https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_141&feed=atom&action=history
Glycoside Hydrolase Family 141 - Revision history
2024-03-29T13:37:55Z
Revision history for this page on the wiki
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Harry Brumer: Text replacement - "\^\^\^(.*)\^\^\^" to "$1"
2021-12-18T21:18:57Z
<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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<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>Harry Gilbert<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>Harry Gilbert<ins class="diffchange diffchange-inline">|Harry Gilbert]]</ins></div></td></tr>
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Harry Brumer
https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_141&diff=12519&oldid=prev
Spencer Williams at 21:49, 16 February 2018
2018-02-16T21:49:57Z
<p></p>
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 21:49, 16 February 2018</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 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>Glycoside hydrolases of family 141 display α-L-fucosidase ([{{EClink}}3.2.1.51 EC 3.2.1.51]) <cite>Ndeh2017</cite> or xylanase ([{{EClink}}3.2.1.8 EC 3.2.1.8]) <cite>Heinze2017</cite>activities. The ''Bacteroides thetaiotaomicron'' enzyme BT1002 <del class="diffchange diffchange-inline">was </del>the founding member of this family. <del class="diffchange diffchange-inline">The </del>enzyme cleaves the fucosodic linkage in 2-O-methyl-D-<del class="diffchange diffchange-inline">xylose</del>-α-1,3-L-<del class="diffchange diffchange-inline">fucose</del>-&alpha;1,4-L-Rhap, a component of <del class="diffchange diffchange-inline">Chain </del>B of rhamnogalacturonan II, a complex pectin conserved in the primary cell walls <cite>Ndeh2017</cite>. Recently, an endo-xylanase from ''Clostridium thermocellum'' (Xyn141E) was also described. Xyn141E is active against a range of xylans, displaying low level <del class="diffchange diffchange-inline">side </del>activity against other &beta;1,4-glycans such as carboxymethyl cellulose, barley beta glucan and ivory nut mannan <cite>Heinze2017</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">[[</ins>Glycoside hydrolases<ins class="diffchange diffchange-inline">]] </ins>of family 141 display α-L-fucosidase ([{{EClink}}3.2.1.51 EC 3.2.1.51]) <cite>Ndeh2017</cite> or xylanase ([{{EClink}}3.2.1.8 EC 3.2.1.8]) <cite>Heinze2017</cite> activities. The ''Bacteroides thetaiotaomicron'' enzyme BT1002 <ins class="diffchange diffchange-inline">is </ins>the founding member of this family. <ins class="diffchange diffchange-inline">This </ins>enzyme cleaves the fucosodic linkage in 2-<ins class="diffchange diffchange-inline">''</ins>O<ins class="diffchange diffchange-inline">''</ins>-methyl-D-<ins class="diffchange diffchange-inline">xylosyl</ins>-α-1,3-L-<ins class="diffchange diffchange-inline">fucosyl</ins>-&alpha;1,4-L-Rhap, a component of <ins class="diffchange diffchange-inline">chain </ins>B of rhamnogalacturonan II, a complex pectin conserved in the primary cell walls <ins class="diffchange diffchange-inline">of plants </ins><cite>Ndeh2017</cite>. Recently, an <ins class="diffchange diffchange-inline">''</ins>endo<ins class="diffchange diffchange-inline">''</ins>-xylanase from ''Clostridium thermocellum'' (Xyn141E) was also described. Xyn141E is active against a range of xylans, displaying low level activity against other &beta;1,4-glycans such as carboxymethyl cellulose, barley beta glucan and ivory nut mannan <cite>Heinze2017</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>== Kinetics 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>== Kinetics 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>Very little is known about the kinetics or mechanism of <del class="diffchange diffchange-inline">GH141 </del>enzymes. However, in the BT1002 crystal structure, the distance of 6.1 Å between the catalytic residues suggests that members of this family may be retaining enzymes and follow a double displacement mechanism <cite>Ndeh2017</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>Very little is known about the kinetics or mechanism of <ins class="diffchange diffchange-inline">family 141 </ins>enzymes. However, in the BT1002 crystal structure, the distance of 6.1 Å between the catalytic residues suggests that members of this family may be retaining enzymes and follow a double displacement mechanism <cite>Ndeh2017</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 ==</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 ==</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>In the <del class="diffchange diffchange-inline">BT1002 </del>crystal structure, two aspartates (Asp523 and Asp564), which are highly conserved and located within the active site pocket, are the proposed catalytic residues. Site directed mutagenesis of these amino acids abolished the catalytic activity of BT1002 indicating the essential role in catalysis. Additionally, the structural location of the catalytic residues suggests that Asp523 (at the base of the pocket) acts as catalytic nucleophile and Asp564 (at the lip of the active site) is the general acid-base residue <cite>Ndeh2017</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>In