo- and ganglio-series glycosphingolipids <cite>Gotoh2015</cite>.<br />
<br />
GH136 lacto-''N''-biosidase required neighboring chaperon gene for folding. Rarely, chaperone-like gene fused to lacto-''N''-biosidase gene in case of ErGH136I and ErGh136II from ''Eubacterium ramulus'' <cite>Michael2020</cite>.<br />
<br />
<br />
== Kinetics and Mechanism ==<br />
Content is to be added here.<br />
<br />
== Catalytic Residues ==<br />
The nucleophile is Asp418. The catalytic acid/base is Asp411 via water molecule.<br />
<br />
== Three-dimensional structures ==<br />
Content is to be added here.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Content is to be added here.<br />
;First catalytic nucleophile identification: Content is to be added here.<br />
;First general acid/base residue identification: Content is to be added here.<br />
;First 3-D structure: Content is to be added here.<br />
<br />
== References ==<br />
<biblio><br />
#Sakurama2013 pmid=23843461<br />
#Gotoh2015 pmid=25839135<br />
#chihaya2017 pmid=28392148<br />
#Michael2020 pmid=32620774<br />
</biblio><br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH136]]</div>Chihaya Yamadahttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_136&diff=15777Glycoside Hydrolase Family 1362020-08-13T04:06:55Z<p>Chihaya Yamada: </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]]: ^^^Chihaya Yamada^^^<br />
* [[Responsible Curator]]: ^^^Shinya Fushinobu^^^<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 GH136'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|retaining<br />
|-<br />
|'''Active site residues'''<br />
|known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH136.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
This family of glycoside hydrolases contains lacto-''N''-biosidase, as demonstrated for LnbX from ''Bifidobacterium longum'' JCM 1217 <cite>Sakurama2013</cite>. LnbX liberates Galβ1-3GlcNAc(lacto-''N''-biose I, LNB) and lactose from lacto-''N''-tetraose, the main component of human milk oligosaccharides. It hydrolyzed the linkage GlcNAcβ1-3Gal in lacto-''N''-hexaose, lacto-''N''-fucopentaose I, and sialyllacto-''N''-tetraose a of human milk oligosaccharides as substrate of LnbX in the GH136. In addition, LnbX liberates Galβ1-3GalNAc (GNB) from the sugar chains of globo- and ganglio-series glycosphingolipids <cite>Gotoh2015</cite>.<br />
<br />
GH136 lacto-''N''-biosidase required neighboring chaperon gene for folding. Rarely, chaperone-like gene fused to lacto-''N''-biosidase gene in case of ErGH136I and ErGh136II from ''Eubacterium ramulus'' <cite>Michael2020</cite>.<br />
<br />
<br />
== Kinetics and Mechanism ==<br />
Content is to be added here.<br />
<br />
== Catalytic Residues ==<br />
The nucleophile is Asp418. The catalytic acid/base is Asp411 via water molecule.<br />
<br />
== Three-dimensional structures ==<br />
Content is to be added here.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Content is to be added here.<br />
;First catalytic nucleophile identification: Content is to be added here.<br />
;First general acid/base residue identification: Content is to be added here.<br />
;First 3-D structure: Content is to be added here.<br />
<br />
== References ==<br />
<biblio><br />
#Sakurama2013 pmid=23843461<br />
#Gotoh2015 pmid=25839135<br />
#chihaya2017 pmid=28392148<br />
#Michael2020 pmid=32620774<br />
</biblio><br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH136]]</div>Chihaya Yamadahttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_136&diff=15776Glycoside Hydrolase Family 1362020-08-12T11:26:27Z<p>Chihaya Yamada: </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]]: ^^^Chihaya Yamada^^^<br />
* [[Responsible Curator]]: ^^^Shinya Fushinobu^^^<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 GH136'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|retaining<br />
|-<br />
|'''Active site residues'''<br />
|known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH136.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
This family of glycoside hydrolases contains lacto-''N''-biosidase, as demonstrated for LnbX from ''Bifidobacterium longum'' JCM 1217 <cite>Sakurama2013</cite>. LnbX hydrolyzed the linkage GlcNAcβ1-3Gal to liberate Galβ1-3GlcNAc(lacto-''N''-biose I, LNB) from lacto-''N''-tetraose, lacto-''N''-hexaose, lacto-''N''-fucopentaose I, and sialyllacto-''N''-tetraose a of Human milk Oligosaccharides as substrate of LnbX in the GH136. In addition, LnbX liberates Galβ1-3GalNAc (GNB) from the sugar chains of globo- and ganglio-series glycosphingolipids <cite>Gotoh2015</cite>. <br />
<br />
<br />
<br />
== Kinetics and Mechanism ==<br />
Content is to be added here.<br />
<br />
== Catalytic Residues ==<br />
The nucleophile is Asp418. The catalytic acid/base is Asp411 via water molecule.<br />
<br />
== Three-dimensional structures ==<br />
Content is to be added here.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Content is to be added here.<br />
;First catalytic nucleophile identification: Content is to be added here.<br />
;First general acid/base residue identification: Content is to be added here.<br />
;First 3-D structure: Content is to be added here.<br />
<br />
== References ==<br />
<biblio><br />
#Sakurama2013 pmid=23843461<br />
#Gotoh2015 pmid=25839135<br />
#chihaya2017 pmid=28392148<br />
#Michael2020 pmid=32620774<br />
