https://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_15&feed=atom&action=history
Carbohydrate Esterase Family 15 - Revision history
2024-03-28T21:08:53Z
Revision history for this page on the wiki
MediaWiki 1.35.10
https://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_15&diff=17472&oldid=prev
Harry Brumer at 15:42, 16 August 2023
2023-08-16T15:42:28Z
<p></p>
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<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Family Firsts ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Family Firsts ==</div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>;First 3-D structure: The first solved structure of a CE15 enzyme was the Cip2 catalytic domain from ''Trichoderma reesei'' (''Tr''GE) <cite>Pokkuluri2011</cite>. </div></td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>;First 3-D structure: The first solved structure of a CE15 enzyme was the Cip2 catalytic domain from ''Trichoderma reesei'' (''Tr''GE<ins class="diffchange diffchange-inline">; PDB [{{PDBlink}}3pic 3pic]</ins>) <cite>Pokkuluri2011</cite>. </div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>;First mechanistic insight: The crystal structure of ''St''GE2 (from ''Sporotrichum thermophile'') in complex with the ligand 4-''O''-methyl-beta-D-glucopyranuronate gave the first direct insight into substrate binding <cite>Charavgi2013</cite>.</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>;First mechanistic insight: The crystal structure of ''St''GE2 (from ''Sporotrichum thermophile'') in complex with the ligand 4-''O''-methyl-beta-D-glucopyranuronate gave the first direct insight into substrate binding <cite>Charavgi2013</cite>.</div></td></tr>
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Harry Brumer
https://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_15&diff=17471&oldid=prev
Harry Brumer at 15:40, 16 August 2023
2023-08-16T15:40:50Z
<p></p>
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<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Substrate specificity ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Substrate specificity ==</div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>All CE15 enzymes characterized to date are glucuronoyl esterases (EC <del class="diffchange diffchange-inline">number </del>[{{EClink}}3.1.1.117 3.1.1.117]), cleaving esters of D-glucuronic acid. The first reported glucuronoyl esterase was ''Sc''GE1 from the white-rot fungus ''Schizophyllum commune'', and the activity was demonstrated by TLC on a methyl ester of 4-''O''-methyl-D-glucuronic acid <cite>Spanikova2006</cite>. While CE15 members are found in both fungal and bacterial species, several bacterial CE15 enzymes are more promiscuous than their fungal counterparts and are active also on esters of galacturonoate <cite>Arnlingbaath2018</cite>. Feruloyl- and acetyl esterase activities have been reported for certain CE15 enzymes as side activities <cite>Desanti2016 Mosbech2018</cite>. The proposed physiological role of CE15 enzymes is to hydrolyze lignin-carbohydrate ester linkages between lignin and glucuronoxylan in plant cell walls, and a few studies have demonstrated their activity on lignocellulose-derived materials and plant biomass <cite>Derrico2016 Arnlingbaath2016 Mosbech2018 </cite>.</div></td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>All CE15 enzymes characterized to date are glucuronoyl esterases (EC [{{EClink}}3.1.1.117 3.1.1.117]), cleaving esters of D-glucuronic acid. The first reported glucuronoyl esterase was ''Sc''GE1 from the white-rot fungus ''Schizophyllum commune'', and the activity was demonstrated by TLC on a methyl ester of 4-''O''-methyl-D-glucuronic acid <cite>Spanikova2006</cite>. While CE15 members are found in both fungal and bacterial species, several bacterial CE15 enzymes are more promiscuous than their fungal counterparts and are active also on esters of galacturonoate <cite>Arnlingbaath2018</cite>. Feruloyl- and acetyl esterase activities have been reported for certain CE15 enzymes as side activities <cite>Desanti2016 Mosbech2018</cite>. The proposed physiological role of CE15 enzymes is to hydrolyze lignin-carbohydrate ester linkages between lignin and glucuronoxylan in plant cell walls, and a few studies have demonstrated their activity on lignocellulose-derived materials and plant biomass <cite>Derrico2016 Arnlingbaath2016 Mosbech2018 </cite>.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Catalytic Residues and Mechanism ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Catalytic Residues and Mechanism ==</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>All CE15 enzymes are serine-type hydrolases, containing a catalytic triad of Glu/Asp-His-Ser <cite>Pokkuluri2011 Charavgi2013 Desanti2017 Arnlingbaath2018</cite>. The position of the acidic residue of the triad is not similarly positioned in all CE15 members as the residue can be found on different loops of the conserved fold <cite>Desanti2017</cite>. A conserved arginine found in all of the CE15 structures, proximal to the catalytic triad, has been proposed to stabilize the formation of the oxyanion during catalysis <cite>Arnlingbaath2018 Mazurkewich2019 Zong2022</cite>.