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Glycoside Hydrolase Family 65 - Revision history
2024-03-28T13:08:12Z
Revision history for this page on the wiki
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Harry Brumer: Text replacement - "\^\^\^(.*)\^\^\^" to "$1"
2021-12-18T21:18:22Z
<p>Text replacement - "\^\^\^(.*)\^\^\^" to "<a href="/index.php?title=User:$1&action=edit&redlink=1" class="new" title="User:$1 (page does not exist)">$1</a>"</p>
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 21:18, 18 December 2021</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>* [[Author]]: <del class="diffchange diffchange-inline">^^^</del>Hiroyuki Nakai<del class="diffchange diffchange-inline">^^^</del></div></td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>* [[Author]]: <ins class="diffchange diffchange-inline">[[User:</ins>Hiroyuki Nakai<ins class="diffchange diffchange-inline">|Hiroyuki Nakai]]</ins></div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>* [[Responsible Curator]]: <del class="diffchange diffchange-inline">^^^</del>Hiroyuki Nakai<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>Hiroyuki Nakai<ins class="diffchange diffchange-inline">|Hiroyuki Nakai]]</ins></div></td></tr>
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Harry Brumer
https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_65&diff=9044&oldid=prev
Harry Brumer: /* Substrate specificities */
2013-07-30T16:32:51Z
<p><span dir="auto"><span class="autocomment">Substrate specificities</span></span></p>
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 16:32, 30 July 2013</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]] belonging to [[GH65]] act on substrates containing &alpha;-glucosidic linkages. [[GH65]] contains mainly [[phosphorylases]]; maltose (Glc-&alpha;-1,4-Glc) phosphorylase (EC [{{EClink}}2.4.1.8 2.4.1.8]), trehalose (Glc-&alpha;1,&alpha;1-Glc) phosphorylase (EC [{{EClink}}2.4.1.64 2.4.1.64]), kojibiose (Glc-&alpha;-1,2-Glc) phosphorylase (EC [{{EClink}}2.4.1.230 2.4.1.230]), and trehalose 6-phosphate (Glc-&alpha;1,&alpha;1-Glc6P) phosphorylase (EC 2.4.1.-<del class="diffchange diffchange-inline">]</del>). Notably &alpha;,&alpha;-trehalases (EC [{{EClink}}3.2.1.28 3.2.1.28]), which a glycoside hydrolases, are also [[GH65]] members.</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]] belonging to [[GH65]] act on substrates containing &alpha;-glucosidic linkages. [[GH65]] contains mainly [[phosphorylases]]; maltose (Glc-&alpha;-1,4-Glc) phosphorylase (EC [{{EClink}}2.4.1.8 2.4.1.8]), trehalose (Glc-&alpha;1,&alpha;1-Glc) phosphorylase (EC [{{EClink}}2.4.1.64 2.4.1.64]), kojibiose (Glc-&alpha;-1,2-Glc) phosphorylase (EC [{{EClink}}2.4.1.230 2.4.1.230]), and trehalose 6-phosphate (Glc-&alpha;1,&alpha;1-Glc6P) phosphorylase (EC 2.4.1.-). Notably &alpha;,&alpha;-trehalases (EC [{{EClink}}3.2.1.28 3.2.1.28]), which a glycoside hydrolases, are also [[GH65]] members.</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>
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Harry Brumer
https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_65&diff=9043&oldid=prev
Harry Brumer: /* Substrate specificities */
2013-07-30T16:32:33Z
<p><span dir="auto"><span class="autocomment">Substrate specificities</span></span></p>
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<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Substrate 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]] belonging to [[GH65]] act on substrates containing &alpha;-glucosidic linkages. [[GH65]] contains mainly [[phosphorylases]]; maltose (Glc-&alpha;-1,4-Glc) phosphorylase (EC [{{EClink}}2.4.1.8 2.4.1.8]), trehalose (Glc-&alpha;1,&alpha;1-Glc) phosphorylase (EC [{{EClink}}2.4.1.64 2.4.1.64]), kojibiose (Glc-&alpha;-1,2-Glc) phosphorylase (EC [{{EClink}}2.4.1.230 2.4.1.230]), and trehalose 6-phosphate (Glc-&alpha;1,&alpha;1-Glc6P) phosphorylase (EC <del class="diffchange diffchange-inline">[{{EClink}}2.4.1.- </del>2.4.1.-]). Notably &alpha;,&alpha;-trehalases (EC [{{EClink}}3.2.1.28 3.2.1.28]), which a glycoside hydrolases, are also [[GH65]] members.