</biblio><br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH136]]</div>Chihaya Yamadahttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_136&diff=15775Glycoside Hydrolase Family 1362020-08-12T11:23:33Z<p>Chihaya Yamada: </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]]: ^^^Chihaya Yamada^^^<br />
* [[Responsible Curator]]: ^^^Shinya Fushinobu^^^<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 GH136'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|retaining<br />
|-<br />
|'''Active site residues'''<br />
|known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH136.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
This family of glycoside hydrolases contains lacto-''N''-biosidase, as demonstrated for LnbX from ''Bifidobacterium longum'' JCM 1217 <cite>Sakurama2013</cite>. LnbX hydrolyzed the linkage GlcNAcβ1-3Gal to liberate Galβ1-3GlcNAc(lacto-''N''-biose I, LNB) in lacto-''N''-tetraose, lacto-''N''-hexaose, lacto-''N''-fucopentaose I, and sialyllacto-''N''-tetraose a of Human milk Oligosaccharides as substrate of LnbX in the GH136. In addition, LnbX liberates Galβ1-3GalNAc (GNB) from the sugar chains of globo- and ganglio-series glycosphingolipids <cite>Gotoh2015</cite>. <br />
<br />
<br />
<br />
== Kinetics and Mechanism ==<br />
Content is to be added here.<br />
<br />
== Catalytic Residues ==<br />
The nucleophile is Asp418. The catalytic acid/base is Asp411 via water molecule.<br />
<br />
== Three-dimensional structures ==<br />
Content is to be added here.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Content is to be added here.<br />
;First catalytic nucleophile identification: Content is to be added here.<br />
;First general acid/base residue identification: Content is to be added here.<br />
;First 3-D structure: Content is to be added here.<br />
<br />
== References ==<br />
<biblio><br />
#Sakurama2013 pmid=23843461<br />
#Gotoh2015 pmid=25839135<br />
#chihaya2017 pmid=28392148<br />
#Michael2020 pmid=32620774<br />
</biblio><br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH136]]</div>Chihaya Yamadahttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_136&diff=15774Glycoside Hydrolase Family 1362020-08-12T01:07:12Z<p>Chihaya Yamada: </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]]: ^^^Chihaya Yamada^^^<br />
* [[Responsible Curator]]: ^^^Shinya Fushinobu^^^<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 GH136'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|retaining<br />
|-<br />
|'''Active site residues'''<br />
|known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH136.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
This family of glycoside hydrolases contains lacto-''N''-biosidase, as demonstrated for LnbX from ''Bifidobacterium longum'' JCM 1217 <cite>Sakurama2013</cite>. LnbX hydrolyzed the linkage Galβ1-3GlcNAc(lacto-''N''-biose I, LNB) in lacto-''N''-tetraose, lacto-''N''-hexaose, lacto-''N''-fucopentaose I, and sialyllacto-''N''-tetraose a of Human milk Oligosaccharides as substrate of LnbX in the GH136. In addition, LnbX liberates Galβ1-3GalNAc (GNB) from the sugar chains of globo- and ganglio-series glycosphingolipids <cite>Gotoh2015</cite>. <br />
<br />
<br />
<br />
== Kinetics and Mechanism ==<br />
Content is to be added here.<br />
<br />
== Catalytic Residues ==<br />
The nucleophile is Asp418. The catalytic acid/base is Asp411 via water molecule.<br />
<br />
== Three-dimensional structures ==<br />
Content is to be added here.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Content is to be added here.<br />
;First catalytic nucleophile identification: Content is to be added here.<br />
;First general acid/base residue identification: Content is to be added here.<br />
;First 3-D structure: Content is to be added here.<br />
<br />
== References ==<br />
<biblio><br />
#Sakurama2013 pmid=23843461<br />
#Gotoh2015 pmid=25839135<br />
#chihaya2017 pmid=28392148<br />
#Michael2020 pmid=32620774<br />
</biblio><br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH136]]</div>Chihaya Yamadahttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_136&diff=15763Glycoside Hydrolase Family 1362020-08-11T07:52:13Z<p>Chihaya Yamada: </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]]: ^^^Chihaya Yamada^^^<br />
* [[Responsible Curator]]: ^^^Shinya Fushinobu^^^<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 GH136'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|retaining<br />
|-<br />
|'''Active site residues'''<br />
|known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH136.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
This family of glycoside hydrolases contains lacto-''N''-biosidase, as demonstrated for LnbX from ''Bifidobacterium longum'' JCM 1217 <cite>Sakurama2013</cite>. LnbX hydrolyzed the linkage Galβ1-3GlcNAc(lacto-''N''-biose I, LNB) in lacto-''N''-tetraose, lacto-''N''-hexaose, lacto-''N''-fucopentaose I, and sialyllacto-''N''-tetraose a of Human milk Oligosaccharides as substrate of the GH136 lacto-''N''-biosidase from ''B. longum'' JCM 1217. In addition, LnbX liberates Galβ1-3GalNAc (GNB) from the sugar chains of globo- and ganglio-series glycosphingolipids <cite>Gotoh2015</cite>. <br />
<br />
<br />
<br />
== Kinetics and Mechanism ==<br />
Content is to be added here.<br />
<br />
== Catalytic Residues ==<br />
The nucleophile is Asp418. The catalytic acid/base is Asp411 via water molecule.<br />
