https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_48&feed=atom&action=history
Glycoside Hydrolase Family 48 - Revision history
2024-03-28T14:36:26Z
Revision history for this page on the wiki
MediaWiki 1.35.10
https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_48&diff=16701&oldid=prev
Harry Brumer: Text replacement - "\^\^\^(.*)\^\^\^" to "$1"
2021-12-18T21:20:50Z
<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>
<table class="diff diff-contentalign-left diff-editfont-monospace" data-mw="interface">
<col class="diff-marker" />
<col class="diff-content" />
<col class="diff-marker" />
<col class="diff-content" />
<tr class="diff-title" lang="en-CA">
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">← Older revision</td>
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 21:20, 18 December 2021</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l1" >Line 1:</td>
<td colspan="2" class="diff-lineno">Line 1:</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><!-- 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><!-- 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>Bareket Dassa<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>Bareket Dassa<ins class="diffchange diffchange-inline">|Bareket Dassa]]</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>Ed Bayer<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>Ed Bayer<ins class="diffchange diffchange-inline">|Ed Bayer]]</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;"></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>
</table>
Harry Brumer
https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_48&diff=7412&oldid=prev
Harry Brumer: updated CAZyDBlink
2012-07-12T15:56:41Z
<p>updated CAZyDBlink</p>
<table class="diff diff-contentalign-left diff-editfont-monospace" data-mw="interface">
<col class="diff-marker" />
<col class="diff-content" />
<col class="diff-marker" />
<col class="diff-content" />
<tr class="diff-title" lang="en-CA">
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">← Older revision</td>
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 15:56, 12 July 2012</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l22" >Line 22:</td>
<td colspan="2" class="diff-lineno">Line 22:</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>
<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>| colspan="2" |<del class="diffchange diffchange-inline">http://www.cazy.org/fam/</del>GH48.html</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>| colspan="2" |<ins class="diffchange diffchange-inline">{{CAZyDBlink}}</ins>GH48.html</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></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></div></td></tr>
<tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l48" >Line 48:</td>
<td colspan="2" class="diff-lineno">Line 48:</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>The structure of the catalytic module of Cel48S of ''C. thermocellum'' showed a similar tunnel-shaped substrate-binding region formed by the alpha helices in the protein. The hydrolysis of the cellulose chain in Cel48S appeared to involve Glu87 (the equivalent of Glu55 in ''C. cellulolyticum'' Cel48F) as an acid to protonate the glycosidic oxygen atom and Tyr351 as a base to extract a proton from the nucleophilic water molecule that attacks the anomeric carbon atom. More recent studies of Cel48F failed to unambiguously identity the catalytic base in the cleavage reaction <cite>Parsiegla2008</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>The structure of the catalytic module of Cel48S of ''C. thermocellum'' showed a similar tunnel-shaped substrate-binding region formed by the alpha helices in the protein. The hydrolysis of the cellulose chain in Cel48S appeared to involve Glu87 (the equivalent of Glu55 in ''C. cellulolyticum'' Cel48F) as an acid to protonate the glycosidic oxygen atom and Tyr351 as a base to extract a proton from the nucleophilic water molecule that attacks the anomeric carbon atom. More recent studies of Cel48F failed to unambiguously identity the catalytic base in the cleavage reaction <cite>Parsiegla2008</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="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>A recent experimental study in ''Thermobifida fusca'' Cel48A confirmed that aspartic acid (Asp225) is the catalytic base in family 48 <del class="diffchange diffchange-inline">glycosyl </del>hydrolases <cite>Kostylev2011</cite>. This residue is equivalent to D230 of ''C. cellulolyticum'' Cel48F and D255 of ''C. thermocellum'' Cel48S. In this study, site-directed mutagenesis demonstrated that the D225E mutation retained partial activity on soluble and insoluble substrates. Azide rescue hydrolysis assays showed that the D225G mutation restored its activity with added azide.</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>A recent experimental study in ''Thermobifida fusca'' Cel48A confirmed that aspartic acid (Asp225) is the catalytic base in family 48 <ins class="diffchange diffchange-inline">glycoside </ins>hydrolases <cite>Kostylev2011</cite>. This residue is equivalent to D230 of ''C. cellulolyticum'' Cel48F and D255 of ''C. thermocellum'' Cel48S. In this study, site-directed mutagenesis demonstrated that the D225E mutation retained partial activity on soluble and insoluble substrates. Azide rescue hydrolysis assays showed that the D225G mutation restored its activity with added azide.</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>
