https://www.cazypedia.org/api.php?action=feedcontributions&feedformat=atom&user=Jean-Guy+BerrinCAZypedia - User contributions [en-ca]2026-05-05T06:48:22ZUser contributionsMediaWiki 1.35.10https://www.cazypedia.org/index.php?title=Auxiliary_Activity_Family_14&diff=14347Auxiliary Activity Family 142019-11-04T07:39:03Z<p>Jean-Guy Berrin: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{CuratorApproved}}<br />
* [[Author]]: ^^^Marie Couturier^^^ and ^^^Jean-Guy Berrin^^^<br />
* [[Responsible Curator]]: ^^^Jean-Guy Berrin^^^<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" |'''Auxiliary Activity Family AA14'''<br />
|-<br />
|'''Clan''' <br />
|Structurally related to [[AA9]]<br />
|-<br />
|'''Mechanism'''<br />
|lytic oxidase<br />
|-<br />
|'''Active site residues'''<br />
|mononuclear copper ion<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}AA14.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Discovery of AA14 LPMOs ==<br />
<br />
The gene encoding the first AA14 family member was identified by analysing transcriptomic and proteomic data from the white-rot basidiomycete ''Pycnoporus coccineus'' <cite>Couturier2015</cite>. This gene was highly upregulated when the fungus was grown on pine or poplar. The corresponding protein (GenBank ID [https://www.ncbi.nlm.nih.gov/nuccore/KY769370 KY769370]) was secreted only during growth on pine and poplar, suggesting a role in wood decay. AA14 modules never occur with CBMs, [[carbohydrate-binding modules]] which explains why the family could not be discovered by the module-walking approach, as were [[AA11]] and [[AA13]].<br />
<br />
== Substrate specificities ==<br />
<br />
The only two AA14 characterized so far were tested for copper-dependent oxidase activity on a range of polysaccharides. No activity could be detected on any substrate tested, including cellulose and xylans. However, addition of either of the AA14 enzymes to a ''Trichoderma reesei'' cocktail mainly composed of cellulases and xylanases led to a boost of glucose release from poplar and pine . This improvement in glucose release was dose dependent, yielding up to ~100% increase on pretreated softwood. AA14 enzymes also showed synergystic action on wood with [[AA9]] LPMOs. Finally, activity was detected on xylan adsorbed onto cellulose chains, using solid state 13C CP/MAS NMR and mass spectrometry. The observed products were C1-oxidized species with an aldonic acid at the reducing end.<br />
<br />
== Kinetics and Mechanism ==<br />
<br />
As all LPMOs, AA14s are copper-dependent mono-oxygenases and accordingly, mass spectrometry analyses revealed that PcAA14A and PcAA14B contained ∼1 copper atom per protein molecule. Additionally, RPE analysis revealed spin-Hamiltonian parameters similar to those obtained for AA9 LPMOs, confirming the presence of the copper(II) ion within the histidine brace coordination environment. However, as for the other LPMOs, the chemical mechanism by which the enzymes perform the reaction is still a matter of debate <cite>Hedegard2018,Bertini2018,Bissaro2017</cite>. Although the natural electron donor for AA14s is unknown, PcAA14A and PcAA14B were both able to produce hydrogen peroxide in the presence of ascorbate, cysteine or gallate as electron donors. They were also active on micronized wood without addition of electron donor, suggesting that wood components such as lignin may act as electron donors <cite>Westereng2015</cite>. N-terminal histidine in AA14s is methylated in vivo as seen for all other fungal LPMOs, but the effect on the reaction performed by the enzyme is not established yet. <br />
<br />
== Catalytic and other important Residues ==<br />
AA14s exhibit the canonical LPMO histidine brace coordinating the copper ion, which is exposed at the surface. In PcAA14B this histidine brace is constituted by His1, His99 and Tyr176. Interestingly, PcAA14B possesses an equally conserved tyrosine residue, Tyr240, at the edge of the substrate-binding surface, albeit located on a different loop region, which could potentially make substrate interactions. This tyrosine residue is also conserved in AA9 LPMOs <cite>Frandsen2016</cite> <br />