<br />
== Three-dimensional structures ==<br />
Content is to be added here.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Content is to be added here.<br />
;First catalytic nucleophile identification: Content is to be added here.<br />
;First general acid/base residue identification: Content is to be added here.<br />
;First 3-D structure: Content is to be added here.<br />
<br />
== References ==<br />
<biblio><br />
#Sakurama2013 pmid=23843461<br />
#Gotoh2015 pmid=25839135<br />
#chihaya2017 pmid=28392148<br />
#Michael2020 pmid=32620774<br />
</biblio><br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH136]]</div>Chihaya Yamadahttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_136&diff=15762Glycoside Hydrolase Family 1362020-08-11T07:43:39Z<p>Chihaya Yamada: </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]]: ^^^Chihaya Yamada^^^<br />
* [[Responsible Curator]]: ^^^Shinya Fushinobu^^^<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 GH136'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|retaining<br />
|-<br />
|'''Active site residues'''<br />
|known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH136.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
This family of glycoside hydrolases contains lacto-''N''-biosidase, as demonstrated for LnbX from ''Bifidobacterium longum'' JCM 1217 <cite>Sakurama2013</cite>. LnbX liberates the disaccharide Galβ1-3GlcNAc(lacto-''N''-biose I, LNB) from Human Milk Oligossacharides, lacto-''N''-tetraose, as substrate of the GH136 lacto-N-biosidase from ''B. longum'' JCM 1217. In addition, LnbX liberates Galβ1-3GalNAc (GNB) from the sugar chains of globo- and ganglio-series glycosphingolipids <cite>Gotoh2015</cite>. <br />
<br />
<br />
<br />
== Kinetics and Mechanism ==<br />
Content is to be added here.<br />
<br />
== Catalytic Residues ==<br />
The nucleophile is Asp418. The catalytic acid/base is Asp411 via water molecule.<br />
<br />
== Three-dimensional structures ==<br />
Content is to be added here.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Content is to be added here.<br />
;First catalytic nucleophile identification: Content is to be added here.<br />
;First general acid/base residue identification: Content is to be added here.<br />
;First 3-D structure: Content is to be added here.<br />
<br />
== References ==<br />
<biblio><br />
#Sakurama2013 pmid=23843461<br />
#Gotoh2015 pmid=25839135<br />
#chihaya2017 pmid=28392148<br />
#Michael2020 pmid=32620774<br />
</biblio><br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH136]]</div>Chihaya Yamadahttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_136&diff=15761Glycoside Hydrolase Family 1362020-08-11T07:38:24Z<p>Chihaya Yamada: </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]]: ^^^Chihaya Yamada^^^<br />
* [[Responsible Curator]]: ^^^Shinya Fushinobu^^^<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 GH136'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|retaining<br />
|-<br />
|'''Active site residues'''<br />
|known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH136.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
This family of glycoside hydrolases contains Lacto-N-biosidase, as demonstrated for LnbX from Bifidobacterium longum JCM 1217 <cite>Sakurama2013</cite>. LnbX liberates the disaccharide Galβ1-3GlcNAc(LNB) from Human Milk Oligossacharides, lacto-N-tetraose, Lacto-N-fucopentaose I, lacto-N-tetraose, lacto-N-fucopentaose I, and sialyllacto-N-tetraose a as substrate of the GH136 lacto-N-biosidase from B. longum JCM 1217.<br />
<br />
In addition, LnbX liberates Galβ1-3GalNAc (GNB) from the sugar chains of globo- and ganglio-series glycosphingolipids <cite>.<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 />
Content is to be added here.<br />
<br />
== Catalytic Residues ==<br />
The nucleophile is Asp418. The catalytic acid/base is Asp411 via water molecule.<br />
<br />
== Three-dimensional structures ==<br />
Content is to be added here.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Content is to be added here.<br />
;First catalytic nucleophile identification: Content is to be added here.<br />
;First general acid/base residue identification: Content is to be added here.<br />
;First 3-D structure: Content is to be added here.<br />
<br />
== References ==<br />
<biblio><br />
#Sakurama2013 pmid=23843461<br />
#Gotoh2015 pmid=25839135<br />
#chihaya2017 pmid=28392148<br />
#Michael2020 pmid=32620774<br />
</biblio><br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH136]]</div>Chihaya Yamadahttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_136&diff=15760Glycoside Hydrolase Family 1362020-08-11T07:34:54Z<p>Chihaya Yamada: </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]]: ^^^Chihaya Yamada^^^<br />
* [[Responsible Curator]]: ^^^Shinya Fushinobu^^^<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 GH136'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|retaining<br />
|-<br />
|'''Active site residues'''<br />
|known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH136.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Content is to be added here.<br />
<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 />
Content is to be added here.<br />
<br />
== Catalytic Residues ==<br />
The nucleophile is Asp418. The catalytic acid/base is Asp411 via water molecule.<br />
<br />