</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>All CE15 enzymes are serine-type hydrolases, containing a catalytic triad of Glu/Asp-His-Ser <cite>Pokkuluri2011 Charavgi2013 Desanti2017 Arnlingbaath2018</cite>. The position of the acidic residue of the triad is not similarly positioned in all CE15 members as the residue can be found on different loops of the conserved fold <cite>Desanti2017</cite>. A conserved arginine found in all of the CE15 structures, proximal to the catalytic triad, has been proposed to stabilize the formation of the oxyanion during catalysis <cite>Arnlingbaath2018 Mazurkewich2019 Zong2022</cite>.</div></td></tr>
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Harry Brumer
https://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_15&diff=17470&oldid=prev
Harry Brumer: standardized EC link
2023-08-16T15:40:23Z
<p>standardized EC link</p>
<table class="diff diff-contentalign-left diff-editfont-monospace" data-mw="interface">
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 15:40, 16 August 2023</td>
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<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Substrate specificity ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Substrate specificity ==</div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>All CE15 enzymes characterized to date are glucuronoyl esterases (EC number [<del class="diffchange diffchange-inline">https://iubmb</del>.<del class="diffchange diffchange-inline">qmul</del>.<del class="diffchange diffchange-inline">ac</del>.<del class="diffchange diffchange-inline">uk/enzyme/EC3/1/1/</del>117<del class="diffchange diffchange-inline">.html </del>3.1.1.117]), cleaving esters of D-glucuronic acid. The first reported glucuronoyl esterase was ''Sc''GE1 from the white-rot fungus ''Schizophyllum commune'', and the activity was demonstrated by TLC on a methyl ester of 4-''O''-methyl-D-glucuronic acid <cite>Spanikova2006</cite>. While CE15 members are found in both fungal and bacterial species, several bacterial CE15 enzymes are more promiscuous than their fungal counterparts and are active also on esters of galacturonoate <cite>Arnlingbaath2018</cite>. Feruloyl- and acetyl esterase activities have been reported for certain CE15 enzymes as side activities <cite>Desanti2016 Mosbech2018</cite>. The proposed physiological role of CE15 enzymes is to hydrolyze lignin-carbohydrate ester linkages between lignin and glucuronoxylan in plant cell walls, and a few studies have demonstrated their activity on lignocellulose-derived materials and plant biomass <cite>Derrico2016 Arnlingbaath2016 Mosbech2018 </cite>.</div></td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>All CE15 enzymes characterized to date are glucuronoyl esterases (EC number [<ins class="diffchange diffchange-inline">{{EClink}}3</ins>.<ins class="diffchange diffchange-inline">1</ins>.<ins class="diffchange diffchange-inline">1</ins>.117 3.1.1.117]), cleaving esters of D-glucuronic acid. The first reported glucuronoyl esterase was ''Sc''GE1 from the white-rot fungus ''Schizophyllum commune'', and the activity was demonstrated by TLC on a methyl ester of 4-''O''-methyl-D-glucuronic acid <cite>Spanikova2006</cite>. While CE15 members are found in both fungal and bacterial species, several bacterial CE15 enzymes are more promiscuous than their fungal counterparts and are active also on esters of galacturonoate <cite>Arnlingbaath2018</cite>. Feruloyl- and acetyl esterase activities have been reported for certain CE15 enzymes as side activities <cite>Desanti2016 Mosbech2018</cite>. The proposed physiological role of CE15 enzymes is to hydrolyze lignin-carbohydrate ester linkages between lignin and glucuronoxylan in plant cell walls, and a few studies have demonstrated their activity on lignocellulose-derived materials and plant biomass <cite>Derrico2016 Arnlingbaath2016 Mosbech2018 </cite>.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Catalytic Residues and Mechanism ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Catalytic Residues and Mechanism ==</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>All CE15 enzymes are serine-type hydrolases, containing a catalytic triad of Glu/Asp-His-Ser <cite>Pokkuluri2011 Charavgi2013 Desanti2017 Arnlingbaath2018</cite>. The position of the acidic residue of the triad is not similarly positioned in all CE15 members as the residue can be found on different loops of the conserved fold <cite>Desanti2017</cite>. A conserved arginine found in all of the CE15 structures, proximal to the catalytic triad, has been proposed to stabilize the formation of the oxyanion during catalysis <cite>Arnlingbaath2018 Mazurkewich2019 Zong2022</cite>.</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>All CE15 enzymes are serine-type hydrolases, containing a catalytic triad of Glu/Asp-His-Ser <cite>Pokkuluri2011 Charavgi2013 Desanti2017 Arnlingbaath2018</cite>. The position of the acidic residue of the triad is not similarly positioned in all CE15 members as the residue can be found on different loops of the conserved fold <cite>Desanti2017</cite>. A conserved arginine found in all of the CE15 structures, proximal to the catalytic triad, has been proposed to stabilize the formation of the oxyanion during catalysis <cite>Arnlingbaath2018 Mazurkewich2019 Zong2022</cite>.</div></td></tr>