<br />
== Three-dimensional structures ==<br />
The structure of PcAA14B was solved by multiple-wavelength anomalous dispersion data recorded at the gadolinium edge, and refined at 3.0 Å resolution <cite>Couturier2018</cite>. The core of PcAA14B structure folds into a largely antiparallel immunoglobulin-like β-sandwich, a fold globally similar to those seen in LPMOs from other families <cite>Tandrup2018</cite>. However, in contrast to the flat substrate-binding surfaces observed in AA9 LPMOs, the surface of PcAA14B has a rippled shape with a clamp formed by two prominent surface loops located at the N-terminal half of the enzyme. It is interesting to note that these loops are equivalent to the L2 and L3 loop regions in AA9 LPMOs which have been shown to be involved in LPMO-substrate interactions <cite>Vaaje-Kolstadt2017</cite>. <br />
<br />
== Family Firsts ==<br />
;First family member identified: AA14 from ''Pycnoporus coccineus'' <cite>Couturier2018</cite>.<br />
;First demonstration of oxidative cleavage: ''Pc''AA114A and ''Pc''AA114AB were shown to oxidatively cleave xylan chains bound to cellulose <cite>Couturier2018</cite>.<br />
;First 3-D structure: ''Pc''AA14B from ''P. coccineus'' [{{PDBlink}}5no7 5NO7] <cite>Couturier2018</cite><br />
<br />
== References ==<br />
<biblio><br />
#Couturier2015 pmid=26692083<br />
#Couturier2018 pmid=29377002<br />
#Bissaro2017 pmid=28846668<br />
#Westereng2015 pmid=26686263<br />
#Tandrup2018 pmid=30381341<br />
#Frandsen2016 pmid=26928935<br />
#Vaaje-Kolstadt2017 pmid=28086105<br />
#Hedegard2018 pmid=29780519<br />
#Bertini2018 pmid=29232119<br />
</biblio><br />
<br />
[[Category:Auxiliary Activity Families|AA014]]</div>Jean-Guy Berrinhttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_131&diff=8839Glycoside Hydrolase Family 1312013-06-26T16:30:59Z<p>Jean-Guy Berrin: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{CuratorApproved}}<br />
* [[Author]]: ^^^Jean-Guy Berrin^^^<br />
* [[Responsible Curator]]: ^^^Jean-Guy Berrin^^^<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 GH131'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|not known<br />
|-<br />
|'''Active site residues'''<br />
|not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH131.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
This family of [[glycoside hydrolases]] comprises only enzymes of fungal origin. Several of these enzymes contain predicted cellulose-binding modules from family [{{CAZyDBlink}}CBM1.html CBM1]. Only one member (gene Pa_3_10940) has been characterized to date from the coprophilic ascomycete ''Podospora anserina'' <cite>Lafond2012</cite>. This first member is a broad specificity β-glucanase with exo-β-1,3/1,6- and endo-β-1,4-glucanase activity <cite>Lafond2012</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
The ''Podospora anserina'' GH131 beta-glucanase displays activity towards a broad range of β-glucan polysaccharides including laminarin, curdlan, pachyman, lichenan, pustulan and also cellulosic derivatives <cite>Lafond2012</cite>. Analysis of the products released from polysaccharides revealed that this β-glucanase is an exo-acting enzyme on β-(1,3)- and β-(1,6)-linked glucan substrates and an endo-acting enzyme on β-(1,4)-linked glucan substrates. Hydrolysis of short β-(1,3), β-(1,4) and β-(1,3)/β-(1,4) gluco-oligosaccharides confirmed this striking feature and revealed that the enzyme acted in an ''exo''-mode on the non-reducing end of gluco-oligosaccharides.<br />
<br />
== Catalytic Residues ==<br />
Not known.<br />
<br />
== Three-dimensional structures ==<br />