== Three-dimensional structures ==<br />
Content is to be added here.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Content is to be added here.<br />
;First catalytic nucleophile identification: Content is to be added here.<br />
;First general acid/base residue identification: Content is to be added here.<br />
;First 3-D structure: Content is to be added here.<br />
<br />
== References ==<br />
<biblio><br />
#Sakurama2013 pmid=23843461<br />
#Gotoh2015 pmid=25839135<br />
#chihaya2017 pmid=28392148<br />
#Michael2020 pmid=32620774<br />
<br />
</biblio><br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH136]]</div>Chihaya Yamadahttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_136&diff=15759Glycoside Hydrolase Family 1362020-08-11T07:27:02Z<p>Chihaya Yamada: </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]]: ^^^Chihaya Yamada^^^<br />
* [[Responsible Curator]]: ^^^Shinya Fushinobu^^^<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 GH136'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|retaining<br />
|-<br />
|'''Active site residues'''<br />
|known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH136.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Content is to be added here.<br />
<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 />
Content is to be added here.<br />
<br />
== Catalytic Residues ==<br />
The nucleophile is Asp418. The catalytic acid/base is Asp411 via water molecule.<br />
<br />
== Three-dimensional structures ==<br />
Content is to be added here.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Content is to be added here.<br />
;First catalytic nucleophile identification: Content is to be added here.<br />
;First general acid/base residue identification: Content is to be added here.<br />
;First 3-D structure: Content is to be added here.<br />
<br />
== References ==<br />
<biblio><br />
#Sakurama2013 pmid=23843461<br />
#chihaya2017 pmid=28392148<br />
#Michael2020 pmid=32620774<br />
<br />
</biblio><br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH136]]</div>Chihaya Yamadahttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_136&diff=15758Glycoside Hydrolase Family 1362020-08-11T04:06:24Z<p>Chihaya Yamada: </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]]: ^^^Chihaya Yamada^^^<br />
* [[Responsible Curator]]: ^^^Shinya Fushinobu^^^<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 GH136'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|retaining<br />
|-<br />
|'''Active site residues'''<br />
|known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH136.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Content is to be added here.<br />
<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 />
Content is to be added here.<br />
<br />
== Catalytic Residues ==<br />
The nucleophile is Asp418. The catalytic acid/base is Asp411 via water molecule.<br />
<br />
== Three-dimensional structures ==<br />
Content is to be added here.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Content is to be added here.<br />
;First catalytic nucleophile identification: Content is to be added here.<br />
;First general acid/base residue identification: Content is to be added here.<br />
;First 3-D structure: Content is to be added here.<br />
<br />
== References ==<br />
<biblio><br />
#chihaya2017 pmid=28392148<br />
#Michael2020 pmid=32620774<br />
<br />
</biblio><br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH136]]</div>Chihaya Yamadahttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_136&diff=15757Glycoside Hydrolase Family 1362020-08-11T04:05:53Z<p>Chihaya Yamada: </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]]: ^^^Chihaya Yamada^^^<br />
* [[Responsible Curator]]: ^^^Shinya Fushinobu^^^<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 GH136'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|retaining<br />
|-<br />
|'''Active site residues'''<br />
|known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH136.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Content is to be added here.<br />
<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 />
Content is to be added here.<br />
<br />
== Catalytic Residues ==<br />
The nucleophile is Asp418. The catalytic acid/base is Asp411 via water molecule.<br />
<br />
== Three-dimensional structures ==<br />
Content is to be added here.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Content is to be added here.<br />
;First catalytic nucleophile identification: Content is to be added here.<br />
;First general acid/base residue identification: Content is to be added here.<br />
;First 3-D structure: Content is to be added here.<br />
<br />
== References ==<br />
<br />
<biblio><br />
#CCB2017 pmid=28392148<br />
#NatureComm2020 pmid=32620774<br />
<biblio><br />
#chihaya2017 pmid=28392148<br />
#Michael2020 pmid=32620774<br />
<br />
</biblio><br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH136]]</div>Chihaya Yamadahttps://www.cazypedia.org/index.php?title=User:Chihaya_Yamada&diff=15756User:Chihaya Yamada2020-08-11T04:05:15Z<p>Chihaya Yamada: </p>
<hr />
<div>[[Image:chihaya.JPG|200px|right]]<br />
<br />