</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]] belonging to [[GH65]] act on substrates containing &alpha;-glucosidic linkages. [[GH65]] contains mainly [[phosphorylases]]; maltose (Glc-&alpha;-1,4-Glc) phosphorylase (EC [{{EClink}}2.4.1.8 2.4.1.8]), trehalose (Glc-&alpha;1,&alpha;1-Glc) phosphorylase (EC [{{EClink}}2.4.1.64 2.4.1.64]), kojibiose (Glc-&alpha;-1,2-Glc) phosphorylase (EC [{{EClink}}2.4.1.230 2.4.1.230]), and trehalose 6-phosphate (Glc-&alpha;1,&alpha;1-Glc6P) phosphorylase (EC 2.4.1.-]). Notably &alpha;,&alpha;-trehalases (EC [{{EClink}}3.2.1.28 3.2.1.28]), which a glycoside hydrolases, are also [[GH65]] members.</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>
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Harry Brumer
https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_65&diff=6909&oldid=prev
Harry Brumer: /* Three-dimensional structures */ changed coloring of figure legend
2011-06-20T07:16:05Z
<p><span dir="auto"><span class="autocomment">Three-dimensional structures: </span> changed coloring of figure legend</span></p>
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 07:16, 20 June 2011</td>
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<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Three-dimensional structures ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Three-dimensional structures ==</div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>[[Image:MalPstructure.png|'''Figure 1:''' Dimer structure of ''L. brevis'' maltose phosphorylase. <del class="diffchange diffchange-inline"><span style="color:#0000ff"></del>An N-terminal complex &beta; sandwich domain is in <del class="diffchange diffchange-inline">blue</span>, </del><span style="color:#<del class="diffchange diffchange-inline">00cc00</del>">a helical linker is in <del class="diffchange diffchange-inline">green</span>, </del><span style="color:#<del class="diffchange diffchange-inline">999900</del>">an (&alpha;/&alpha;)<sub>6</sub> barrel catalytic domain is in <del class="diffchange diffchange-inline">yellow </span> and </del><span style="color:#<del class="diffchange diffchange-inline">ff0000</del>"> a C-terminal &beta; sheet domain is in <del class="diffchange diffchange-inline">red </span>. </del><span style="color:#<del class="diffchange diffchange-inline">ff00ff</del>">A phosphate molecule bound to chain B is shown as magenta <del class="diffchange diffchange-inline">spheres</del></span>.|frame|right]]</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>[[Image:MalPstructure.png|'''Figure 1:''' Dimer structure of ''L. brevis'' maltose phosphorylase. An N-terminal complex &beta; sandwich domain is in <span style="color:#<ins class="diffchange diffchange-inline">0000ff</ins>"><ins class="diffchange diffchange-inline">blue</span>, </ins>a helical linker is in <span style="color:#<ins class="diffchange diffchange-inline">00cc00</ins>"><ins class="diffchange diffchange-inline">green</span>, </ins>an (&alpha;/&alpha;)<sub>6</sub> barrel catalytic domain is in <span style="color:#<ins class="diffchange diffchange-inline">999900</ins>"><ins class="diffchange diffchange-inline">yellow</span> and </ins>a C-terminal &beta; sheet domain is in <span style="color:#<ins class="diffchange diffchange-inline">ff0000</ins>"><ins class="diffchange diffchange-inline">red </span>. </ins>A phosphate molecule bound to chain B is shown as <ins class="diffchange diffchange-inline"><span style="color:#ff00ff"></ins>magenta</span> <ins class="diffchange diffchange-inline">spheres</ins>.|frame|right]]</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>The three-dimensional structure of ''L. brevis'' maltose phosphorylase (PDB ID [{{PDBlink}}1h54 1h54]) represents the first determined in this family <cite>Egloff2001</cite>. ''L. brevis'' maltose phosphorylase is a dimeric enzyme ('''Figure 1'''). The monomer structure consists of an N-terminal complex &beta; sandwich domain, a helical linker, an (&alpha;/&alpha;)<sub>6</sub> barrel catalytic domain, and a C-terminal &beta; sheet domain. The structure of the (&alpha;/&alpha;)<sub>6</sub> barrel domain is similar to those of [[GH15]] glucoamylases (EC [{{EClink}}3.2.1.28 3.2.1.28]) <cite>Aleshin1992</cite>. [[GH15]] and [[GH65]] together constitute glycoside hydrolase [[Clan]] GH-L <cite>Cantarel2009</cite>. [[GH94]] phosphorylases and a [[GH95]] fucosidase were also shown to be structurally similar to [[GH65]] <cite>Hidaka2004 Nagae2007</cite>.