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Harry Brumer
https://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_15&diff=17467&oldid=prev
Johan Larsbrink at 15:15, 16 August 2023
2023-08-16T15:15:17Z
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<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div><!-- This is the end of the table --></div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div><!-- This is the end of the table --></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>[[File: CE15_CAZypedia_Figure.png|thumb|right|400px|'''Figure 1. Comparison of structurally determined CE15 members.''' The <del class="diffchange diffchange-inline">CE15s </del>(A) ''St''GE2 from ''Thermothelomyces thermophila'' (PDB ID [{{PDBlink}}4g4j 4G4J]), (B) ''Ot''CE15A from ''Opitutus terrae'' (PDB ID [{{PDBlink}}6gs0 6GS0]), and (C) ''Tt''CE15A from ''Teredinibacter turnerae'' (PDB ID [{{PDBlink}}6hsw 6HSW]) are shown in cartoon representation. The catalytic triad in each enzyme is shown as sticks and the methyl ester of 4-''O''-methyl glucuronoate first observed in ''St''GE2 is shown in all structures as green sticks. While all CE15 members contain the alpha/beta hydrolase fold, the most prominent difference across the CE15 family observed to-date are the presence, absence, or variety of inserted regions that protrude and build-up ridges around the active site (the differently colored regions in the ''Ot''CE15A and ''Tt''CE15A). The extent to which these regions affect the enzyme’s substrate specificity has yet to be fully elucidated.]]</div></td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>[[File: CE15_CAZypedia_Figure.png|thumb|right|400px|'''Figure 1. Comparison of structurally determined CE15 members.''' The <ins class="diffchange diffchange-inline">enzymes </ins>(A) ''St''GE2 from ''Thermothelomyces thermophila'' (PDB ID [{{PDBlink}}4g4j 4G4J]), (B) ''Ot''CE15A from ''Opitutus terrae'' (PDB ID [{{PDBlink}}6gs0 6GS0]), and (C) ''Tt''CE15A from ''Teredinibacter turnerae'' (PDB ID [{{PDBlink}}6hsw 6HSW]) are shown in cartoon representation. The catalytic triad in each enzyme is shown as sticks and the methyl ester of 4-''O''-methyl glucuronoate first observed in ''St''GE2 is shown in all structures as green sticks. While all CE15 members contain the alpha/beta hydrolase fold, the most prominent difference across the CE15 family observed to-date are the presence, absence, or variety of inserted regions that protrude and build-up ridges around the active site (the differently colored regions in the ''Ot''CE15A and ''Tt''CE15A). The extent to which these regions affect the enzyme’s substrate specificity has yet to be fully elucidated.]]</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Substrate specificity ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Substrate specificity ==</div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>All CE15 enzymes characterized to<del class="diffchange diffchange-inline">-</del>date are glucuronoyl esterases, cleaving esters of D-glucuronic acid. The first reported glucuronoyl esterase was ''Sc''GE1 from the white-rot fungus ''Schizophyllum commune'', and the activity was demonstrated by TLC on a methyl ester of 4-''O''-methyl-D-glucuronic acid <cite>Spanikova2006</cite>. While CE15 members are found in both fungal and bacterial species, several bacterial CE15 enzymes are more promiscuous than their fungal counterparts and are active also on esters of galacturonoate <cite>Arnlingbaath2018</cite>. Feruloyl- and acetyl esterase activities have been reported for certain CE15 enzymes as side activities <cite>Desanti2016 Mosbech2018</cite>. The proposed physiological role of CE15 enzymes is to hydrolyze lignin-carbohydrate ester linkages between lignin and glucuronoxylan in plant cell walls, and a few studies have demonstrated their activity on lignocellulose-derived materials and plant biomass <cite>Derrico2016 Arnlingbaath2016 Mosbech2018 </cite>.