Chihaya Yamada is an assistant professor at the Laboratory of Enzymology in the Department of Biotechnology, Graduate School of Agricultural and Life Sciences, The University of Tokyo located in Tokyo, Japan. I obtained Ph.D degree in Agriculture at The University of Tokyo in 2013. I contributed to structural analysis of lacto-''N''-biosidase (LnbX) from ''Bifidobacterium longum'' subsp. ''longum'' belonging to [[GH136]] with Prof. ^^^Shinya Fushinobu^^^ and Prof. ^^^Takane Katayama^^^ <cite>chihaya2017</cite>. My reseach interests are new enzymes from human gut microbiota.<br />
<br />
----<br />
<br />
<biblio><br />
#chihaya2017 pmid=28392148<br />
#Michael2020 pmid=32620774<br />
<br />
</biblio><br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Yamada,Chihaya]]</div>Chihaya Yamadahttps://www.cazypedia.org/index.php?title=User:Chihaya_Yamada&diff=15755User:Chihaya Yamada2020-08-11T04:04:50Z<p>Chihaya Yamada: </p>
<hr />
<div>[[Image:chihaya.JPG|200px|right]]<br />
<br />
Chihaya Yamada is an assistant professor at the Laboratory of Enzymology in the Department of Biotechnology, Graduate School of Agricultural and Life Sciences, The University of Tokyo located in Tokyo, Japan. I obtained Ph.D degree in Agriculture at The University of Tokyo in 2013. I contributed to structural analysis of lacto-''N''-biosidase (LnbX) from ''Bifidobacterium longum'' subsp. ''longum'' belonging to [[GH136]] with Prof. ^^^Shinya Fushinobu^^^ and Prof. Takane Katayama <cite>chihaya2017</cite>. My reseach interests are new enzymes from human gut microbiota.<br />
<br />
----<br />
<br />
<biblio><br />
#chihaya2017 pmid=28392148<br />
#Michael2020 pmid=32620774<br />
<br />
</biblio><br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Yamada,Chihaya]]</div>Chihaya Yamadahttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_136&diff=15754Glycoside Hydrolase Family 1362020-08-11T04:02:26Z<p>Chihaya Yamada: </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]]: ^^^Chihaya Yamada^^^<br />
* [[Responsible Curator]]: ^^^Shinya Fushinobu^^^<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 GH136'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|retaining<br />
|-<br />
|'''Active site residues'''<br />
|known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH136.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Content is to be added here.<br />
<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 />
Content is to be added here.<br />
<br />
== Catalytic Residues ==<br />
The nucleophile is Asp418. The catalytic acid/base is Asp411 via water molecule.<br />
<br />
== Three-dimensional structures ==<br />
Content is to be added here.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Content is to be added here.<br />
;First catalytic nucleophile identification: Content is to be added here.<br />
;First general acid/base residue identification: Content is to be added here.<br />
;First 3-D structure: Content is to be added here.<br />
<br />
== References ==<br />
<br />
<biblio><br />
#CCB2017 pmid=28392148<br />
#NatureComm2020 pmid=32620774<br />
<br />
</biblio><br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH136]]</div>Chihaya Yamadahttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_136&diff=15753Glycoside Hydrolase Family 1362020-08-11T03:59:15Z<p>Chihaya Yamada: </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]]: ^^^Chihaya Yamada^^^<br />
* [[Responsible Curator]]: ^^^Shinya Fushinobu^^^<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 GH136'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|retaining<br />
|-<br />
|'''Active site residues'''<br />
|known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH136.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Content is to be added here.<br />
<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 />
Content is to be added here.<br />
<br />
== Catalytic Residues ==<br />
The nucleophile is Asp418. The catalytic acid/base is Asp411 via water molecule.<br />
<br />
== Three-dimensional structures ==<br />
Content is to be added here.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Content is to be added here.<br />
;First catalytic nucleophile identification: Content is to be added here.<br />
;First general acid/base residue identification: Content is to be added here.<br />
;First 3-D structure: Content is to be added here.<br />
<br />
== References ==<br />
<biblio><br />
#CCB2017 pmid=28392148<br />
#NatureComm2020 pmid=32620774<br />
<br />
</biblio><br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH136]]</div>Chihaya Yamadahttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_136&diff=15752Glycoside Hydrolase Family 1362020-08-11T03:58:12Z<p>Chihaya Yamada: </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]]: ^^^Chihaya Yamada^^^<br />
* [[Responsible Curator]]: ^^^Shinya Fushinobu^^^<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 GH136'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|retaining<br />
|-<br />
|'''Active site residues'''<br />
|known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH136.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Content is to be added here.<br />
<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 />
Content is to be added here.<br />
<br />
== Catalytic Residues ==<br />
The nucleophile is Asp418. The catalytic acid/base is Asp411 via water molecule.<br />
<br />
== Three-dimensional structures ==<br />
Content is to be added here.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Content is to be added here.<br />
;First catalytic nucleophile identification: Content is to be added here.<br />