</table>
Harry Brumer
https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_48&diff=7255&oldid=prev
Bareket Dassa at 10:03, 20 March 2012
2012-03-20T10:03:45Z
<p></p>
<table class="diff diff-contentalign-left diff-editfont-monospace" data-mw="interface">
<col class="diff-marker" />
<col class="diff-content" />
<col class="diff-marker" />
<col class="diff-content" />
<tr class="diff-title" lang="en-CA">
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">← Older revision</td>
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 10:03, 20 March 2012</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l48" >Line 48:</td>
<td colspan="2" class="diff-lineno">Line 48:</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>The structure of the catalytic module of Cel48S of ''C. thermocellum'' showed a similar tunnel-shaped substrate-binding region formed by the alpha helices in the protein. The hydrolysis of the cellulose chain in Cel48S appeared to involve Glu87 (the equivalent of Glu55 in ''C. cellulolyticum'' Cel48F) as an acid to protonate the glycosidic oxygen atom and Tyr351 as a base to extract a proton from the nucleophilic water molecule that attacks the anomeric carbon atom. More recent studies of Cel48F failed to unambiguously identity the catalytic base in the cleavage reaction <cite>Parsiegla2008</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>The structure of the catalytic module of Cel48S of ''C. thermocellum'' showed a similar tunnel-shaped substrate-binding region formed by the alpha helices in the protein. The hydrolysis of the cellulose chain in Cel48S appeared to involve Glu87 (the equivalent of Glu55 in ''C. cellulolyticum'' Cel48F) as an acid to protonate the glycosidic oxygen atom and Tyr351 as a base to extract a proton from the nucleophilic water molecule that attacks the anomeric carbon atom. More recent studies of Cel48F failed to unambiguously identity the catalytic base in the cleavage reaction <cite>Parsiegla2008</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="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>A recent experimental study in Thermobifida fusca Cel48A confirmed that aspartic acid (Asp225) is the catalytic base in family 48 glycosyl hydrolases <cite>Kostylev2011</cite>.This residue is equivalent to D230 of C. cellulolyticum Cel48F and D255 of C. thermocellum Cel48S. In this study, site-directed mutagenesis demonstrated that the D225E mutation retained partial activity on soluble and insoluble substrates. Azide rescue hydrolysis assays showed that the D225G mutation restored its activity with added azide.</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>A recent experimental study in <ins class="diffchange diffchange-inline">''</ins>Thermobifida fusca<ins class="diffchange diffchange-inline">'' </ins>Cel48A confirmed that aspartic acid (Asp225) is the catalytic base in family 48 glycosyl hydrolases <cite>Kostylev2011</cite>. This residue is equivalent to D230 of <ins class="diffchange diffchange-inline">''</ins>C. cellulolyticum<ins class="diffchange diffchange-inline">'' </ins>Cel48F and D255 of <ins class="diffchange diffchange-inline">''</ins>C. thermocellum<ins class="diffchange diffchange-inline">'' </ins>Cel48S. In this study, site-directed mutagenesis demonstrated that the D225E mutation retained partial activity on soluble and insoluble substrates. Azide rescue hydrolysis assays showed that the D225G mutation restored its activity with added azide.</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 colspan="2" class="diff-lineno" id="mw-diff-left-l67" >Line 67:</td>