Only one crystal structure of a glycoside hydrolase family 131 protein from ''Coprinopsis cinerea'' is available <cite>Miyazaki2013</cite>. The structure of CcGH131A was found to be composed of a β-jelly roll fold.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: No experimental proof.<br />
;First catalytic nucleophile identification: No experimental proof.<br />
;First general acid/base residue identification: No experimental proof.<br />
;First 3-D structure: ''Coprinopsis cinerea'' CcGH131A <cite>Miyazaki2013</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Lafond2012 pmid=23023747<br />
#Miyazaki2013 pmid=23711369<br />
</biblio><br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH131]]</div>Jean-Guy Berrinhttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_131&diff=8838Glycoside Hydrolase Family 1312013-06-26T16:29:28Z<p>Jean-Guy Berrin: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{CuratorApproved}}<br />
* [[Author]]: ^^^Jean-Guy Berrin^^^<br />
* [[Responsible Curator]]: ^^^Jean-Guy Berrin^^^<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 GH131'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|not known<br />
|-<br />
|'''Active site residues'''<br />
|not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH131.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
This family of [[glycoside hydrolases]] comprises only enzymes of fungal origin. Several of these enzymes contain predicted cellulose-binding modules from family [{{CAZyDBlink}}CBM1.html CBM1]. Only one member (gene Pa_3_10940) has been characterized to date from the coprophilic ascomycete ''Podospora anserina'' <cite>Lafond2012</cite>. This first member is a broad specificity β-glucanase with exo-β-1,3/1,6- and endo-β-1,4-glucanase activity <cite>Lafond2012</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
The ''Podospora anserina'' GH131 beta-glucanase displays activity towards a broad range of β-glucan polysaccharides including laminarin, curdlan, pachyman, lichenan, pustulan and also cellulosic derivatives <cite>Lafond2012</cite>. Analysis of the products released from polysaccharides revealed that this β-glucanase is an exo-acting enzyme on β-(1,3)- and β-(1,6)-linked glucan substrates and an endo-acting enzyme on β-(1,4)-linked glucan substrates. Hydrolysis of short β-(1,3), β-(1,4) and β-(1,3)/β-(1,4) gluco-oligosaccharides confirmed this striking feature and revealed that the enzyme acted in an ''exo''-mode on the non-reducing end of gluco-oligosaccharides.<br />
<br />
== Catalytic Residues ==<br />
Not known.<br />
<br />
== Three-dimensional structures ==<br />
Only one crystal structure of a glycoside hydrolase family 131 protein from ''Coprinopsis cinerea'' is available <cite>Miyazaki2013</cite>. The structure of CcGH131A was found to be composed of a β-jelly roll fold and mainly consisted of two β-sheets, sheet-A and sheet-B.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: No experimental proof.<br />
;First catalytic nucleophile identification: No experimental proof.<br />
;First general acid/base residue identification: No experimental proof.<br />
;First 3-D structure: ''Coprinopsis cinerea'' CcGH131A <cite>Miyazaki2013</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Lafond2012 pmid=23023747<br />
#Miyazaki2013 pmid=23711369<br />
</biblio><br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH131]]</div>Jean-Guy Berrinhttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_131&diff=8837Glycoside Hydrolase Family 1312013-06-26T15:17:50Z<p>Jean-Guy Berrin: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{CuratorApproved}}<br />
* [[Author]]: ^^^Jean-Guy Berrin^^^<br />
* [[Responsible Curator]]: ^^^Jean-Guy Berrin^^^<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 GH131'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|not known<br />
|-<br />
|'''Active site residues'''<br />
|not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH131.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