</div></td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>All CE15 enzymes characterized to date are glucuronoyl esterases <ins class="diffchange diffchange-inline">(EC number [https://iubmb.qmul.ac.uk/enzyme/EC3/1/1/117.html 3.1.1.117])</ins>, cleaving esters of D-glucuronic acid. The first reported glucuronoyl esterase was ''Sc''GE1 from the white-rot fungus ''Schizophyllum commune'', and the activity was demonstrated by TLC on a methyl ester of 4-''O''-methyl-D-glucuronic acid <cite>Spanikova2006</cite>. While CE15 members are found in both fungal and bacterial species, several bacterial CE15 enzymes are more promiscuous than their fungal counterparts and are active also on esters of galacturonoate <cite>Arnlingbaath2018</cite>. Feruloyl- and acetyl esterase activities have been reported for certain CE15 enzymes as side activities <cite>Desanti2016 Mosbech2018</cite>. The proposed physiological role of CE15 enzymes is to hydrolyze lignin-carbohydrate ester linkages between lignin and glucuronoxylan in plant cell walls, and a few studies have demonstrated their activity on lignocellulose-derived materials and plant biomass <cite>Derrico2016 Arnlingbaath2016 Mosbech2018 </cite>.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Catalytic Residues and Mechanism ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Catalytic Residues and Mechanism ==</div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>All CE15 enzymes are serine-type hydrolases, containing a catalytic triad of Glu/Asp-His-Ser <cite>Pokkuluri2011 Charavgi2013 Desanti2017 Arnlingbaath2018</cite>. The position of the acidic residue of the triad is not similarly positioned in all CE15 members as the residue can be found on different loops of the conserved fold <cite>Desanti2017</cite>. A conserved arginine found in all of the CE15 structures, proximal to the catalytic triad, has been proposed to stabilize the formation of the oxyanion during catalysis <cite>Arnlingbaath2018</cite>.</div></td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>All CE15 enzymes are serine-type hydrolases, containing a catalytic triad of Glu/Asp-His-Ser <cite>Pokkuluri2011 Charavgi2013 Desanti2017 Arnlingbaath2018</cite>. The position of the acidic residue of the triad is not similarly positioned in all CE15 members as the residue can be found on different loops of the conserved fold <cite>Desanti2017</cite>. A conserved arginine found in all of the CE15 structures, proximal to the catalytic triad, has been proposed to stabilize the formation of the oxyanion during catalysis <cite>Arnlingbaath2018 <ins class="diffchange diffchange-inline">Mazurkewich2019 Zong2022</ins></cite>.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Three-dimensional structures ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Three-dimensional structures ==</div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>Representative structures of CE15 enzymes from bacterial and fungal sources have been determined, including ''Tr''GE (Cip2) from ''T. reesei'' (''Hypocrea jecorina'', PDB [{{PDBlink}}3pic 3pic]) <cite>Pokkuluri2011</cite>, ''St''GE2 from ''Thermothelomyces thermophila'' (''Sporotrichum thermophile'', PDB [{{PDBlink}}4g4g 4g4g], [{{PDBlink}}4g4i 4g4i], and [{{PDBlink}}4g4j 4g4j]) <cite>Charavgi2013</cite>, marine metagenome sequence MZ0003 (PDB [{{PDBlink}}6ehn 6ehn]) <cite>Desanti2017</cite>, ''Ot''CE15A (PDB [{{PDBlink}}6grw 6grw] and [{{PDBlink}}6gs0 6gs0]) and ''Su''CE15C (PDB [{{PDBlink}}6gry 6gry] and [{{PDBlink}}6gu8 6gu8]) <cite>Arnlingbaath2018</cite> (see the CAZy database for a [http://www.cazy.org/CE15_structure.html continuously updated list]). All structurally determined CE15 enzymes share an alpha/beta hydrolase fold, consisting of a three-layer alpha-beta-alpha sandwich with the active site in a solvent-exposed cleft. The structures of the bacterial enzymes determined thus far exhibit sizeable inserts which result in much deeper active site pockets compared to the shallow active sites seen in fungal glucuronoyl esterase structures <cite>Desanti2017 Arnlingbaath2018 </cite>.</div></td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>Representative structures of CE15 enzymes from bacterial and fungal sources have been determined, including ''Tr''GE (Cip2) from ''T. reesei'' (''Hypocrea jecorina'', PDB [{{PDBlink}}3pic 3pic]) <cite>Pokkuluri2011</cite>, ''St''GE2 from ''Thermothelomyces thermophila'' (''Sporotrichum thermophile'', PDB [{{PDBlink}}4g4g 4g4g], [{{PDBlink}}4g4i 4g4i], and [{{PDBlink}}4g4j 4g4j]) <cite>Charavgi2013</cite>, marine metagenome sequence MZ0003 (PDB [{{PDBlink}}6ehn 6ehn]) <cite>Desanti2017</cite>, ''Ot''CE15A (PDB [{{PDBlink}}6grw 6grw] and [{{PDBlink}}6gs0 6gs0]) and ''Su''CE15C (PDB [{{PDBlink}}6gry 6gry] and [{{PDBlink}}6gu8 6gu8]) <cite>Arnlingbaath2018</cite> (see the CAZy database for a [http://www.cazy.org/CE15_structure.html continuously updated list]). All structurally determined CE15 enzymes share an alpha/beta hydrolase fold, consisting of a three-layer alpha-beta-alpha sandwich with the active site in a solvent-exposed cleft. The structures of the bacterial enzymes determined thus far exhibit sizeable inserts which result in much deeper active site pockets compared to the shallow active sites seen in fungal glucuronoyl esterase structures <cite>Desanti2017 Arnlingbaath2018 </cite><ins class="diffchange diffchange-inline">. The first structures with a more complex ligand than a monosaccharide were of the bacterial ''Ot''CE15A (PDB [{{PDBlink}}6t0i 6t0i]) with a glucuronoxylooligosaccharide <cite>Mazurkewich2019</cite>, which was followed by a similar structure of the fungal ''Cu''GE from ''Cerrena unicolor'' (PDB [{{PDBlink}}6rv9 6rv9])</ins>.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Family Firsts ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Family Firsts ==</div></td></tr>