<td colspan="2" class="diff-lineno">Line 67:</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 sterochemistry determination: ''Cellulomonas fimi'' CenE, described as an endo-β-1,4-glucanase, catalyzes the hydrolysis of cellohexaose with inversion of anomeric carbon configuration, characteristic of a single displacement reaction <cite>Shen1994 </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 sterochemistry determination: ''Cellulomonas fimi'' CenE, described as an endo-β-1,4-glucanase, catalyzes the hydrolysis of cellohexaose with inversion of anomeric carbon configuration, characteristic of a single displacement reaction <cite>Shen1994 </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="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 [[catalytic nucleophile]] identification: Asp225 was experimentally shown to be the catalytic base in T. fusca Cel48A <del class="diffchange diffchange-inline">(see </del><cite><del class="diffchange diffchange-inline">Parsiegla2008</del></cite><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>;First [[catalytic nucleophile]] identification: Asp225 was experimentally shown to be the catalytic base in <ins class="diffchange diffchange-inline">''</ins>T. fusca<ins class="diffchange diffchange-inline">'' </ins>Cel48A <ins class="diffchange diffchange-inline"> </ins><cite><ins class="diffchange diffchange-inline">Kostylev2011</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>;First [[general acid/base]] residue identification: Glu was the proposed proton donor in the cleavage reaction <cite>Kostylev2011</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 [[general acid/base]] residue identification: Glu was the proposed proton donor in the cleavage reaction <cite>Kostylev2011</cite>.</div></td></tr>
</table>
Bareket Dassa
https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_48&diff=7254&oldid=prev
Bareket Dassa at 10:01, 20 March 2012
2012-03-20T10:01:53Z
<p></p>
<table class="diff diff-contentalign-left diff-editfont-monospace" data-mw="interface">
<col class="diff-marker" />
<col class="diff-content" />
<col class="diff-marker" />
<col class="diff-content" />
<tr class="diff-title" lang="en-CA">
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">← Older revision</td>
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 10:01, 20 March 2012</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l48" >Line 48:</td>
<td colspan="2" class="diff-lineno">Line 48:</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>The structure of the catalytic module of Cel48S of ''C. thermocellum'' showed a similar tunnel-shaped substrate-binding region formed by the alpha helices in the protein. The hydrolysis of the cellulose chain in Cel48S appeared to involve Glu87 (the equivalent of Glu55 in ''C. cellulolyticum'' Cel48F) as an acid to protonate the glycosidic oxygen atom and Tyr351 as a base to extract a proton from the nucleophilic water molecule that attacks the anomeric carbon atom. More recent studies of Cel48F failed to unambiguously identity the catalytic base in the cleavage reaction <cite>Parsiegla2008</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>The structure of the catalytic module of Cel48S of ''C. thermocellum'' showed a similar tunnel-shaped substrate-binding region formed by the alpha helices in the protein. The hydrolysis of the cellulose chain in Cel48S appeared to involve Glu87 (the equivalent of Glu55 in ''C. cellulolyticum'' Cel48F) as an acid to protonate the glycosidic oxygen atom and Tyr351 as a base to extract a proton from the nucleophilic water molecule that attacks the anomeric carbon atom. More recent studies of Cel48F failed to unambiguously identity the catalytic base in the cleavage reaction <cite>Parsiegla2008</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="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>A recent experimental study in Thermobifida fusca Cel48A confirmed that aspartic acid (Asp225) is the catalytic base in family 48 glycosyl hydrolases <del class="diffchange diffchange-inline">(Wilson)</del>.This residue is equivalent to D230 of C. cellulolyticum Cel48F and D255 of C. thermocellum Cel48S. In this study, site-directed mutagenesis demonstrated that the D225E mutation retained partial activity on soluble and insoluble substrates. Azide rescue hydrolysis assays showed that the D225G mutation restored its activity with added azide<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>A recent experimental study in Thermobifida fusca Cel48A confirmed that aspartic acid (Asp225) is the catalytic base in family 48 glycosyl hydrolases <ins class="diffchange diffchange-inline"><cite>Kostylev2011</cite></ins>.This residue is equivalent to D230 of C. cellulolyticum Cel48F and D255 of C. thermocellum Cel48S. In this study, site-directed mutagenesis demonstrated that the D225E mutation retained partial activity on soluble and insoluble substrates. Azide rescue hydrolysis assays showed that the D225G mutation restored its activity with added azide.</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"><cite>Kostylev2011</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>== 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 colspan="2" class="diff-lineno" id="mw-diff-left-l97" >Line 97:</td>