;First general acid/base residue identification: Content is to be added here.<br />
;First 3-D structure: Content is to be added here.<br />
<br />
== References ==<br />
<biblio><br />
#CCB2017 pmid=28392148<br />
<br />
<biblio><br />
#NatureComm2020 pmid=32620774<br />
<br />
[[Category:Glycoside Hydrolase Families|GH136]]</div>Chihaya Yamadahttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_136&diff=15751Glycoside Hydrolase Family 1362020-08-11T03:57:35Z<p>Chihaya Yamada: </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]]: ^^^Chihaya Yamada^^^<br />
* [[Responsible Curator]]: ^^^Shinya Fushinobu^^^<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 GH136'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|retaining<br />
|-<br />
|'''Active site residues'''<br />
|known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH136.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Content is to be added here.<br />
<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 />
Content is to be added here.<br />
<br />
== Catalytic Residues ==<br />
The nucleophile is Asp418. The catalytic acid/base is Asp411 via water molecule.<br />
<br />
== Three-dimensional structures ==<br />
Content is to be added here.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Content is to be added here.<br />
;First catalytic nucleophile identification: Content is to be added here.<br />
;First general acid/base residue identification: Content is to be added here.<br />
;First 3-D structure: Content is to be added here.<br />
<br />
== References ==<br />
<biblio><br />
#CCB2017 pmid=28392148<br />
<biblio><br />
#NatureCommu2020 pmid=32620774<br />
<br />
[[Category:Glycoside Hydrolase Families|GH136]]</div>Chihaya Yamadahttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_136&diff=15750Glycoside Hydrolase Family 1362020-08-11T03:57:11Z<p>Chihaya Yamada: </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]]: ^^^Chihaya Yamada^^^<br />
* [[Responsible Curator]]: ^^^Shinya Fushinobu^^^<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 GH136'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|retaining<br />
|-<br />
|'''Active site residues'''<br />
|known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH136.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Content is to be added here.<br />
<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 />
Content is to be added here.<br />
<br />
== Catalytic Residues ==<br />
The nucleophile is Asp418. The catalytic acid/base is Asp411 via water molecule.<br />
<br />
== Three-dimensional structures ==<br />
Content is to be added here.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Content is to be added here.<br />
;First catalytic nucleophile identification: Content is to be added here.<br />
;First general acid/base residue identification: Content is to be added here.<br />
;First 3-D structure: Content is to be added here.<br />
<br />
== References ==<br />
<biblio><br />
#CCB2017 pmid=28392148<br />
<br />
</biblio><br />
#NatureCommu2020 pmid=32620774<br />
<br />
[[Category:Glycoside Hydrolase Families|GH136]]</div>Chihaya Yamadahttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_136&diff=15749Glycoside Hydrolase Family 1362020-08-11T03:52:41Z<p>Chihaya Yamada: </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]]: ^^^Chihaya Yamada^^^<br />
* [[Responsible Curator]]: ^^^Shinya Fushinobu^^^<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 GH136'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|retaining<br />
|-<br />
|'''Active site residues'''<br />
|known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH136.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Content is to be added here.<br />
<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 />
Content is to be added here.<br />
<br />
== Catalytic Residues ==<br />
The nucleophile is Asp418. The catalytic acid/base is Asp411 via water molecule.<br />
<br />
== Three-dimensional structures ==<br />
Content is to be added here.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Content is to be added here.<br />
;First catalytic nucleophile identification: Content is to be added here.<br />
;First general acid/base residue identification: Content is to be added here.<br />
;First 3-D structure: Content is to be added here.<br />
<br />
== References ==<br />
<biblio><br />
#CCB2017 pmid=28392148<br />
<br />
</biblio><br />
<br />
[[Category:Glycoside Hydrolase Families|GH136]]</div>Chihaya Yamadahttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_136&diff=15748Glycoside Hydrolase Family 1362020-08-11T03:39:09Z<p>Chihaya Yamada: </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]]: ^^^Chihaya Yamada^^^<br />
* [[Responsible Curator]]: ^^^Shinya Fushinobu^^^<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 GH136'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|retaining<br />
|-<br />
|'''Active site residues'''<br />
|known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH136.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Content is to be added here.<br />
<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 />
Content is to be added here.<br />
<br />
== Catalytic Residues ==<br />
The nucleophile is Asp418. The catalytic acid/base is Asp411 via water molecule.<br />
<br />
== Three-dimensional structures ==<br />