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<td colspan="2" class="diff-lineno">Line 52:</td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>#Charavgi2013 pmid=23275164</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>#Charavgi2013 pmid=23275164</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>#Desanti2017 pmid=29222424</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>#Desanti2017 pmid=29222424</div></td></tr>
<tr><td colspan="2"> </td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;">#Mazurkewich2019 pmid=31740581</ins></div></td></tr>
<tr><td colspan="2"> </td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;">#Zong2022 pmid=35304453</ins></div></td></tr>
<tr><td colspan="2"> </td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;">#Ernst2020 pmid=32094331</ins></div></td></tr>
<tr><td colspan="2"> </td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;"></ins></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div></biblio></div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div></biblio></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>[[Category:Carbohydrate Esterase Families|CE015]]</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>[[Category:Carbohydrate Esterase Families|CE015]]</div></td></tr>
</table>
Johan Larsbrink
https://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_15&diff=16500&oldid=prev
Harry Brumer: Text replacement - "\^\^\^(.*)\^\^\^" to "$1"
2021-12-18T21:14:47Z
<p>Text replacement - "\^\^\^(.*)\^\^\^" to "<a href="/index.php?title=User:$1&action=edit&redlink=1" class="new" title="User:$1 (page does not exist)">$1</a>"</p>
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 21:14, 18 December 2021</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l1" >Line 1:</td>
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<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --></div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>{{CuratorApproved}}</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>{{CuratorApproved}}</div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>* [[Author]]: <del class="diffchange diffchange-inline">^^^</del>Jenny Arnling Bååth<del class="diffchange diffchange-inline">^^^ </del>and <del class="diffchange diffchange-inline">^^^</del>Scott Mazurkewich<del class="diffchange diffchange-inline">^^^</del></div></td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>* [[Author]]: <ins class="diffchange diffchange-inline">[[User:</ins>Jenny Arnling Bååth<ins class="diffchange diffchange-inline">|Jenny Arnling Bååth]] </ins>and <ins class="diffchange diffchange-inline">[[User:Scott Mazurkewich|</ins>Scott Mazurkewich<ins class="diffchange diffchange-inline">]]</ins></div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>* [[Responsible Curator]]: <del class="diffchange diffchange-inline">^^^</del>Johan Larsbrink<del class="diffchange diffchange-inline">^^^</del></div></td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>* [[Responsible Curator]]: <ins class="diffchange diffchange-inline">[[User:</ins>Johan Larsbrink<ins class="diffchange diffchange-inline">|Johan Larsbrink]]</ins></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>----</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>----</div></td></tr>
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</table>
Harry Brumer
https://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_15&diff=14617&oldid=prev
Harry Brumer at 20:30, 23 March 2020
2020-03-23T20:30:21Z
<p></p>
<table class="diff diff-contentalign-left diff-editfont-monospace" data-mw="interface">
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 20:30, 23 March 2020</td>
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<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Substrate specificity ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Substrate specificity ==</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>All CE15 enzymes characterized to-date are glucuronoyl esterases, cleaving esters of D-glucuronic acid. The first reported glucuronoyl esterase was ''Sc''GE1 from the white-rot fungus ''Schizophyllum commune'', and the activity was demonstrated by TLC on a methyl ester of 4-''O''-methyl-D-glucuronic acid <cite>Spanikova2006</cite>. While CE15 members are found in both fungal and bacterial species, several bacterial CE15 enzymes are more promiscuous than their fungal counterparts and are active also on esters of galacturonoate <cite>Arnlingbaath2018</cite>. Feruloyl- and acetyl esterase activities have been reported for certain CE15 enzymes as side activities <cite>Desanti2016 Mosbech2018</cite>. The proposed physiological role of CE15 enzymes is to hydrolyze lignin-carbohydrate ester linkages between lignin and glucuronoxylan in plant cell walls, and a few studies have demonstrated their activity on lignocellulose-derived materials and plant biomass <cite>Derrico2016 Arnlingbaath2016 Mosbech2018 </cite>.