the <ins class="diffchange diffchange-inline">X-ray </ins>crystal structure <ins class="diffchange diffchange-inline">of ''B. thetaiotaomicron'' BT1002</ins>, two aspartates (Asp523 and Asp564), which are highly conserved and located within the active site pocket, are the proposed catalytic residues. Site directed mutagenesis of these amino acids abolished the catalytic activity of BT1002 indicating the essential role in catalysis. Additionally, the structural location of the catalytic residues suggests that Asp523 (at the base of the pocket) acts as catalytic nucleophile and Asp564 (at the lip of the active site) is the general acid-base residue <cite>Ndeh2017</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="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:BT1002.png|thumb|300px|right|'''Figure 1.''' '''BT1002 strucutre'''. ([{{PDBlink}}5MQP PDB ID 5PDB]) The figure shows the β-parallel catalytic domain (purple) and the additional β-sandwich domain (yellow)]]</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:BT1002.png|thumb|300px|right|'''Figure 1.''' '''BT1002 strucutre'''. ([{{PDBlink}}5MQP PDB ID 5PDB]) The figure shows the β-parallel catalytic domain (purple) and the additional β-sandwich domain (yellow)]]</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 three-dimensional structure has been <del class="diffchange diffchange-inline">solved </del>for ''B. thetaiotaomicron'' BT1002 at 2 Å ([{{PDBlink}}5MQP PDB ID 5PDB]). The protein has two domains: a N-terminal β-sandwich and a C-terminal catalytic domain that folds into a right-handed parallel &beta;-helix . The overall fold displays similarity to members of [[Polysaccharide Lyase Family 1]] and [[Glycoside Hydrolase Family 28]]<del class="diffchange diffchange-inline">. </del>(Figure 1) <cite>Ndeh2017</cite>. The active site pocket is in a similar location to the catalytic centre of GH120 &beta;-xylosidases <cite>Huang2012</cite>, which also displays the same fold as the GH141 enzyme BT1002. The catalytic resisdues identified in the GH120 &beta;-xylosidase <cite>Cecchini2015</cite>, however, are not conserved in the GH141 &alpha;-L-fucosidase.</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 three-dimensional structure has been <ins class="diffchange diffchange-inline">determined </ins>for ''B. thetaiotaomicron'' BT1002 at 2 Å ([{{PDBlink}}5MQP PDB ID 5PDB]). The protein has two domains: a N-terminal β-sandwich and a C-terminal catalytic domain that folds into a right-handed parallel &beta;-helix . The overall fold displays similarity to members of [[Polysaccharide Lyase Family 1]] and [[Glycoside Hydrolase Family 28]] (Figure 1) <cite>Ndeh2017</cite>. The active site pocket is in a similar location to the catalytic centre of GH120 &beta;-xylosidases <cite>Huang2012</cite>, which also displays the same fold as the GH141 enzyme BT1002. The catalytic resisdues identified in the GH120 &beta;-xylosidase <cite>Cecchini2015</cite>, however, are not conserved in the GH141 &alpha;-L-fucosidase.</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>
</table>
Spencer Williams
https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_141&diff=12458&oldid=prev
Harry Brumer: /* Three-dimensional structures */ fixed links
2018-02-14T09:03:08Z
<p><span dir="auto"><span class="autocomment">Three-dimensional structures: </span> fixed links</span></p>
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 09:03, 14 February 2018</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> [[File:BT1002.png|thumb|300px|right|'''Figure 1.''' '''BT1002 strucutre'''. ([{{PDBlink}}5MQP PDB ID 5PDB]) The figure shows the β-parallel catalytic domain (purple) and the additional β-sandwich domain (yellow)]]</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:BT1002.png|thumb|300px|right|'''Figure 1.''' '''BT1002 strucutre'''. ([{{PDBlink}}5MQP PDB ID 5PDB]) The figure shows the β-parallel catalytic domain (purple) and the additional β-sandwich domain (yellow)]]</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 three-dimensional structure has been solved for ''B. thetaiotaomicron'' BT1002 at 2 Å ([{{PDBlink}}5MQP PDB ID 5PDB]). The protein has two domains: a N-terminal β-sandwich and a C-terminal catalytic domain that folds into a right-handed parallel &beta;-helix . The overall fold displays similarity to members of <del class="diffchange diffchange-inline">polysaccharide lyase family 1 (</del>[[<del class="diffchange diffchange-inline">PL1</del>]]<del class="diffchange diffchange-inline">) </del>and <del class="diffchange diffchange-inline">glycoside hydrolase family 28 (</del>[[<del class="diffchange diffchange-inline">GH28</del>]]<del class="diffchange diffchange-inline">)</del>. (Figure 1) <cite>Ndeh2017</cite>. The active site pocket is in a similar location to the catalytic centre of GH120 &beta;-xylosidases <cite>Huang2012</cite>, which also displays the same fold as the GH141 enzyme BT1002. The catalytic resisdues identified in the GH120 &beta;-xylosidase <cite>Cecchini2015</cite>, however, are not conserved in the GH141 &alpha;-L-fucosidase. <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>The three-dimensional structure has been solved for ''B. thetaiotaomicron'' BT1002 at 2 Å ([{{PDBlink}}5MQP PDB ID 5PDB]). The protein has two domains: a N-terminal β-sandwich and a C-terminal catalytic domain that folds into a right-handed parallel &beta;-helix . The overall fold displays similarity to members of [[<ins class="diffchange diffchange-inline">Polysaccharide Lyase Family 1</ins>]] and [[<ins class="diffchange diffchange-inline">Glycoside Hydrolase Family 28</ins>]]. (Figure 1) <cite>Ndeh2017</cite>. The active site pocket is in a similar location to the catalytic centre of GH120 &beta;-xylosidases <cite>Huang2012</cite>, which also displays the same fold as the GH141 enzyme BT1002. The catalytic resisdues identified in the GH120 &beta;-xylosidase <cite>Cecchini2015</cite>, however, are not conserved in the GH141 &alpha;-L-fucosidase.