Content is to be added here.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Content is to be added here.<br />
;First catalytic nucleophile identification: Content is to be added here.<br />
;First general acid/base residue identification: Content is to be added here.<br />
;First 3-D structure: Content is to be added here.<br />
<br />
== References ==<br />
<biblio><br />
#Cantarel2009 pmid=18838391<br />
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [https://doi.org/10.1042/BIO03004026 Download PDF version].<br />
</biblio><br />
<br />
[[Category:Glycoside Hydrolase Families|GH136]]</div>Chihaya Yamadahttps://www.cazypedia.org/index.php?title=User:Chihaya_Yamada&diff=15746User:Chihaya Yamada2020-08-11T01:50:14Z<p>Chihaya Yamada: </p>
<hr />
<div>[[Image:chihaya.JPG|200px|right]]<br />
<br />
Chihaya Yamada is an assistant professor at Laboratory of Enzymology in Department of Biotechnology, Graduate School of Agricultural and Life Sciences, The University of Tokyo located in Tokyo, Japan. I obtained Ph.D degree in Agriculture at The University of Tokyo in 2013. I contributed to structure analysis of lacto-''N''-biosidase (LnbX) from ''Bifidobacterium longum'' subsp. ''longum'' belonging to [[GH136]] with Prof. Shinya Fushinobu and Prof. Takane Katayama. My reseach interests are new enzymes from Human gut microbiota.<br />
<br />
----<br />
<br />
<biblio><br />
#chihaya2017 pmid=28392148<br />
#Michael2020 pmid=32620774<br />
<br />
</biblio><br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Yamada,Chihaya]]</div>Chihaya Yamadahttps://www.cazypedia.org/index.php?title=File:Chihaya.JPG&diff=15741File:Chihaya.JPG2020-08-10T15:05:19Z<p>Chihaya Yamada: Chihaya Yamada uploaded a new version of File:Chihaya.JPG</p>
<hr />
<div></div>Chihaya Yamadahttps://www.cazypedia.org/index.php?title=File:Chihaya.JPG&diff=15740File:Chihaya.JPG2020-08-10T14:55:01Z<p>Chihaya Yamada: </p>
<hr />
<div></div>Chihaya Yamadahttps://www.cazypedia.org/index.php?title=User:Chihaya_Yamada&diff=15739User:Chihaya Yamada2020-08-10T14:51:19Z<p>Chihaya Yamada: </p>
<hr />
<div>[[Image:chihaya.JPG|200px|right]]<br />
<br />
Chihaya Yamada is an assistant professor at Laboratory of Enzymology in Department of Biotechnology, Graduate School of Agricultural and Life Sciences, The University of Tokyo located in Tokyo, Japan. I obtained Ph.D degree in Department of Biotechnology, The University of Tokyo in 2013. I contributed to structure analysis of lacto-''N''-biosidase (LnbX) from ''Bifidobacterium longum'' subsp. ''longum'' belonging to [[GH136]] with Prof. Shinya Fushinobu and Prof. Takane Katayama. My reseach interests are new enzymes from Human gut microbiota.<br />
<br />
----<br />
<br />
<biblio><br />
#chihaya2017 pmid=28392148<br />
#Michael2020 pmid=32620774<br />
<br />
</biblio><br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Yamada,Chihaya]]</div>Chihaya Yamadahttps://www.cazypedia.org/index.php?title=User:Chihaya_Yamada&diff=15738User:Chihaya Yamada2020-08-10T14:50:41Z<p>Chihaya Yamada: </p>
<hr />
<div>[[Image:chihaya.png|200px|right]]<br />
<br />
Chihaya Yamada is an assistant professor at Laboratory of Enzymology in Department of Biotechnology, Graduate School of Agricultural and Life Sciences, The University of Tokyo located in Tokyo, Japan. I obtained Ph.D degree in Department of Biotechnology, The University of Tokyo in 2013. I contributed to structure analysis of lacto-''N''-biosidase (LnbX) from ''Bifidobacterium longum'' subsp. ''longum'' belonging to [[GH136]] with Prof. Shinya Fushinobu and Prof. Takane Katayama. My reseach interests are new enzymes from Human gut microbiota.<br />
<br />
----<br />
<br />
<biblio><br />
#chihaya2017 pmid=28392148<br />
#Michael2020 pmid=32620774<br />
<br />
</biblio><br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Yamada,Chihaya]]</div>Chihaya Yamadahttps://www.cazypedia.org/index.php?title=User:Chihaya_Yamada&diff=15737User:Chihaya Yamada2020-08-10T14:49:59Z<p>Chihaya Yamada: </p>
<hr />
<div>[[Image:Blank_user-200px.png|200px|right]]<br />
[[File:chihaya.jpg]]<br />
Chihaya Yamada is an assistant professor at Laboratory of Enzymology in Department of Biotechnology, Graduate School of Agricultural and Life Sciences, The University of Tokyo located in Tokyo, Japan. I obtained Ph.D degree in Department of Biotechnology, The University of Tokyo in 2013. I contributed to structure analysis of lacto-''N''-biosidase (LnbX) from ''Bifidobacterium longum'' subsp. ''longum'' belonging to [[GH136]] with Prof. Shinya Fushinobu and Prof. Takane Katayama. My reseach interests are new enzymes from Human gut microbiota.<br />
<br />
----<br />
<br />
<biblio><br />
#chihaya2017 pmid=28392148<br />
#Michael2020 pmid=32620774<br />
<br />
</biblio><br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Yamada,Chihaya]]</div>Chihaya Yamadahttps://www.cazypedia.org/index.php?title=User:Chihaya_Yamada&diff=15736User:Chihaya Yamada2020-08-10T14:48:55Z<p>Chihaya Yamada: </p>
<hr />
<div>[[Image:Blank_user-200px.png|200px|right]]<br />
<br />
<br />
<br />
Chihaya Yamada is an assistant professor at Laboratory of Enzymology in Department of Biotechnology, Graduate School of Agricultural and Life Sciences, The University of Tokyo located in Tokyo, Japan. I obtained Ph.D degree in Department of Biotechnology, The University of Tokyo in 2013. I contributed to structure analysis of lacto-''N''-biosidase (LnbX) from ''Bifidobacterium longum'' subsp. ''longum'' belonging to [[GH136]] with Prof. Shinya Fushinobu and Prof. Takane Katayama. My reseach interests are new enzymes from Human gut microbiota.<br />