<td colspan="2" class="diff-lineno">Line 96:</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>#Sanchez2003 pmid=12823562</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>#Sanchez2003 pmid=12823562</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>#Irwin2000 pmid=10931180</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>#Irwin2000 pmid=10931180</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"> Normal 0 false false false EN-US X-NONE HE MicrosoftInternetExplorer4 </del>Kostylev2011 pmid=21764975</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>#Kostylev2011 pmid=21764975</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></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:Glycoside Hydrolase Families|GH048]]</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:Glycoside Hydrolase Families|GH048]]</div></td></tr>
</table>
Bareket Dassa
https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_48&diff=7253&oldid=prev
Bareket Dassa at 10:00, 20 March 2012
2012-03-20T10:00:29Z
<p></p>
<table class="diff diff-contentalign-left diff-editfont-monospace" data-mw="interface">
<col class="diff-marker" />
<col class="diff-content" />
<col class="diff-marker" />
<col class="diff-content" />
<tr class="diff-title" lang="en-CA">
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">← Older revision</td>
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 10:00, 20 March 2012</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l46" >Line 46:</td>
<td colspan="2" class="diff-lineno">Line 46:</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>The crystal structure of Cel48F, a cellulosome component of ''C. cellulolyticum'', revealed the active center at the junction of the cleft and tunnel regions, where Glu55 is the proposed proton donor in the cleavage reaction, and the corresponding base was initially proposed to be either Glu44 or Asp230 <cite>Parsiegla1998</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>The crystal structure of Cel48F, a cellulosome component of ''C. cellulolyticum'', revealed the active center at the junction of the cleft and tunnel regions, where Glu55 is the proposed proton donor in the cleavage reaction, and the corresponding base was initially proposed to be either Glu44 or Asp230 <cite>Parsiegla1998</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="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>The structure of the catalytic module of Cel48S of ''C. thermocellum'' showed a similar tunnel-shaped substrate-binding region formed by the alpha helices in the protein. The hydrolysis of the cellulose chain in Cel48S appeared to involve Glu87 (the equivalent of Glu55 in ''C. cellulolyticum'' Cel48F) as an acid to protonate the glycosidic oxygen atom and Tyr351 as a base to extract a proton from the nucleophilic water molecule that attacks the anomeric carbon atom.</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>The structure of the catalytic module of Cel48S of ''C. thermocellum'' showed a similar tunnel-shaped substrate-binding region formed by the alpha helices in the protein. The hydrolysis of the cellulose chain in Cel48S appeared to involve Glu87 (the equivalent of Glu55 in ''C. cellulolyticum'' Cel48F) as an acid to protonate the glycosidic oxygen atom and Tyr351 as a base to extract a proton from the nucleophilic water molecule that attacks the anomeric carbon atom<ins class="diffchange diffchange-inline">. More recent studies of Cel48F failed to unambiguously identity the catalytic base in the cleavage reaction <cite>Parsiegla2008</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="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">More </del>recent <del class="diffchange diffchange-inline">studies of Cel48F failed to unambiguously identity </del>the catalytic base in the <del class="diffchange diffchange-inline">cleavage reaction </del><cite><del class="diffchange diffchange-inline">Parsiegla2008</del></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><ins class="diffchange diffchange-inline">A </ins>recent <ins class="diffchange diffchange-inline">experimental study in Thermobifida fusca Cel48A confirmed that aspartic acid (Asp225) is </ins>the catalytic base in <ins class="diffchange diffchange-inline">family 48 glycosyl hydrolases (Wilson).This residue is equivalent to D230 of C. cellulolyticum Cel48F and D255 of C. thermocellum Cel48S. In this study, site-directed mutagenesis demonstrated that the D225E mutation retained partial activity on soluble and insoluble substrates. Azide rescue hydrolysis assays showed that </ins>the <ins class="diffchange diffchange-inline">D225G mutation restored its activity with added azide.</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><cite><ins class="diffchange diffchange-inline">Kostylev2011</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 colspan="2" class="diff-lineno" id="mw-diff-left-l67" >Line 67:</td>