</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>All CE15 enzymes characterized to-date are glucuronoyl esterases, cleaving esters of D-glucuronic acid. The first reported glucuronoyl esterase was ''Sc''GE1 from the white-rot fungus ''Schizophyllum commune'', and the activity was demonstrated by TLC on a methyl ester of 4-''O''-methyl-D-glucuronic acid <cite>Spanikova2006</cite>. While CE15 members are found in both fungal and bacterial species, several bacterial CE15 enzymes are more promiscuous than their fungal counterparts and are active also on esters of galacturonoate <cite>Arnlingbaath2018</cite>. Feruloyl- and acetyl esterase activities have been reported for certain CE15 enzymes as side activities <cite>Desanti2016 Mosbech2018</cite>. The proposed physiological role of CE15 enzymes is to hydrolyze lignin-carbohydrate ester linkages between lignin and glucuronoxylan in plant cell walls, and a few studies have demonstrated their activity on lignocellulose-derived materials and plant biomass <cite>Derrico2016 Arnlingbaath2016 Mosbech2018 </cite>.</div></td></tr>
<tr><td colspan="2"> </td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;">== Catalytic Residues and Mechanism ==</ins></div></td></tr>
<tr><td colspan="2"> </td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;">All CE15 enzymes are serine-type hydrolases, containing a catalytic triad of Glu/Asp-His-Ser <cite>Pokkuluri2011 Charavgi2013 Desanti2017 Arnlingbaath2018</cite>. The position of the acidic residue of the triad is not similarly positioned in all CE15 members as the residue can be found on different loops of the conserved fold <cite>Desanti2017</cite>. A conserved arginine found in all of the CE15 structures, proximal to the catalytic triad, has been proposed to stabilize the formation of the oxyanion during catalysis <cite>Arnlingbaath2018</cite>.</ins></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Three-dimensional structures ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Three-dimensional structures ==</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>Representative structures of CE15 enzymes from bacterial and fungal sources have been determined, including ''Tr''GE (Cip2) from ''T. reesei'' (''Hypocrea jecorina'', PDB [{{PDBlink}}3pic 3pic]) <cite>Pokkuluri2011</cite>, ''St''GE2 from ''Thermothelomyces thermophila'' (''Sporotrichum thermophile'', PDB [{{PDBlink}}4g4g 4g4g], [{{PDBlink}}4g4i 4g4i], and [{{PDBlink}}4g4j 4g4j]) <cite>Charavgi2013</cite>, marine metagenome sequence MZ0003 (PDB [{{PDBlink}}6ehn 6ehn]) <cite>Desanti2017</cite>, ''Ot''CE15A (PDB [{{PDBlink}}6grw 6grw] and [{{PDBlink}}6gs0 6gs0]) and ''Su''CE15C (PDB [{{PDBlink}}6gry 6gry] and [{{PDBlink}}6gu8 6gu8]) <cite>Arnlingbaath2018</cite> (see the CAZy database for a [http://www.cazy.org/CE15_structure.html continuously updated list]). All structurally determined CE15 enzymes share an alpha/beta hydrolase fold, consisting of a three-layer alpha-beta-alpha sandwich with the active site in a solvent-exposed cleft. The structures of the bacterial enzymes determined thus far exhibit sizeable inserts which result in much deeper active site pockets compared to the shallow active sites seen in fungal glucuronoyl esterase structures <cite>Desanti2017 Arnlingbaath2018 </cite>.</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>Representative structures of CE15 enzymes from bacterial and fungal sources have been determined, including ''Tr''GE (Cip2) from ''T. reesei'' (''Hypocrea jecorina'', PDB [{{PDBlink}}3pic 3pic]) <cite>Pokkuluri2011</cite>, ''St''GE2 from ''Thermothelomyces thermophila'' (''Sporotrichum thermophile'', PDB [{{PDBlink}}4g4g 4g4g], [{{PDBlink}}4g4i 4g4i], and [{{PDBlink}}4g4j 4g4j]) <cite>Charavgi2013</cite>, marine metagenome sequence MZ0003 (PDB [{{PDBlink}}6ehn 6ehn]) <cite>Desanti2017</cite>, ''Ot''CE15A (PDB [{{PDBlink}}6grw 6grw] and [{{PDBlink}}6gs0 6gs0]) and ''Su''CE15C (PDB [{{PDBlink}}6gry 6gry] and [{{PDBlink}}6gu8 6gu8]) <cite>Arnlingbaath2018</cite> (see the CAZy database for a [http://www.cazy.org/CE15_structure.html continuously updated list]). All structurally determined CE15 enzymes share an alpha/beta hydrolase fold, consisting of a three-layer alpha-beta-alpha sandwich with the active site in a solvent-exposed cleft. The structures of the bacterial enzymes determined thus far exhibit sizeable inserts which result in much deeper active site pockets compared to the shallow active sites seen in fungal glucuronoyl esterase structures <cite>Desanti2017 Arnlingbaath2018 </cite>.