<br />
----<br />
<br />
<biblio><br />
#chihaya2017 pmid=28392148<br />
#Michael2020 pmid=32620774<br />
<br />
</biblio><br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Yamada,Chihaya]]</div>Chihaya Yamadahttps://www.cazypedia.org/index.php?title=User:Chihaya_Yamada&diff=15735User:Chihaya Yamada2020-08-10T14:48:29Z<p>Chihaya Yamada: </p>
<hr />
<div>[[Image:Blank_user-200px.png|200px|right]]<br />
<br />
<br />
<br />
Chihaya Yamada is an assistant professor at Laboratory of Enzymology in Department of Biotechnology, Graduate School of Agricultural and Life Sciences, The University of Tokyo located in Tokyo, Japan. I obtained Ph.D degree in Department of Biotechnology, The University of Tokyo in 2013. I contributed to structure analysis of lacto-''N''-biosidase (LnbX) from ''Bifidobacterium longum'' subsp. ''longum'' belonging to [[GH136]] with Prof. ^^^Shinya Fushinobu^^^and Prof. [[USER:Takane Katayama]]. My reseach interests are new enzymes from Human gut microbiota.<br />
<br />
----<br />
<br />
<biblio><br />
#chihaya2017 pmid=28392148<br />
#Michael2020 pmid=32620774<br />
<br />
</biblio><br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Yamada,Chihaya]]</div>Chihaya Yamadahttps://www.cazypedia.org/index.php?title=User:Chihaya_Yamada&diff=15734User:Chihaya Yamada2020-08-10T14:44:48Z<p>Chihaya Yamada: </p>
<hr />
<div>[[Image:Blank_user-200px.png|200px|right]]<br />
<br />
<br />
<br />
Chihaya Yamada is an assistant professor at Laboratory of Enzymology in Department of Biotechnology, Graduate School of Agricultural and Life Sciences, The University of Tokyo located in Tokyo, Japan. I obtained Ph.D degree in Department of Biotechnology, The University of Tokyo in 2013. I contributed to structure analysis of lacto-''N''-biosidase (LnbX) from ''Bifidobacterium longum'' subsp. ''longum'' belonging to [[GH136]] with Prof. [[USER:Shinya Fushinobu]] and Prof. [[USER:Takane Katayama]]. My reseach interests are new enzymes from Human gut microbiota.<br />
<br />
----<br />
<br />
<biblio><br />
#chihaya2017 pmid=28392148<br />
#Michael2020 pmid=32620774<br />
<br />
</biblio><br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Yamada,Chihaya]]</div>Chihaya Yamadahttps://www.cazypedia.org/index.php?title=User:Chihaya_Yamada&diff=15733User:Chihaya Yamada2020-08-10T14:34:55Z<p>Chihaya Yamada: </p>
<hr />
<div>[[Image:Blank_user-200px.png|200px|right]]<br />
<br />
Chihaya Yamada is an assistant professor at Laboratory of Enzymology in Department of Biotechnology, Graduate School of Agricultural and Life Sciences, The University of Tokyo located in Tokyo, Japan. I obtained Ph.D degree in Department of Biotechnology, The University of Tokyo in 2013. I contributed to structure analysis of lacto-''N''-biosidase (LnbX) from ''Bifidobacterium longum'' subsp. ''longum'' belonging to [[GH136]] with Prof. [[USER:Shinya Fushinobu]] and Prof. [[USER:Takane Katayama]]. My reseach interests are new enzymes from Human gut microbiota.<br />
<br />
----<br />
<br />
<biblio><br />
#chihaya2017 pmid=28392148<br />
#Michael2020 pmid=32620774<br />
<br />
</biblio><br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Yamada,Chihaya]]</div>Chihaya Yamadahttps://www.cazypedia.org/index.php?title=User:Chihaya_Yamada&diff=15732User:Chihaya Yamada2020-08-10T14:34:38Z<p>Chihaya Yamada: </p>
<hr />
<div>[[Image:Blank_user-200px.png|200px|right]]<br />
[[File:IMG-1180.jpg]]<br />
<br />
Chihaya Yamada is an assistant professor at Laboratory of Enzymology in Department of Biotechnology, Graduate School of Agricultural and Life Sciences, The University of Tokyo located in Tokyo, Japan. I obtained Ph.D degree in Department of Biotechnology, The University of Tokyo in 2013. I contributed to structure analysis of lacto-''N''-biosidase (LnbX) from ''Bifidobacterium longum'' subsp. ''longum'' belonging to [[GH136]] with Prof. [[USER:Shinya Fushinobu]] and Prof. [[USER:Takane Katayama]]. My reseach interests are new enzymes from Human gut microbiota.<br />
<br />
----<br />
<br />
<biblio><br />
#chihaya2017 pmid=28392148<br />
#Michael2020 pmid=32620774<br />
<br />
</biblio><br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Yamada,Chihaya]]</div>Chihaya Yamadahttps://www.cazypedia.org/index.php?title=User:Chihaya_Yamada&diff=15731User:Chihaya Yamada2020-08-10T14:33:38Z<p>Chihaya Yamada: </p>
<hr />
<div>[[Image:Blank_user-200px.png|200px|right]]<br />
<br />
<br />
Chihaya Yamada is an assistant professor at Laboratory of Enzymology in Department of Biotechnology, Graduate School of Agricultural and Life Sciences, The University of Tokyo located in Tokyo, Japan. I obtained Ph.D degree in Department of Biotechnology, The University of Tokyo in 2013. I contributed to structure analysis of lacto-''N''-biosidase (LnbX) from ''Bifidobacterium longum'' subsp. ''longum'' belonging to [[GH136]] with Prof. [[USER:Shinya Fushinobu]] and Prof. [[USER:Takane Katayama]]. My reseach interests are new enzymes from Human gut microbiota.<br />
<br />
----<br />
<br />
<biblio><br />
#chihaya2017 pmid=28392148<br />
#Michael2020 pmid=32620774<br />
<br />
</biblio><br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Yamada,Chihaya]]</div>Chihaya Yamada