This family of [[glycoside hydrolases]] comprises only enzymes of fungal origin. Several of these enzymes contain predicted cellulose-binding modules from family [{{CAZyDBlink}}CBM1.html CBM1]. Only one member (gene Pa_3_10940) has been characterized to date from the coprophilic ascomycete ''Podospora anserina'' <cite>Lafond2012</cite>. This first member is a broad specificity β-glucanase with exo-β-1,3/1,6- and endo-β-1,4-glucanase activity <cite>Lafond2012</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
The ''Podospora anserina'' GH131 beta-glucanase displays activity towards a broad range of β-glucan polysaccharides including laminarin, curdlan, pachyman, lichenan, pustulan and also cellulosic derivatives <cite>Lafond2012</cite>. Analysis of the products released from polysaccharides revealed that this β-glucanase is an exo-acting enzyme on β-(1,3)- and β-(1,6)-linked glucan substrates and an endo-acting enzyme on β-(1,4)-linked glucan substrates. Hydrolysis of short β-(1,3), β-(1,4) and β-(1,3)/β-(1,4) gluco-oligosaccharides confirmed this striking feature and revealed that the enzyme acted in an ''exo''-mode on the non-reducing end of gluco-oligosaccharides.<br />
<br />
== Catalytic Residues ==<br />
Not known.<br />
<br />
== Three-dimensional structures ==<br />
Only one crystal structure of a glycoside hydrolase family 131 protein from ''Coprinopsis cinerea'' is available <cite>Miyazaki2013</cite>. The structure of CcGH131A was found to be composed of a β-jelly roll fold and mainly consisted of two β-sheets, sheet-A and sheet-B. Arg96, Glu98, Glu138, and His218 are likely to be catalytically critical residues and it was suggested that the catalytic mechanism of CcGH131A is different from that of typical glycosidases <cite>Miyazaki2013</cite>.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: No experimental proof.<br />
;First catalytic nucleophile identification: No experimental proof.<br />
;First general acid/base residue identification: No experimental proof.<br />
;First 3-D structure: ''Coprinopsis cinerea'' CcGH131A <cite>Miyazaki2013</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Lafond2012 pmid=23023747<br />
#Miyazaki2013 pmid=23711369<br />
</biblio><br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH131]]</div>Jean-Guy Berrinhttps://www.cazypedia.org/index.php?title=User:Jean-Guy_Berrin&diff=8148User:Jean-Guy Berrin2013-01-20T10:33:56Z<p>Jean-Guy Berrin: </p>
<hr />
<div>[[Image:berrin.jpg|200px|right]] This is the user page of '''Jean-Guy Berrin'''. I started working on carbohydrate-active enzymes during my Master studies focusing on the characterization of a fungal [[GH11]] xylanase from ''Aspergillus niger'' <cite>Berrin2000</cite>. During my PhD held at the Institute of Food Research Norwich (UK) under the supervision of Nathalie Juge, I investigated the role of the human beta-glucosidase ([[GH1]]) in the metabolism of flavonoid glycosides through the study of its structure-activity relationships <cite>Tribolo2007 Berrin2003</cite>. After my PhD, I went back to France at the CEA (French Alternative Energies and Atomic Energy Commission) for a post doc on NADH oxidases followed by a post doc at Aix Marseille University on the characterization of fungal [[GH11]] xylanases for food applications (see for example <cite>AndreLeroux2008</cite> and reviews <cite>BerrinJuge2009 Paes2012</cite>). In 2008, I obtained a permanent research scientist position at INRA (Franch National Institute for Agricultural Research, Biotechnology of Filamentous Fungi group, Marseille, France). My main interest is to explore the enzymatic potential of the INRA collection of filamentous fungi (CIRM) to improve plant biomass deconstruction <cite>Couturier2012 Berrin2012</cite>. A large number of genes have been targeted by computational genome analysis and secretomic approaches leading to the characterization of CAZymes from [[GH5]], [[GH6]], [[GH11]], [[GH26]], [[GH45]], [[GH51]], [[GH62]] (see for example <cite>Couturier2011</cite>). I also characterized the first member of the [[GH131]] family <cite>Lafond2012</cite>. More information at [https://www.researchgate.net/profile/Jean-Guy_Berrin/ ResearchGate].<br />