</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>The three-dimensional structure of ''L. brevis'' maltose phosphorylase (PDB ID [{{PDBlink}}1h54 1h54]) represents the first determined in this family <cite>Egloff2001</cite>. ''L. brevis'' maltose phosphorylase is a dimeric enzyme ('''Figure 1'''). The monomer structure consists of an N-terminal complex &beta; sandwich domain, a helical linker, an (&alpha;/&alpha;)<sub>6</sub> barrel catalytic domain, and a C-terminal &beta; sheet domain. The structure of the (&alpha;/&alpha;)<sub>6</sub> barrel domain is similar to those of [[GH15]] glucoamylases (EC [{{EClink}}3.2.1.28 3.2.1.28]) <cite>Aleshin1992</cite>. [[GH15]] and [[GH65]] together constitute glycoside hydrolase [[Clan]] GH-L <cite>Cantarel2009</cite>. [[GH94]] phosphorylases and a [[GH95]] fucosidase were also shown to be structurally similar to [[GH65]] <cite>Hidaka2004 Nagae2007</cite>.</div></td></tr>
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Harry Brumer
https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_65&diff=6908&oldid=prev
Harry Brumer: /* Three-dimensional structures */ minor language tuning
2011-06-20T07:14:06Z
<p><span dir="auto"><span class="autocomment">Three-dimensional structures: </span> minor language tuning</span></p>
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 07:14, 20 June 2011</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>== 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>[[Image:MalPstructure.png|'''Figure 1:''' Dimer structure of ''L. brevis'' maltose phosphorylase. <span style="color:#0000ff">An N-terminal complex &beta; sandwich domain is in blue</span>, <span style="color:#00cc00">a helical linker is in green</span>, <span style="color:#999900">an (&alpha;/&alpha;)<sub>6</sub> barrel catalytic domain is in yellow </span> and <span style="color:#ff0000"> a C-terminal &beta; sheet domain is in red </span>. <span style="color:#ff00ff">A phosphate molecule bound to chain B is shown as magenta spheres</span>.|frame|right]]</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>[[Image:MalPstructure.png|'''Figure 1:''' Dimer structure of ''L. brevis'' maltose phosphorylase. <span style="color:#0000ff">An N-terminal complex &beta; sandwich domain is in blue</span>, <span style="color:#00cc00">a helical linker is in green</span>, <span style="color:#999900">an (&alpha;/&alpha;)<sub>6</sub> barrel catalytic domain is in yellow </span> and <span style="color:#ff0000"> a C-terminal &beta; sheet domain is in red </span>. <span style="color:#ff00ff">A phosphate molecule bound to chain B is shown as magenta spheres</span>.|frame|right]]</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 of ''L. brevis'' maltose phosphorylase (PDB ID [{{PDBlink}}1h54 1h54]) <del class="diffchange diffchange-inline">was firstly </del>determined <cite>Egloff2001</cite>. ''L. brevis'' maltose phosphorylase is a dimeric enzyme ('''Figure 1'''). The monomer structure consists of an N-terminal complex &beta; sandwich domain, a helical linker, an (&alpha;/&alpha;)<sub>6</sub> barrel catalytic domain, and a C-terminal &beta; sheet domain. The structure of (&alpha;/&alpha;)<sub>6</sub> barrel domain is similar to [[GH15]] <del class="diffchange diffchange-inline">glucoamylase </del>(EC [{{EClink}}3.2.1.28 3.2.1.28]) <cite>Aleshin1992</cite>. [[GH15]] and [[GH65]] together constitute glycoside hydrolase <del class="diffchange diffchange-inline">clan </del>L <cite>Cantarel2009</cite>. [[GH94]] phosphorylases and a [[GH95]] fucosidase were also shown to be structurally similar to [[GH65]] <cite>Hidaka2004 Nagae2007</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 of ''L. brevis'' maltose phosphorylase (PDB ID [{{PDBlink}}1h54 1h54]) <ins class="diffchange diffchange-inline">represents the first </ins>determined <ins class="diffchange diffchange-inline">in this family </ins><cite>Egloff2001</cite>. ''L. brevis'' maltose phosphorylase is a dimeric enzyme ('''Figure 1'''). The monomer structure consists of an N-terminal complex &beta; sandwich domain, a helical linker, an (&alpha;/&alpha;)<sub>6</sub> barrel catalytic domain, and a C-terminal &beta; sheet domain. The structure of <ins class="diffchange diffchange-inline">the </ins>(&alpha;/&alpha;)<sub>6</sub> barrel domain is similar to <ins class="diffchange diffchange-inline">those of </ins>[[GH15]] <ins class="diffchange diffchange-inline">glucoamylases </ins>(EC [{{EClink}}3.2.1.28 3.2.1.28]) <cite>Aleshin1992</cite>. [[GH15]] and [[GH65]] together constitute glycoside hydrolase <ins class="diffchange diffchange-inline">[[Clan]] GH-</ins>L <cite>Cantarel2009</cite>. [[GH94]] phosphorylases and a [[GH95]] fucosidase were also shown to be structurally similar to [[GH65]] <cite>Hidaka2004 Nagae2007</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>== 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_65&diff=6907&oldid=prev
Harry Brumer: /* Catalytic Residues */ minor language tuning
2011-06-20T07:11:11Z
<p><span dir="auto"><span class="autocomment">Catalytic Residues: </span> minor language tuning</span></p>
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 07:11, 20 June 2011</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>== 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>The [[general acid]] catalyst was first predicted by superimposing the active site structure of maltose phosphorylase from ''Lactobacillus brevis'' <cite>Egloff2001</cite> with <del class="diffchange diffchange-inline">a </del>catalytic (&alpha;/&alpha;)<sub>6</sub> barrel domain of GH15 glucoamylase (EC [{{EClink}}3.2.1.28 3.2.1.28]) from ''Aspergillus awamori'' <cite>Aleshin1992</cite>. Considering the similarities of the active site structure, Glu487 of ''L. brevis'' maltose phosphorylase was <del class="diffchange diffchange-inline">estimated as </del>the [[general acid]]. <del class="diffchange diffchange-inline">Additionally it had been proved </del>by site-direct mutagenesis <del class="diffchange diffchange-inline">on </del>Glu487 of ''Paenibacillus'' sp. maltose phosphorylase <cite>Hidaka2005</cite>, which corresponds to the Glu487 of ''L. brevis'' maltose phosphorylase. A histidine located near the phosphate (His671 in ''L. brevis'' maltose phosphorylase) <del class="diffchange diffchange-inline">could </del>assist <del class="diffchange diffchange-inline">the </del>catalysis as a [[general base]] <cite>Egloff2001</cite>, but no experimental <del class="diffchange diffchange-inline">evidences are shown</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 [[general acid]] catalyst was first predicted by superimposing the active site structure of maltose phosphorylase from ''Lactobacillus brevis'' <cite>Egloff2001</cite> with <ins class="diffchange diffchange-inline">the </ins>catalytic (&alpha;/&alpha;)<sub>6</sub> barrel domain of <ins class="diffchange diffchange-inline">a [[</ins>GH15<ins class="diffchange diffchange-inline">]] </ins>glucoamylase (EC [{{EClink}}3.2.1.28 3.2.1.28]) from ''Aspergillus awamori'' <cite>Aleshin1992</cite>. Considering the similarities of the active site structure, Glu487 of ''L. brevis'' maltose phosphorylase was <ins class="diffchange diffchange-inline">proposed to be </ins>the [[general acid]]. <ins class="diffchange diffchange-inline">Additional support for this assignment was obtained </ins>by site-direct mutagenesis <ins class="diffchange diffchange-inline">of </ins>Glu487 of ''Paenibacillus'' sp. maltose phosphorylase <cite>Hidaka2005</cite>, which corresponds to the Glu487 of ''L. brevis'' maltose phosphorylase. A histidine located near the phosphate (His671 in ''L. brevis'' maltose phosphorylase) <ins class="diffchange diffchange-inline">may </ins>assist catalysis <ins class="diffchange diffchange-inline">by acting </ins>as a [[general base]] <cite>Egloff2001</cite>, but no experimental <ins class="diffchange diffchange-inline">evidence has yet been provided</ins>.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Three-dimensional structures ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Three-dimensional structures ==</div></td></tr>