<td colspan="2" class="diff-lineno">Line 68:</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 sterochemistry determination: ''Cellulomonas fimi'' CenE, described as an endo-β-1,4-glucanase, catalyzes the hydrolysis of cellohexaose with inversion of anomeric carbon configuration, characteristic of a single displacement reaction <cite>Shen1994 </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 sterochemistry determination: ''Cellulomonas fimi'' CenE, described as an endo-β-1,4-glucanase, catalyzes the hydrolysis of cellohexaose with inversion of anomeric carbon configuration, characteristic of a single displacement reaction <cite>Shen1994 </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="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 [[catalytic nucleophile]] identification: <del class="diffchange diffchange-inline">…“Waiting patiently”… </del>(see <cite>Parsiegla2008</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 [[catalytic nucleophile]] identification: <ins class="diffchange diffchange-inline">Asp225 was experimentally shown to be the catalytic base in T. fusca Cel48A </ins>(see <cite>Parsiegla2008</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="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 [[general acid/base]] residue identification: Glu was the proposed proton donor in the cleavage reaction <cite><del class="diffchange diffchange-inline">Parsiegla1998</del></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 [[general acid/base]] residue identification: Glu was the proposed proton donor in the cleavage reaction <cite><ins class="diffchange diffchange-inline">Kostylev2011</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>;First 3-D structure: The crystal structure of catalytic module of ''C. cellulolyticum'' Cel48F in complex with oligosaccharides <cite>Parsiegla2008</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 3-D structure: The crystal structure of catalytic module of ''C. cellulolyticum'' Cel48F in complex with oligosaccharides <cite>Parsiegla2008</cite>.</div></td></tr>
<tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l96" >Line 96:</td>
<td colspan="2" class="diff-lineno">Line 97:</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>#Sanchez2003 pmid=12823562</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>#Sanchez2003 pmid=12823562</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>#Irwin2000 pmid=10931180</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>#Irwin2000 pmid=10931180</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;"># Normal 0 false false false EN-US X-NONE HE MicrosoftInternetExplorer4 Kostylev2011 pmid=21764975</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:Glycoside Hydrolase Families|GH048]]</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:Glycoside Hydrolase Families|GH048]]</div></td></tr>
</table>
Bareket Dassa
https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_48&diff=4912&oldid=prev
Spencer Williams at 04:20, 13 June 2010
2010-06-13T04:20:15Z
<p></p>
<table class="diff diff-contentalign-left diff-editfont-monospace" data-mw="interface">
<col class="diff-marker" />
<col class="diff-content" />
<col class="diff-marker" />
<col class="diff-content" />
<tr class="diff-title" lang="en-CA">
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">← Older revision</td>
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 04:20, 13 June 2010</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l30" >Line 30:</td>
<td colspan="2" class="diff-lineno">Line 30:</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 specificities ==</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 specificities ==</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">'''</del>Family 48<del class="diffchange diffchange-inline">''' </del>[[glycoside hydrolases]] are major and key components of some cellulase systems, occurring in free enzyme systems (e.g., in ''[http://www.cazy.org/b291.html Thermobifida fusca]''), multi-functional enzymes (e.g, in ''[http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?id=44001 Caldicellulosiruptor saccharolyticus]''), anaerobic fungi (e.g., ''[http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?id=99929 Piromyces equi]'') and every [http://www.weizmann.ac.il/Biological_Chemistry/scientist/Bayer/new_pages/reserch_topics/cellulosome_systems.html cellulosome] system thus far described. The GH48 cellulase is commonly the most abundant enzyme subunit in cellulosome-producing bacteria. Each bacterium usually contains a single gene that codes for a GH48 enzyme, although a few bacteria (e.g., ''[http://www.cazy.org/b514.html Clostridium thermocellum]'' and ''[http://www.cazy.org/b897.html Anaerocellum thermophilum]'') contain two or more GH48 genes. Of the two ''C. thermocellum'' GH48 enzymes, one (Cel48S) is a [http://www.weizmann.ac.il/Biological_Chemistry/scientist/Bayer/new_pages/reserch_topics/Cohesin_dockerin.html dockerin]-containing cellulosomal enzyme, and the other (Cel48Y) is a free, non-cellulosomal enzyme that contains a cellulose-binding CBM3.