<br />
<br />
<br />
----<br />
<biblio><br />
#AndreLeroux2008 pmid=18384043<br />
#Berrin2000 pmid=10833405<br />
#Berrin2003 pmid=12667141<br />
#Berrin2012 pmid=22773628<br />
#BerrinJuge2009 pmid=18320143<br />
#Paes2012 pmid=22067746<br />
#Couturier2011 pmid=21037302<br />
#Couturier2012 pmid=22300648<br />
#Lafond2012 pmid=23023747<br />
#Tribolo2007 pmid=17555766<br />
</biblio><br />
<br />
[[Category:Contributors|Berrin, Jean-Guy]]</div>Jean-Guy Berrinhttps://www.cazypedia.org/index.php?title=File:Berrin.jpg&diff=8147File:Berrin.jpg2013-01-20T10:07:33Z<p>Jean-Guy Berrin: </p>
<hr />
<div></div>Jean-Guy Berrinhttps://www.cazypedia.org/index.php?title=User:Jean-Guy_Berrin&diff=8146User:Jean-Guy Berrin2013-01-20T10:04:03Z<p>Jean-Guy Berrin: </p>
<hr />
<div>[[Image:berrin.jpg|200px|right]] This is the user page of '''Jean-Guy Berrin'''. I started working on carbohydrate-active enzymes during my Master studies focusing on the characterization of a fungal [[GH11]] xylanase from ''Aspergillus niger'' <cite>Berrin2000</cite>. During my PhD held at the Institute of Food Research Norwich (UK) under the supervision of Nathalie Juge, I investigated the role of the human beta-glucosidase ([[GH1]]) in the metabolism of flavonoid glycosides through the study of its structure-activity relationships <cite>Tribolo2007 Berrin2003</cite>. After my PhD, I went back to France at the CEA (French Alternative Energies and Atomic Energy Commission) for a post doc on NADH oxidases followed by a post doc at Aix Marseille University on the characterization of fungal [[GH11]] xylanases for food applications (see for example <cite>AndreLeroux2008</cite> and reviews <cite>BerrinJuge2009 Paes2012</cite>). In 2008, I obtained a permanent research scientist position at INRA (Franch National Institute for Agricultural Research, Biotechnology of Filamentous Fungi group, Marseille, France). My main interest is to explore the enzymatic potential of the INRA collection of filamentous fungi (CIRM) to improve plant biomass deconstruction <cite>Couturier2012 Berrin2012</cite>. A large number of genes have been targeted by computational genome analysis and secretomic approaches leading to the characterization of CAZymes from [[GH5]], [[GH6]], [[GH11]], [[GH26]], [[GH45]], [[GH51]], [[GH62]] (see for example <cite>Couturier2011</cite>). I also characterized the first member of the [[GH131]] family <cite>Lafond2012</cite>.<br />
<br />
<br />
<br />
----<br />
<biblio><br />
#AndreLeroux2008 pmid=18384043<br />
#Berrin2000 pmid=10833405<br />
#Berrin2003 pmid=12667141<br />
#Berrin2012 pmid=22773628<br />
#BerrinJuge2009 pmid=18320143<br />
#Paes2012 pmid=22067746<br />
#Couturier2011 pmid=21037302<br />
#Couturier2012 pmid=22300648<br />
#Lafond2012 pmid=23023747<br />
#Tribolo2007 pmid=17555766<br />
</biblio><br />
<br />
[[Category:Contributors|Berrin, Jean-Guy]]</div>Jean-Guy Berrinhttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_131&diff=7655Glycoside Hydrolase Family 1312012-10-25T16:25:56Z<p>Jean-Guy Berrin: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{CuratorApproved}}<br />
* [[Author]]: ^^^Jean-Guy Berrin^^^<br />
* [[Responsible Curator]]: ^^^Jean-Guy Berrin^^^<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 GH131'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|not known<br />
|-<br />
|'''Active site residues'''<br />
|not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH131.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