</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>
</table>
Harry Brumer
https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_141&diff=12457&oldid=prev
Harry Brumer: fixed links
2018-02-14T09:01:33Z
<p>fixed links</p>
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<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 09:01, 14 February 2018</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="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;"><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --></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;"><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="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]]: ^^^Ana Luis^^^</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]]: ^^^Ana Luis^^^</div></td></tr>
<tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l29" >Line 29:</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 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>Glycoside hydrolases of family 141 <del class="diffchange diffchange-inline">([http://www.cazy.org/GH141.html CAZy]) </del>display α-L-fucosidase ([<del class="diffchange diffchange-inline">http://www.enzyme-database.org/query.php?ec=</del>3.2.1.51 EC 3.2.1.51]) <cite>Ndeh2017</cite> or xylanase ([<del class="diffchange diffchange-inline">http://www.enzyme-database.org/query.php?ec=</del>3.2.1.8 EC 3.2.1.8]) <cite>Heinze2017</cite>activities. The ''Bacteroides thetaiotaomicron'' enzyme BT1002 was the founding member of this family. The enzyme cleaves the fucosodic linkage in 2-O-methyl-D-xylose-α-1,3-L-fucose-&alpha;1,4-L-Rhap, a component of Chain B of rhamnogalacturonan II, a complex pectin conserved in the primary cell walls <cite>Ndeh2017</cite>. Recently, an endo-xylanase from ''Clostridium thermocellum'' (Xyn141E) was also described. Xyn141E is active against a range of xylans, displaying low level side activity against other &beta;1,4-glycans such as carboxymethyl cellulose, barley beta glucan and ivory nut mannan <cite>Heinze2017</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>Glycoside hydrolases of family 141 display α-L-fucosidase ([<ins class="diffchange diffchange-inline">{{EClink}}</ins>3.2.1.51 EC 3.2.1.51]) <cite>Ndeh2017</cite> or xylanase ([<ins class="diffchange diffchange-inline">{{EClink}}</ins>3.2.1.8 EC 3.2.1.8]) <cite>Heinze2017</cite>activities. The ''Bacteroides thetaiotaomicron'' enzyme BT1002 was the founding member of this family. The enzyme cleaves the fucosodic linkage in 2-O-methyl-D-xylose-α-1,3-L-fucose-&alpha;1,4-L-Rhap, a component of Chain B of rhamnogalacturonan II, a complex pectin conserved in the primary cell walls <cite>Ndeh2017</cite>. Recently, an endo-xylanase from ''Clostridium thermocellum'' (Xyn141E) was also described. Xyn141E is active against a range of xylans, displaying low level side activity against other &beta;1,4-glycans such as carboxymethyl cellulose, barley beta glucan and ivory nut mannan <cite>Heinze2017</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>== Kinetics 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>== Kinetics and Mechanism ==</div></td></tr>
<tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l38" >Line 38:</td>
<td colspan="2" class="diff-lineno">Line 37:</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> [[File:BT1002.png|thumb|300px|right|'''Figure 1.''' '''BT1002 strucutre'''. ([<del class="diffchange diffchange-inline">https://www.rcsb.org/structure/</del>5MQP PDB ID 5PDB]) The figure shows the β-parallel catalytic domain (purple) and the additional β-sandwich domain (yellow)]]</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:BT1002.png|thumb|300px|right|'''Figure 1.''' '''BT1002 strucutre'''. ([<ins class="diffchange diffchange-inline">{{PDBlink}}</ins>5MQP PDB ID 5PDB]) The figure shows the β-parallel catalytic domain (purple) and the additional β-sandwich domain (yellow)]]</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 three-dimensional structure has been solved for ''B. thetaiotaomicron'' BT1002 at 2 Å ([<del class="diffchange diffchange-inline">https://www.rcsb.org/structure/</del>5MQP PDB ID 5PDB]). The protein has two domains: a N-terminal β-sandwich and a C-terminal catalytic domain that folds into a right-handed parallel &beta;-helix . The overall fold displays similarity to members of polysaccharide lyase family 1 ([[PL1]]) and glycoside hydrolase family 28 ([[GH28]]). (Figure 1) <cite>Ndeh2017</cite>. The active site pocket is in a similar location to the