</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>Family 48 [[glycoside hydrolases]] are major and key components of some cellulase systems, occurring in free enzyme systems (e.g., in ''[http://www.cazy.org/b291.html Thermobifida fusca]''), multi-functional enzymes (e.g, in ''[http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?id=44001 Caldicellulosiruptor saccharolyticus]''), anaerobic fungi (e.g., ''[http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?id=99929 Piromyces equi]'') and every [http://www.weizmann.ac.il/Biological_Chemistry/scientist/Bayer/new_pages/reserch_topics/cellulosome_systems.html cellulosome] system thus far described. The GH48 cellulase is commonly the most abundant enzyme subunit in cellulosome-producing bacteria. Each bacterium usually contains a single gene that codes for a GH48 enzyme, although a few bacteria (e.g., ''[http://www.cazy.org/b514.html Clostridium thermocellum]'' and ''[http://www.cazy.org/b897.html Anaerocellum thermophilum]'') contain two or more GH48 genes. Of the two ''C. thermocellum'' GH48 enzymes, one (Cel48S) is a [http://www.weizmann.ac.il/Biological_Chemistry/scientist/Bayer/new_pages/reserch_topics/Cohesin_dockerin.html dockerin]-containing cellulosomal enzyme, and the other (Cel48Y) is a free, non-cellulosomal enzyme that contains a cellulose-binding CBM3.</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>The following activities have been reported: endo-β-1,4-glucanase, chitinase, endo-processive cellulase and cellobiohydrolase. Its preferred substrate is amorphous or crystalline cellulose over carboxymethylcellulose (CMC), and its activity is strongly inhibited by the presence of cellobiose. Although its activity on various substrates is characteristically very low, it is thought to be a critically important enzyme which imparts a major component of synergy to its cellulase system.</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>The following activities have been reported: endo-β-1,4-glucanase, chitinase, endo-processive cellulase and cellobiohydrolase. Its preferred substrate is amorphous or crystalline cellulose over carboxymethylcellulose (CMC), and its activity is strongly inhibited by the presence of cellobiose. Although its activity on various substrates is characteristically very low, it is thought to be a critically important enzyme which imparts a major component of synergy to its cellulase system.</div></td></tr>
</table>
Spencer Williams
https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_48&diff=4336&oldid=prev
Bareket Dassa at 10:50, 14 April 2010
2010-04-14T10:50:50Z
<p></p>
<table class="diff diff-contentalign-left diff-editfont-monospace" data-mw="interface">
<col class="diff-marker" />
<col class="diff-content" />
<col class="diff-marker" />
<col class="diff-content" />
<tr class="diff-title" lang="en-CA">
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">← Older revision</td>
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 10:50, 14 April 2010</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l54" >Line 54:</td>
<td colspan="2" class="diff-lineno">Line 54:</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><gallery widths=200px heights=220px perrow=2 caption="3D structures of GH48 proteins (click images for large versions)"></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><gallery widths=200px heights=220px perrow=2 caption="3D structures of GH48 proteins (click images for large versions)"></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>File:1FAE.jpg|PDB ID [{{PDBlink}}1fae 1fae] from "Crystal structure of the cellulase CEL48F from ''C. cellulolyticum'' in complex with cellobiose" <cite>Parsiegla2000</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>File:1FAE.jpg|PDB ID [{{PDBlink}}1fae 1fae] from "Crystal structure of the cellulase CEL48F from ''C. cellulolyticum'' in complex with cellobiose" <cite>Parsiegla2000</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>File:1L1Y.jpg|PDB ID [{{PDBlink}}1l1y 1l1y] and [{{PDBlink}}<del class="diffchange diffchange-inline">1L2A 1L2A</del>] from "The Crystal Structure and Catalytic Mechanism of Cellobiohydrolase CelS, the Major Enzymatic Component of the ''Clostridium thermocellum'' cellulosome" <cite>Guimaraes2002</cite>, in complex with cellohexaose and cellobiose.</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:1L1Y.jpg|PDB ID [{{PDBlink}}1l1y 1l1y] and [{{PDBlink}}<ins class="diffchange diffchange-inline">1l2a 1l2a</ins>] from "The Crystal Structure and Catalytic Mechanism of Cellobiohydrolase CelS, the Major Enzymatic Component of the ''Clostridium thermocellum'' cellulosome" <cite>Guimaraes2002</cite>, in complex with cellohexaose and cellobiose.</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></gallery></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></gallery></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>3D structures of Cel48F in complex with different ligands are also available:</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>3D structures of Cel48F in complex with different ligands are also available:</div></td></tr>