</div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div><del style="font-weight: bold; text-decoration: none;"></del></div></td><td colspan="2"> </td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div><del style="font-weight: bold; text-decoration: none;">== Catalytic Residues and Mechanism ==</del></div></td><td colspan="2"> </td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div><del style="font-weight: bold; text-decoration: none;">All CE15 enzymes are serine-type hydrolases, containing a catalytic triad of Glu/Asp-His-Ser <cite>Pokkuluri2011 Charavgi2013 Desanti2017 Arnlingbaath2018</cite>. The position of the acidic residue of the triad is not similarly positioned in all CE15 members as the residue can be found on different loops of the conserved fold <cite>Desanti2017</cite>. A conserved arginine found in all of the CE15 structures, proximal to the catalytic triad, has been proposed to stabilize the formation of the oxyanion during catalysis <cite>Arnlingbaath2018</cite>.</del></div></td><td colspan="2"> </td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Family Firsts ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Family Firsts ==</div></td></tr>
</table>
Harry Brumer
https://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_15&diff=13942&oldid=prev
Harry Brumer at 16:26, 16 July 2019
2019-07-16T16:26:23Z
<p></p>
<table class="diff diff-contentalign-left diff-editfont-monospace" data-mw="interface">
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 16:26, 16 July 2019</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l11" >Line 11:</td>
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<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|{{Hl2}} colspan="2" align="center" |'''Carbohydrate Esterase Family CE15'''</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|{{Hl2}} colspan="2" align="center" |'''Carbohydrate Esterase Family CE15'''</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|-</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|-</div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>|'''<del class="diffchange diffchange-inline">Clan</del>''' </div></td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins class="diffchange diffchange-inline">|</ins>|'''<ins class="diffchange diffchange-inline">Acid/alcohol sugar substrate</ins>''' </div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>|<del class="diffchange diffchange-inline">GH-x</del></div></td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>|<ins class="diffchange diffchange-inline">Acid</ins></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|-</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|-</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|'''Mechanism'''</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|'''Mechanism'''</div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>|<del class="diffchange diffchange-inline">retaining/inverting</del></div></td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>|<ins class="diffchange diffchange-inline">serine hydrolase</ins></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|-</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|-</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|'''Active site residues'''</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|'''Active site residues'''</div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>|known<del class="diffchange diffchange-inline">/not known</del></div></td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>|known<ins class="diffchange diffchange-inline">, catalytic triad</ins></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|-</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|-</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''</div></td></tr>
</table>
Harry Brumer
https://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_15&diff=13933&oldid=prev
Johan Larsbrink at 11:19, 15 July 2019
2019-07-15T11:19:27Z
<p></p>
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 11:19, 15 July 2019</td>
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<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>{{<del class="diffchange diffchange-inline">UnderConstruction</del>}}</div></td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>{{<ins class="diffchange diffchange-inline">CuratorApproved</ins>}}</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>* [[Author]]: ^^^Jenny Arnling Bååth^^^ and ^^^Scott Mazurkewich^^^</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>* [[Author]]: ^^^Jenny Arnling Bååth^^^ and ^^^Scott Mazurkewich^^^</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>* [[Responsible Curator]]: ^^^Johan Larsbrink^^^</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>* [[Responsible Curator]]: ^^^Johan Larsbrink^^^</div></td></tr>
</table>
Johan Larsbrink
https://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_15&diff=13930&oldid=prev
Scott Mazurkewich at 18:12, 11 July 2019
2019-07-11T18:12:36Z
<p></p>