catalytic centre of GH120 &beta;-xylosidases <cite>Huang2012</cite>, which also displays the same fold as the GH141 enzyme BT1002. The catalytic resisdues identified in the GH120 &beta;-xylosidase <cite>Cecchini2015</cite>, however, are not conserved in the GH141 &alpha;-L-fucosidase. </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 three-dimensional structure has been solved for ''B. thetaiotaomicron'' BT1002 at 2 Å ([<ins class="diffchange diffchange-inline">{{PDBlink}}</ins>5MQP PDB ID 5PDB]). The protein has two domains: a N-terminal β-sandwich and a C-terminal catalytic domain that folds into a right-handed parallel &beta;-helix . The overall fold displays similarity to members of polysaccharide lyase family 1 ([[PL1]]) and glycoside hydrolase family 28 ([[GH28]]). (Figure 1) <cite>Ndeh2017</cite>. The active site pocket is in a similar location to the catalytic centre of GH120 &beta;-xylosidases <cite>Huang2012</cite>, which also displays the same fold as the GH141 enzyme BT1002. The catalytic resisdues identified in the GH120 &beta;-xylosidase <cite>Cecchini2015</cite>, however, are not conserved in the GH141 &alpha;-L-fucosidase. </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>
<tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l52" >Line 52:</td>
<td colspan="2" class="diff-lineno">Line 51:</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>#Ndeh2017 pmid=28329766</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>#Ndeh2017 pmid=28329766</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>#Heinze2017 pmid=28894250</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>#Heinze2017 pmid=28894250</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="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>#Huang2012 pmid=22992047</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>#Huang2012 pmid=22992047</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="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>#Cecchini2015 pmid=26297820</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>#Cecchini2015 pmid=26297820</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|GH141]]</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|GH141]]</div></td></tr>
</table>
Harry Brumer
https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_141&diff=12435&oldid=prev
Harry Gilbert at 18:32, 13 February 2018
2018-02-13T18:32:17Z
<p></p>
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<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 18:32, 13 February 2018</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="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]]: ^^^Ana Luis^^^</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]]: ^^^Ana Luis^^^</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]]: ^^^Harry Gilbert^^^</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]]: ^^^Harry Gilbert^^^</div></td></tr>
<tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l29" >Line 29:</td>
<td colspan="2" class="diff-lineno">Line 29:</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>Glycoside hydrolases of family 141 ([http://www.cazy.org/GH141.html CAZy]) display α-L-fucosidase ([http://www.enzyme-database.org/query.php?ec=3.2.1.51 EC 3.2.1.51]) <cite>Ndeh2017</cite> or xylanase ([http://www.enzyme-database.org/query.php?ec=3.2.1.8 EC 3.2.1.8]) <cite>Heinze2017</cite>activities. The ''Bacteroides thetaiotaomicron'' enzyme BT1002 was the founding member of this family. The enzyme cleaves the fucosodic linkage in 2-O-methyl-D-xylose-α-1,3-L-fucose-&alpha;1,4-L-Rhap, a component of Chain B of rhamnogalacturonan II, a complex pectin conserved in the primary cell walls <cite>Ndeh2017</cite>. Recently, an endo-xylanase from ''Clostridium thermocellum'' (Xyn141E) was also described. Xyn141E is active against a range of xylans, displaying <del class="diffchange diffchange-inline">lowl elvel </del>side activity against other &beta;1,4-glycans such as carboxymethyl cellulose, barley beta glucan and <del class="diffchange diffchange-inline">mannan from </del>ivory nut <cite>Heinze2017</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>Glycoside hydrolases of family 141 ([http://www.cazy.org/GH141.html CAZy]) display α-L-fucosidase ([http://www.enzyme-database.org/query.php?ec=3.2.1.51 EC 3.2.1.51]) <cite>Ndeh2017</cite> or xylanase ([http://www.enzyme-database.org/query.php?ec=3.2.1.8 EC 3.2.1.8]) <cite>Heinze2017</cite>activities. The ''Bacteroides thetaiotaomicron'' enzyme BT1002 was the founding member of this family. The enzyme cleaves the fucosodic linkage in 2-O-methyl-D-xylose-α-1,3-L-fucose-&alpha;1,4-L-Rhap, a component of Chain B of rhamnogalacturonan II, a complex pectin conserved in the primary cell walls <cite>Ndeh2017</cite>. Recently, an endo-xylanase from ''Clostridium thermocellum'' (Xyn141E) was also described. Xyn141E is active against a range of xylans, displaying <ins class="diffchange diffchange-inline">low level </ins>side activity against other &beta;1,4-glycans such as carboxymethyl cellulose, barley beta glucan and ivory nut <ins class="diffchange diffchange-inline">mannan </ins><cite>Heinze2017</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>== Kinetics 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>== Kinetics and Mechanism ==</div></td></tr>
<tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l40" >Line 40:</td>
<td colspan="2" class="diff-lineno">Line 40:</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:BT1002.png|thumb|300px|right|'''Figure 1.''' '''BT1002 strucutre'''. ([https://www.rcsb.org/structure/5MQP PDB ID 5PDB]) The figure shows the β-parallel catalytic domain (purple) and the additional β-sandwich domain (yellow)]]</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:BT1002.png|thumb|300px|right|'''Figure 1.''' '''BT1002 strucutre'''. ([https://www.rcsb.org/structure/5MQP PDB ID 5PDB]) The figure shows the β-parallel catalytic domain (purple) and the additional β-sandwich domain (yellow)]]</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 three-dimensional structure has been solved for ''B. thetaiotaomicron'' BT1002 at 2 Å ([https://www.rcsb.org/structure/5MQP PDB ID 5PDB]). The protein has two domains: a N-terminal β-sandwich and a C-terminal catalytic domain that folds into a right-handed parallel &beta;-helix . The overall fold displays similarity to members of polysaccharide lyase family 1 ([[PL1]]) and glycoside hydrolase family 28 ([[GH28]]). (Figure 1) <cite>Ndeh2017</cite>. The active site pocket is in a similar location to the catalytic centre of GH120 &beta;-xylosidases <cite>Huang2012</cite>. The catalytic resisdues identified in the GH120 &beta;-xylosidase <cite>Cecchini2015</cite>, however, are not conserved in the GH141 &alpha;-L-fucosidase. </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 three-dimensional structure has been solved for ''B. thetaiotaomicron'' BT1002 at 2 Å ([https://www.rcsb.org/structure/5MQP PDB ID 5PDB]). The protein has two domains: a N-terminal β-sandwich and a C-terminal catalytic domain that folds into a right-handed parallel &beta;-helix . The overall fold displays similarity to members of polysaccharide lyase family 1 ([[PL1]]) and glycoside hydrolase family 28 ([[GH28]]). (Figure 1) <cite>Ndeh2017</cite>. The active site pocket is in a similar location to the catalytic centre of GH120 &beta;-xylosidases <cite>Huang2012</cite><ins class="diffchange diffchange-inline">, which also displays the same fold as the GH141 enzyme BT1002</ins>. The catalytic resisdues identified in the GH120 &beta;-xylosidase <cite>Cecchini2015</cite>, however, are not conserved in the GH141 &alpha;-L-fucosidase. </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>
</table>
Harry Gilbert
https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_141&diff=12434&oldid=prev
Harry Gilbert at 18:29, 13 February 2018
2018-02-13T18:29:08Z
<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 18:29, 13 February 2018</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l40" >Line 40:</td>
<td colspan="2" class="diff-lineno">Line 40:</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:BT1002.png|thumb|300px|right|'''Figure 1.''' '''BT1002 strucutre'''. ([https://www.rcsb.org/structure/5MQP PDB ID 5PDB]) The figure shows the β-parallel catalytic domain (purple) and the additional β-sandwich domain (yellow)]]</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:BT1002.png|thumb|300px|right|'''Figure 1.''' '''BT1002 strucutre'''. ([https://www.rcsb.org/structure/5MQP PDB ID 5PDB]) The figure shows the β-parallel catalytic domain (purple) and the additional β-sandwich domain (yellow)]]</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 three-dimensional structure has been solved for ''B. thetaiotaomicron'' BT1002 at 2 Å ([https://www.rcsb.org/structure/5MQP PDB ID 5PDB]). The protein has two domains: a N-terminal β-sandwich and a C-terminal catalytic domain that folds into a right-handed parallel &beta;-helix . The overall fold displays similarity to members of polysaccharide lyase family 1 ([[PL1]]) and glycoside hydrolase family 28 ([[GH28]]). (Figure 1) <cite>Ndeh2017</cite>. The active site pocket is in a similar location to the catalytic centre of GH120 &beta;-xylosidases <cite>Huang2012</cite>. The catalytic resisdues identified in the GH120 &beta;-xylosidase, however, are not conserved in the <del class="diffchange diffchange-inline">Gh141 </del>&alpha;-L-fucosidase <del class="diffchange diffchange-inline">talytic residues identified in a GH120 in are not conserved in </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>The three-dimensional structure has been solved for ''B. thetaiotaomicron'' BT1002 at 2 Å ([https://www.rcsb.org/structure/5MQP PDB ID 5PDB]). The protein has two domains: a N-terminal β-sandwich and a C-terminal catalytic domain that folds into a right-handed parallel &beta;-helix . The overall fold displays similarity to members of polysaccharide lyase family 1 ([[PL1]]) and glycoside hydrolase family 28 ([[GH28]]). (Figure 1) <cite>Ndeh2017</cite>. The active site pocket is in a similar location to the catalytic centre of GH120 &beta;-xylosidases <cite>Huang2012</cite>. The catalytic resisdues identified in the GH120 &beta;-xylosidase <ins class="diffchange diffchange-inline"><cite>Cecchini2015</cite></ins>, however, are not conserved in the <ins class="diffchange diffchange-inline">GH141 </ins>&alpha;-L-fucosidase<ins class="diffchange diffchange-inline">. </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>
<tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l54" >Line 54:</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>#Huang2012 pmid=22992047</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>#Huang2012 pmid=22992047</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 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;">#Cecchini2015 pmid=26297820</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|GH141]]</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|GH141]]</div></td></tr>
</table>
Harry Gilbert
https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_141&diff=12433&oldid=prev
Harry Gilbert at 18:25, 13 February 2018
2018-02-13T18:25:47Z
<p></p>
<table class="diff diff-contentalign-left diff-editfont-monospace" data-mw="interface">
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<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 18:25, 13 February 2018</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l39" >Line 39:</td>
<td colspan="2" class="diff-lineno">Line 39:</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> [[File:BT1002.png|thumb|300px|right|'''Figure 1.''' '''BT1002 strucutre'''. ([https://www.rcsb.org/structure/5MQP PDB ID 5PDB]) The figure shows the β-parallel catalytic domain (purple) and the additional β-sandwich domain (yellow)]]</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:BT1002.png|thumb|300px|right|'''Figure 1.''' '''BT1002 strucutre'''. ([https://www.rcsb.org/structure/5MQP PDB ID 5PDB]) The figure shows the β-parallel catalytic domain (purple) and the additional β-sandwich domain (yellow)]]</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>The three-dimensional structure has been solved for ''B. thetaiotaomicron'' BT1002 at 2 Å ([https://www.rcsb.org/structure/5MQP PDB ID 5PDB]). The protein has two domains: a N-terminal β-sandwich and a C-terminal catalytic domain that folds into a right-handed parallel &beta;-helix . The overall fold displays similarity to members of polysaccharide lyase family 1 ([[PL1]]) and glycoside hydrolase family 28 ([[GH28]]). (Figure 1) <cite>Ndeh2017</cite>. The active site pocket is in a similar location to the catalytic centre of GH120 &beta;-xylosidases <cite></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> </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>The three-dimensional structure has been solved for ''B. thetaiotaomicron'' BT1002 at 2 Å ([https://www.rcsb.org/structure/5MQP PDB ID 5PDB]). The protein has two domains: a N-terminal β-sandwich and a C-terminal catalytic domain that folds into a right-handed parallel &beta;-helix . The overall fold displays similarity to members of polysaccharide lyase family 1 ([[PL1]]) and glycoside hydrolase family 28 ([[GH28]]). (Figure 1) <cite>Ndeh2017</cite>. The active site pocket is in a similar location to the catalytic centre of GH120 &beta;-xylosidases <cite><ins class="diffchange diffchange-inline">Huang2012</ins></cite><ins class="diffchange diffchange-inline">. The catalytic resisdues identified in the GH120 &beta;-xylosidase, however, are not conserved in the Gh141 &alpha;-L-fucosidase talytic residues identified in a GH120 in are not conserved in </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>
<tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l51" >Line 51:</td>
<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>#Ndeh2017 pmid=28329766</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>#Ndeh2017 pmid=28329766</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>#Heinze2017 pmid=28894250</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>#Heinze2017 pmid=28894250</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 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;">#Huang2012 pmid=22992047</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|GH141]]</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|GH141]]</div></td></tr>
</table>
Harry Gilbert
https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_141&diff=12432&oldid=prev
Harry Gilbert at 18:19, 13 February 2018
2018-02-13T18:19:23Z
<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 18:19, 13 February 2018</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l39" >Line 39:</td>
<td colspan="2" class="diff-lineno">Line 39:</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> [[File:BT1002.png|thumb|300px|right|'''Figure 1.''' '''BT1002 strucutre'''. ([https://www.rcsb.org/structure/5MQP PDB ID 5PDB]) The figure shows the β-parallel catalytic domain (purple) and the additional β-sandwich domain (yellow)]]</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:BT1002.png|thumb|300px|right|'''Figure 1.''' '''BT1002 strucutre'''. ([https://www.rcsb.org/structure/5MQP PDB ID 5PDB]) The figure shows the β-parallel catalytic domain (purple) and the additional β-sandwich domain (yellow)]]</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>The three-dimensional structure has been solved for ''B. thetaiotaomicron'' BT1002 at 2 Å ([https://www.rcsb.org/structure/5MQP PDB ID 5PDB]). The protein has two domains: a N-terminal β-sandwich and a C-terminal <del class="diffchange diffchange-inline">β</del>-parallel <del class="diffchange diffchange-inline">helical catalytic domain </del>(Figure 1) <cite>Ndeh2017</cite>. The