This family of [[glycoside hydrolases]] comprises only enzymes of fungal origin. Several of these enzymes contain cellulose-binding CBMs from family 1. Only one member (gene Pa_3_10940) has been characterized to date from the coprophilic ascomycete ''Podospora anserina'' <cite>Lafond2012</cite>. This first member is a broad specificity β-glucanase with exo-β-1,3/1,6- and endo-β-1,4-glucanase activity <cite>Lafond2012</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
The ''Podospora anserina'' GH131 beta-glucanase displays activity towards a broad range of β-glucan polysaccharides including laminarin, curdlan, pachyman, lichenan, pustulan and also cellulosic derivatives <cite>Lafond2012</cite>. Analysis of the products released from polysaccharides revealed that this β-glucanase is an exo-acting enzyme on β-(1,3)- and β-(1,6)-linked glucan substrates and an endo-acting enzyme on β-(1,4)-linked glucan substrates. Hydrolysis of short β-(1,3), β-(1,4) and β-(1,3)/β-(1,4) gluco-oligosaccharides confirmed this striking feature and revealed that the enzyme was performing in an exo-mode on the non-reducing end of gluco-oligosaccharides.<br />
<br />
== Catalytic Residues ==<br />
Not known.<br />
<br />
== Three-dimensional structures ==<br />
Not known.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: No experimental proof.<br />
;First catalytic nucleophile identification: No experimental proof.<br />
;First general acid/base residue identification: No experimental proof.<br />
;First 3-D structure: Not known.<br />
<br />
== References ==<br />
<biblio><br />
#Lafond2012 pmid=23023747<br />
</biblio><br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH131]]</div>Jean-Guy Berrinhttps://www.cazypedia.org/index.php?title=User:Jean-Guy_Berrin&diff=7654User:Jean-Guy Berrin2012-10-25T15:54:16Z<p>Jean-Guy Berrin: </p>
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<div>This is the user page of '''Jean-Guy Berrin'''. I started working on carbohydrate-active enzymes during my Master studies focusing on the characterization of a fungal [[GH11]] xylanase from ''Aspergillus niger'' (<cite>Berrin2000</cite>). During my PhD held at the Institute of Food Research Norwich (UK) under the supervision of Nathalie Juge, I investigated the role of the human beta-glucosidase ([[GH1]]) in the metabolism of flavonoid glycosides through the study of its structure-activity relationships (<cite>Tribolo2007 Berrin2003</cite>). After my PhD, I went back to France at the CEA (French Alternative Energies and Atomic Energy Commission) for a post doc on NADH oxidases followed by a post doc at Aix Marseille University on the characterization of fungal [[GH11]] xylanases for food applications (see for example <cite>AndreLeroux2008</cite> and reviews <cite>BerrinJuge2009 Paes2012</cite>). In 2008, I obtained a permanent research scientist position at INRA (Franch National Institute for Agricultural Research, Biotechnology of Filamentous Fungi group, Marseille, France). My main interest is to explore the enzymatic potential of the INRA collection of filamentous fungi (CIRM) to improve plant biomass deconstruction (<cite>Couturier2012 Berrin 2012</cite>). A large number of genes have been targeted by computational genome analysis and secretomic approaches leading to the characterization of CAZymes from [[GH5]], [[GH6]], [[GH11]], [[GH26]], [[GH45]], [[GH51]], [[GH62]] (see for example <cite>Couturier2011</cite>). I also characterized the first member of the [[GH131]] family (<cite>Lafond2012</cite>).<br />
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[[Category:Contributors|Berrin, Jean-Guy]]<br />
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<biblio><br />
#AndreLeroux2008 pmid=18384043<br />
#Berrin2000 pmid=10833405<br />
#Berrin2003 pmid=12667141<br />
#Berrin2012 pmid=22773628<br />
#BerrinJuge2009 pmid=18320143<br />
#Paes2012 pmid=22067746<br />
#Couturier2011 pmid=21037302<br />
#Couturier2012 pmid=22300648<br />
#Lafond2012 pmid=23023747<br />
#Tribolo2007 pmid=17555766</div>Jean-Guy Berrinhttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_131&diff=7551Glycoside Hydrolase Family 1312012-10-16T07:28:59Z<p>Jean-Guy Berrin: </p>