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 18:12, 11 July 2019</td>
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<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td colspan="2"> </td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;">[[File: CE15_CAZypedia_Figure.png|thumb|right|400px|'''Figure 1. Comparison of structurally determined CE15 members.''' The CE15s (A) ''St''GE2 from ''Thermothelomyces thermophila'' (PDB ID [{{PDBlink}}4g4j 4G4J]), (B) ''Ot''CE15A from ''Opitutus terrae'' (PDB ID [{{PDBlink}}6gs0 6GS0]), and (C) ''Tt''CE15A from ''Teredinibacter turnerae'' (PDB ID [{{PDBlink}}6hsw 6HSW]) are shown in cartoon representation. The catalytic triad in each enzyme is shown as sticks and the methyl ester of 4-''O''-methyl glucuronoate first observed in ''St''GE2 is shown in all structures as green sticks. While all CE15 members contain the alpha/beta hydrolase fold, the most prominent difference across the CE15 family observed to-date are the presence, absence, or variety of inserted regions that protrude and build-up ridges around the active site (the differently colored regions in the ''Ot''CE15A and ''Tt''CE15A). The extent to which these regions affect the enzyme’s substrate specificity has yet to be fully elucidated.]]</ins></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Substrate specificity ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Substrate specificity ==</div></td></tr>
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Scott Mazurkewich
https://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_15&diff=13485&oldid=prev
Harry Brumer at 18:51, 28 January 2019
2019-01-28T18:51:54Z
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 18:51, 28 January 2019</td>
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<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Three-dimensional structures ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Three-dimensional structures ==</div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>Representative structures of CE15 enzymes from bacterial and fungal sources have been determined, including ''Tr''GE (Cip2) from ''T. reesei'' (''Hypocrea jecorina''<del class="diffchange diffchange-inline">) (</del>PDB [{{PDBlink}}3pic 3pic]) <cite>Pokkuluri2011</cite>, ''St''GE2 from ''Thermothelomyces thermophila'' (<del class="diffchange diffchange-inline">previously </del>''Sporotrichum thermophile'' <del class="diffchange diffchange-inline">(</del>PDB [{{PDBlink}}4g4g 4g4g], [{{PDBlink}}4g4i 4g4i], and [{{PDBlink}}4g4j 4g4j]) <cite>Charavgi2013</cite>, marine metagenome sequence MZ0003 (PDB [{{PDBlink}}6ehn 6ehn]) <cite>Desanti2017</cite>, ''Ot''CE15A (PDB [{{PDBlink}}6grw 6grw] and [{{PDBlink}}6gs0 6gs0]) and ''Su''CE15C (PDB [{{PDBlink}}6gry 6gry] and [{{PDBlink}}6gu8 6gu8]) <cite>Arnlingbaath2018</cite> (see the CAZy database for a [http://www.cazy.org/CE15_structure.html continuously updated list]). All structurally determined CE15 enzymes share an alpha/beta hydrolase fold, consisting of a three-layer alpha-beta-alpha sandwich with the active site in a solvent-exposed cleft. The structures of the bacterial enzymes determined thus far exhibit sizeable inserts which result in much deeper active site pockets compared to the shallow active sites seen in fungal glucuronoyl esterase structures <cite>Desanti2017 Arnlingbaath2018 </cite>.</div></td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>Representative structures of CE15 enzymes from bacterial and fungal sources have been determined, including ''Tr''GE (Cip2) from ''T. reesei'' (''Hypocrea jecorina''<ins class="diffchange diffchange-inline">, </ins>PDB [{{PDBlink}}3pic 3pic]) <cite>Pokkuluri2011</cite>, ''St''GE2 from ''Thermothelomyces thermophila'' (''Sporotrichum thermophile''<ins class="diffchange diffchange-inline">, </ins>PDB [{{PDBlink}}4g4g 4g4g], [{{PDBlink}}4g4i 4g4i], and [{{PDBlink}}4g4j 4g4j]) <cite>Charavgi2013</cite>, marine metagenome sequence MZ0003 (PDB [{{PDBlink}}6ehn 6ehn]) <cite>Desanti2017</cite>, ''Ot''CE15A (PDB [{{PDBlink}}6grw 6grw] and [{{PDBlink}}6gs0 6gs0]) and ''Su''CE15C (PDB [{{PDBlink}}6gry 6gry] and [{{PDBlink}}6gu8 6gu8]) <cite>Arnlingbaath2018</cite> (see the CAZy database for a [http://www.cazy.org/CE15_structure.html continuously updated list]). All structurally determined CE15 enzymes share an alpha/beta hydrolase fold, consisting of a three-layer alpha-beta-alpha sandwich with the active site in a solvent-exposed cleft. The structures of the bacterial enzymes determined thus far exhibit sizeable inserts which result in much deeper active site pockets compared to the shallow active sites seen in fungal glucuronoyl esterase structures <cite>Desanti2017 Arnlingbaath2018 </cite>.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Catalytic Residues and Mechanism ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Catalytic Residues and Mechanism ==</div></td></tr>
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Harry Brumer