</table>
Bareket Dassa
https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_48&diff=4335&oldid=prev
Bareket Dassa at 10:49, 14 April 2010
2010-04-14T10:49:58Z
<p></p>
<table class="diff diff-contentalign-left diff-editfont-monospace" data-mw="interface">
<col class="diff-marker" />
<col class="diff-content" />
<col class="diff-marker" />
<col class="diff-content" />
<tr class="diff-title" lang="en-CA">
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">← Older revision</td>
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 10:49, 14 April 2010</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l53" >Line 53:</td>
<td colspan="2" class="diff-lineno">Line 53:</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 are available for two family 48 enzymes: Cel48F (from ''Clostridium cellulolyticum'') and Cel48A (from ''Clostridium thermocellum''). Both enzymes have an (α/α)<sub>6</sub> barrel topology.</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 are available for two family 48 enzymes: Cel48F (from ''Clostridium cellulolyticum'') and Cel48A (from ''Clostridium thermocellum''). Both enzymes have an (α/α)<sub>6</sub> barrel topology.</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><gallery widths=200px heights=220px perrow=2 caption="3D structures of GH48 proteins (click images for large versions)"></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><gallery widths=200px heights=220px perrow=2 caption="3D structures of GH48 proteins (click images for large versions)"></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>File:1FAE.jpg|PDB ID [{{PDBlink}}<del class="diffchange diffchange-inline">1FAE 1FAE</del>] from "Crystal structure of the cellulase CEL48F from ''C. cellulolyticum'' in complex with cellobiose" <cite>Parsiegla2000</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>File:1FAE.jpg|PDB ID [{{PDBlink}}<ins class="diffchange diffchange-inline">1fae 1fae</ins>] from "Crystal structure of the cellulase CEL48F from ''C. cellulolyticum'' in complex with cellobiose" <cite>Parsiegla2000</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>File:1L1Y.jpg|PDB ID [{{PDBlink}}1l1y <del class="diffchange diffchange-inline">1L1Y</del>] and [{{PDBlink}}1L2A 1L2A] from "The Crystal Structure and Catalytic Mechanism of Cellobiohydrolase CelS, the Major Enzymatic Component of the ''Clostridium thermocellum'' cellulosome" <cite>Guimaraes2002</cite>, in complex with cellohexaose and cellobiose.</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:1L1Y.jpg|PDB ID [{{PDBlink}}1l1y <ins class="diffchange diffchange-inline">1l1y</ins>] and [{{PDBlink}}1L2A 1L2A] from "The Crystal Structure and Catalytic Mechanism of Cellobiohydrolase CelS, the Major Enzymatic Component of the ''Clostridium thermocellum'' cellulosome" <cite>Guimaraes2002</cite>, in complex with cellohexaose and cellobiose.</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></gallery></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></gallery></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>3D structures of Cel48F in complex with different ligands are also available:</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>3D structures of Cel48F in complex with different ligands are also available:</div></td></tr>
</table>
Bareket Dassa
https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_48&diff=4228&oldid=prev
Bareket Dassa at 08:30, 22 March 2010
2010-03-22T08:30:52Z
<p></p>
<table class="diff diff-contentalign-left diff-editfont-monospace" data-mw="interface">
<col class="diff-marker" />
<col class="diff-content" />
<col class="diff-marker" />
<col class="diff-content" />
<tr class="diff-title" lang="en-CA">
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">← Older revision</td>
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 08:30, 22 March 2010</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l59" >Line 59:</td>