active site pocket is in a similar location to the catalytic centre of GH120 &beta;-xylosidases </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 three-dimensional structure has been solved for ''B. thetaiotaomicron'' BT1002 at 2 Å ([https://www.rcsb.org/structure/5MQP PDB ID 5PDB]). The protein has two domains: a N-terminal β-sandwich and a C-terminal <ins class="diffchange diffchange-inline">catalytic domain that folds into a right</ins>-<ins class="diffchange diffchange-inline">handed </ins>parallel <ins class="diffchange diffchange-inline">&beta;-helix . The overall fold displays similarity to members of polysaccharide lyase family 1 ([[PL1]]) and glycoside hydrolase family 28 ([[GH28]]). </ins>(Figure 1) <cite>Ndeh2017</cite>. The active site pocket is in a similar location to the catalytic centre of GH120 &beta;-xylosidases <ins class="diffchange diffchange-inline"><cite></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>== 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 Gilbert
https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_141&diff=12431&oldid=prev
Harry Gilbert at 18:15, 13 February 2018
2018-02-13T18:15:11Z
<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 18:15, 13 February 2018</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l29" >Line 29:</td>
<td colspan="2" class="diff-lineno">Line 29:</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>Glycoside hydrolases of family 141 ([http://www.cazy.org/GH141.html CAZy]) display α-L-fucosidase ([http://www.enzyme-database.org/query.php?ec=3.2.1.51 EC 3.2.1.51]) or xylanase ([http://www.enzyme-database.org/query.php?ec=3.2.1.8 EC 3.2.1.8]) activities. The ''Bacteroides thetaiotaomicron'' enzyme BT1002 was the founding member of this family. The enzyme cleaves the fucosodic linkage in 2-O-methyl-D-xylose-α-1,3-L-fucose-&alpha;1,4-L-Rhap <del class="diffchange diffchange-inline">linkages in </del>Chain B of rhamnogalacturonan II, a complex pectin conserved in the primary cell walls <cite>Ndeh2017</cite>. Recently, an endo-xylanase from ''Clostridium thermocellum'' (Xyn141E) was also described. Xyn141E is <del class="diffchange diffchange-inline">most </del>active against <del class="diffchange diffchange-inline">arabinoxylan. However</del>, <del class="diffchange diffchange-inline">this enzyme also displays </del>side <del class="diffchange diffchange-inline">activities </del>against carboxymethyl cellulose, barley beta glucan and mannan from ivory nut <cite>Heinze2017</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>Glycoside hydrolases of family 141 ([http://www.cazy.org/GH141.html CAZy]) display α-L-fucosidase ([http://www.enzyme-database.org/query.php?ec=3.2.1.51 EC 3.2.1.51]) <ins class="diffchange diffchange-inline"><cite>Ndeh2017</cite> </ins>or xylanase ([http://www.enzyme-database.org/query.php?ec=3.2.1.8 EC 3.2.1.8]) <ins class="diffchange diffchange-inline"><cite>Heinze2017</cite></ins>activities. The ''Bacteroides thetaiotaomicron'' enzyme BT1002 was the founding member of this family. The enzyme cleaves the fucosodic linkage in 2-O-methyl-D-xylose-α-1,3-L-fucose-&alpha;1,4-L-Rhap<ins class="diffchange diffchange-inline">, a component of </ins>Chain B of rhamnogalacturonan II, a complex pectin conserved in the primary cell walls <cite>Ndeh2017</cite>. Recently, an endo-xylanase from ''Clostridium thermocellum'' (Xyn141E) was also described. Xyn141E is active against <ins class="diffchange diffchange-inline">a range of xylans</ins>, <ins class="diffchange diffchange-inline">displaying lowl elvel </ins>side <ins class="diffchange diffchange-inline">activity </ins>against <ins class="diffchange diffchange-inline">other &beta;1,4-glycans such as </ins>carboxymethyl cellulose, barley beta glucan and mannan from ivory nut <cite>Heinze2017</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>== Kinetics 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>== Kinetics and Mechanism ==</div></td></tr>
<tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l35" >Line 35:</td>
<td colspan="2" class="diff-lineno">Line 35:</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 ==</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 ==</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>In BT1002 structure, two aspartates (<del class="diffchange diffchange-inline">Asp 523 </del>and Asp564) located within the active site pocket are the catalytic residues. Site directed mutagenesis of these <del class="diffchange diffchange-inline">residues </del>abolished the catalytic activity of BT1002 indicating the essential role in catalysis. Additionally, the structural location of the catalytic residues suggests that Asp523 (at the base of the pocket) acts as catalytic nucleophile and Asp564 (at the lip of the active site) is the general acid-base residue <cite>Ndeh2017</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>In <ins class="diffchange diffchange-inline">the </ins>BT1002 <ins class="diffchange diffchange-inline">crystal </ins>structure, two aspartates (<ins class="diffchange diffchange-inline">Asp523 </ins>and Asp564)<ins class="diffchange diffchange-inline">, which are highly conserved and </ins>located within the active site pocket<ins class="diffchange