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<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: ^^^Jean-Guy Berrin^^^<br />
* [[Responsible Curator]]: ^^^Jean-Guy Berrin^^^<br />
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<!-- 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 GH131'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|not known<br />
|-<br />
|'''Active site residues'''<br />
|not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH131.html<br />
|}<br />
</div><br />
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== Substrate specificities ==<br />
Content is to be added here. In the meantime, please see these references for an essential introduction to the CAZy classification system: <cite>DaviesSinnott2008 Cantarel2009</cite>. This paper describes the creation of GH131 <cite>Lafond2012</cite><br />
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== Kinetics and Mechanism ==<br />
Content is to be added here.<br />
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== Catalytic Residues ==<br />
Content is to be added here.<br />
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== Three-dimensional structures ==<br />
Content is to be added here.<br />
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== 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 />
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== References ==<br />
<biblio><br />
#Lafond2012 pmid=23023747<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. Biochem. J. (BJ Classic Paper, online only). [http://dx.doi.org/10.1042/BJ20080382 DOI: 10.1042/BJ20080382]<br />
</biblio><br />
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[[Category:Glycoside Hydrolase Families|GH131]]</div>Jean-Guy Berrinhttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_131&diff=7550Glycoside Hydrolase Family 1312012-10-16T07:25:44Z<p>Jean-Guy Berrin: </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]]: ^^^Jean-Guy Berrin^^^<br />
* [[Responsible Curator]]: ^^^Jean-Guy Berrin^^^<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 GH131'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|retaining/inverting<br />
|-<br />
|'''Active site residues'''<br />
|known/not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH131.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Content is to be added here. In the meantime, please see these references for an essential introduction to the CAZy classification system: <cite>DaviesSinnott2008 Cantarel2009</cite>. This paper describes the creation of GH131 <cite>Lafond2012</cite><br />
<br />
== Kinetics and Mechanism ==<br />
Content is to be added here.<br />
<br />
== Catalytic Residues ==<br />
Content is to be added here.<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 />
#Lafond2012 pmid=23023747<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. Biochem. J. (BJ Classic Paper, online only). [http://dx.doi.org/10.1042/BJ20080382 DOI: 10.1042/BJ20080382]<br />
</biblio><br />
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[[Category:Glycoside Hydrolase Families|GH131]]</div>Jean-Guy Berrinhttps://www.cazypedia.org/index.php?title=User:Jean-Guy_Berrin&diff=7549User:Jean-Guy Berrin2012-10-16T07:16:47Z<p>Jean-Guy Berrin: </p>
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<div>Hi. This in Jean-Guy's page.<br />
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[[Category:Contributors|Berrin,Jean-Guy]]</div>Jean-Guy Berrinhttps://www.cazypedia.org/index.php?title=User:Jean-Guy_Berrin&diff=7548User:Jean-Guy Berrin2012-10-16T07:16:27Z<p>Jean-Guy Berrin: Created page with "Hi. Berrin,Jean-Guy"</p>
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<div>Hi. <br />
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[[Category:Contributors|Berrin,Jean-Guy]]</div>Jean-Guy Berrin