<td colspan="2" class="diff-lineno">Line 59:</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>* with cellotetraose ([{{PDBlink}}1f9d 1f9d])</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>* with cellotetraose ([{{PDBlink}}1f9d 1f9d])</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>* with the thio-oligosaccharide inhibitor PIPS-IG3 ([{{PDBlink}}1f9o 1f9o])</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>* with the thio-oligosaccharide inhibitor PIPS-IG3 ([{{PDBlink}}1f9o 1f9o])</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>* with cellobiose ([{{PDBlink}}<del class="diffchange diffchange-inline">1afea </del>1fae])</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>* with cellobiose ([{{PDBlink}}<ins class="diffchange diffchange-inline">1fea </ins>1fae])</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>* with cellobiitol ([{{PDBlink}}1fbo 1fbo])</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>* with cellobiitol ([{{PDBlink}}1fbo 1fbo])</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>* with cellohexaose ([{{PDBlink}}1fbw 1fbw])</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>* with cellohexaose ([{{PDBlink}}1fbw 1fbw])</div></td></tr>
</table>
Bareket Dassa
https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_48&diff=4227&oldid=prev
Bareket Dassa at 08:30, 22 March 2010
2010-03-22T08:30:17Z
<p></p>
<table class="diff diff-contentalign-left diff-editfont-monospace" data-mw="interface">
<col class="diff-marker" />
<col class="diff-content" />
<col class="diff-marker" />
<col class="diff-content" />
<tr class="diff-title" lang="en-CA">
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">← Older revision</td>
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 08:30, 22 March 2010</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l57" >Line 57:</td>
<td colspan="2" class="diff-lineno">Line 57:</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></gallery></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></gallery></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>3D structures of Cel48F in complex with different ligands are also available:</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>3D structures of Cel48F in complex with different ligands are also available:</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>* with cellotetraose ([{{PDBlink}}<del class="diffchange diffchange-inline">1F9D </del>1f9d])</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>* with cellotetraose ([{{PDBlink}}<ins class="diffchange diffchange-inline">1f9d </ins>1f9d])</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>* with the thio-oligosaccharide inhibitor PIPS-IG3 ([{{PDBlink}}<del class="diffchange diffchange-inline">1F9O </del>1f9o])</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>* with the thio-oligosaccharide inhibitor PIPS-IG3 ([{{PDBlink}}<ins class="diffchange diffchange-inline">1f9o </ins>1f9o])</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>* with cellobiose ([{{PDBlink}}<del class="diffchange diffchange-inline">1FAE </del>1fae])</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>* with cellobiose ([{{PDBlink}}<ins class="diffchange diffchange-inline">1afea </ins>1fae])</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>* with cellobiitol ([{{PDBlink}}<del class="diffchange diffchange-inline">1FBO </del>1fbo])</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>* with cellobiitol ([{{PDBlink}}<ins class="diffchange diffchange-inline">1fbo </ins>1fbo])</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>* with cellohexaose ([{{PDBlink}}<del class="diffchange diffchange-inline">1FBW </del>1fbw])</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>* with cellohexaose ([{{PDBlink}}<ins class="diffchange diffchange-inline">1fbw </ins>1fbw])</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>* with a thio-oligosaccharide ([{{PDBlink}}<del class="diffchange diffchange-inline">1G9J </del>1g9j])</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>* with a thio-oligosaccharide ([{{PDBlink}}<ins class="diffchange diffchange-inline">1g9j </ins>1g9j])</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>* mutant E55Q with a thio-oligosaccharide ([{{PDBlink}}<del class="diffchange diffchange-inline">2QNO </del>2qno])</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>* mutant E55Q with a thio-oligosaccharide ([{{PDBlink}}<ins class="diffchange diffchange-inline">2qno </ins>2qno])</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>== 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="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 sterochemistry determination: ''Cellulomonas fimi'' CenE, described as an endo-β-1,4-glucanase, catalyzes the hydrolysis of cellohexaose with inversion of anomeric carbon configuration, characteristic of a single displacement reaction <cite>Shen1994 </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 sterochemistry determination: ''Cellulomonas fimi'' CenE, described as an endo-β-1,4-glucanase, catalyzes the hydrolysis of cellohexaose with inversion of anomeric carbon configuration, characteristic of a single displacement reaction <cite>Shen1994 </cite>.</div></td></tr>
</table>
Bareket Dassa