diffchange-inline">, </ins>are the <ins class="diffchange diffchange-inline">proposed </ins>catalytic residues. Site directed mutagenesis of these <ins class="diffchange diffchange-inline">amino acids </ins>abolished the catalytic activity of BT1002 indicating the essential role in catalysis. Additionally, the structural location of the catalytic residues suggests that Asp523 (at the base of the pocket) acts as catalytic nucleophile and Asp564 (at the lip of the active site) is the general acid-base residue <cite>Ndeh2017</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="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:BT1002.png|thumb|300px|right|'''Figure 1.''' '''BT1002 strucutre'''. ([https://www.rcsb.org/structure/5MQP PDB ID 5PDB]) The figure shows the β-parallel catalytic domain (purple) and the additional β-sandwich domain (yellow)]]</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:BT1002.png|thumb|300px|right|'''Figure 1.''' '''BT1002 strucutre'''. ([https://www.rcsb.org/structure/5MQP PDB ID 5PDB]) The figure shows the β-parallel catalytic domain (purple) and the additional β-sandwich domain (yellow)]]</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>The three-dimensional structure has been solved for ''B. thetaiotaomicron'' BT1002 at 2 Å ([https://www.rcsb.org/structure/5MQP PDB ID 5PDB]). The protein has two domains: a N-terminal β-sandwich and a C-terminal β-parallel catalytic domain (Figure 1) <cite>Ndeh2017</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>The three-dimensional structure has been solved for ''B. thetaiotaomicron'' BT1002 at 2 Å ([https://www.rcsb.org/structure/5MQP PDB ID 5PDB]). The protein has two domains: a N-terminal β-sandwich and a C-terminal β-parallel <ins class="diffchange diffchange-inline">helical </ins>catalytic domain (Figure 1) <cite>Ndeh2017</cite>. <ins class="diffchange diffchange-inline">The active site pocket is in a similar location to the catalytic centre of GH120 &beta;-xylosidases </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>
</table>
Harry Gilbert
https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_141&diff=12430&oldid=prev
Harry Gilbert at 17:36, 13 February 2018
2018-02-13T17:36:35Z
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 17:36, 13 February 2018</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 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>Glycoside hydrolases of family 141 ([http://www.cazy.org/GH141.html CAZy]) display α-L-fucosidase ([http://www.enzyme-database.org/query.php?ec=3.2.1.51 EC 3.2.1.51]) or xylanase ([http://www.enzyme-database.org/query.php?ec=3.2.1.8 EC 3.2.1.8]) activities. The ''Bacteroides thetaiotaomicron'' enzyme BT1002 was the founding member of this family. The enzyme cleaves 2-O-methyl-D-xylose-α-1,3-L-fucose <del class="diffchange diffchange-inline">from </del>rhamnogalacturonan II, a complex pectin conserved in the primary cell walls <cite>Ndeh2017</cite>. Recently, an endo-xylanase from ''Clostridium thermocellum'' (Xyn141E) was also described. Xyn141E is most active against arabinoxylan. However, this enzyme also displays side activities against carboxymethyl cellulose, barley beta glucan and mannan from ivory nut <cite>Heinze2017</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>Glycoside hydrolases of family 141 ([http://www.cazy.org/GH141.html CAZy]) display α-L-fucosidase ([http://www.enzyme-database.org/query.php?ec=3.2.1.51 EC 3.2.1.51]) or xylanase ([http://www.enzyme-database.org/query.php?ec=3.2.1.8 EC 3.2.1.8]) activities. The ''Bacteroides thetaiotaomicron'' enzyme BT1002 was the founding member of this family. The enzyme cleaves <ins class="diffchange diffchange-inline">the fucosodic linkage in </ins>2-O-methyl-D-xylose-α-1,3-L-fucose<ins class="diffchange diffchange-inline">-&alpha;1,4-L-Rhap linkages in Chain B of </ins>rhamnogalacturonan II, a complex pectin conserved in the primary cell walls <cite>Ndeh2017</cite>. Recently, an endo-xylanase from ''Clostridium thermocellum'' (Xyn141E) was also described. Xyn141E is most active against arabinoxylan. However, this enzyme also displays side activities against carboxymethyl cellulose, barley beta glucan and mannan from ivory nut <cite>Heinze2017</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>== Kinetics 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>== Kinetics 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>Very little is known about the kinetics or mechanism of GH141 enzymes. However, in BT1002 crystal structure, the distance of 6.1 Å between the catalytic residues suggests that members of this family may be retaining enzymes and follow a double displacement mechanism <cite>Ndeh2017</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>Very little is known about the kinetics or mechanism of GH141 enzymes. However, in <ins class="diffchange diffchange-inline">the </ins>BT1002 crystal structure, the distance of 6.1 Å between the catalytic residues suggests that members of this family may be retaining enzymes and follow a double displacement mechanism <cite>Ndeh2017</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 ==</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 ==</div></td></tr>
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Harry Gilbert