</table>
Harry Brumer
https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_65&diff=6906&oldid=prev
Harry Brumer: /* Kinetics and Mechanism */
2011-06-20T07:07:45Z
<p><span dir="auto"><span class="autocomment">Kinetics and Mechanism</span></span></p>
<table class="diff diff-contentalign-left diff-editfont-monospace" data-mw="interface">
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 07:07, 20 June 2011</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>== 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>Phosphorolysis by [[GH65]] enzymes proceeds with [[inverting|inversion]] of anomeric configuration, as first shown by Fitting and Doudoroff <cite>Fitting1952</cite> using maltose phosphorylase from ''Neisseria meningitidis'', i.e. the reaction catalyzed is: maltose + Pi &harr; &beta;-glucose 1-phosphate + glucose. The reaction mechanism for [[inverting]] [[GH65]] phosphorylase has been proposed to be similar to a [[general acid/base]]-catalysed one-step displacement mechanism for inverting [[glycoside hydrolases]] <cite>Egloff2001 Nakai2009</cite>. This mechanism involves direct nucleophilic attack by phosphate on the anomeric (C1) carbon assisted by [[general acid]] catalysis involving protonation of the glycosidic oxygen. In this mechanism, phosphate is the nucleophile, rather than a water molecule activated by a [[general base]] catalyst as in [[inverting]] [[glycoside hydrolases]]. The possibility of [[general base]] assistance in the phosphorylases of this family, via a histidine residue proximal to the phosphate nucleophile, is also suggested <cite>Egloff2001</cite>. The inverting phosphorolysis catalyzed by GH65 enzyme is readily reversible, which confers the phosphorylases with a capacity to effectively synthesize various &alpha;-glucosides from &beta;-glucose 1-phosphate as a glycosyl donor, together with various acceptor molecules. Notably &beta;-glucosyl fluoride can also be used as donor in <del class="diffchange diffchange-inline">the </del>synthetic reactions <cite>Tsumuraya1990</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>Phosphorolysis by [[GH65]] enzymes proceeds with [[inverting|inversion]] of anomeric configuration, as first shown by Fitting and Doudoroff <cite>Fitting1952</cite> using maltose phosphorylase from ''Neisseria meningitidis'', i.e. the reaction catalyzed is: maltose + Pi &harr; &beta;-glucose 1-phosphate + glucose. The reaction mechanism for [[inverting]] [[GH65]] phosphorylase has been proposed to be similar to a [[general acid/base]]-catalysed one-step displacement mechanism for inverting [[glycoside hydrolases]] <cite>Egloff2001 Nakai2009</cite>. This mechanism involves direct nucleophilic attack by phosphate on the anomeric (C1) carbon assisted by [[general acid]] catalysis involving protonation of the glycosidic oxygen. In this mechanism, phosphate is the nucleophile, rather than a water molecule activated by a [[general base]] catalyst as in [[inverting]] [[glycoside hydrolases]]. The possibility of [[general base]] assistance in the phosphorylases of this family, via a histidine residue proximal to the phosphate nucleophile, is also suggested <cite>Egloff2001</cite>. The inverting phosphorolysis catalyzed by GH65 enzyme is readily reversible, which confers the phosphorylases with a capacity to effectively synthesize various &alpha;-glucosides from &beta;-glucose 1-phosphate as a glycosyl donor, together with various acceptor molecules. Notably &beta;-glucosyl fluoride can also be used as donor in synthetic reactions <cite>Tsumuraya1990</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>
</table>
Harry Brumer
https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_65&diff=6905&oldid=prev
Harry Brumer: minor language tuning
2011-06-20T07:07:03Z
<p>minor language tuning</p>
<table class="diff diff-contentalign-left diff-editfont-monospace" data-mw="interface">
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 07:07, 20 June 2011</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]] belonging to [[GH65]] act on substrates containing &alpha;-glucosidic linkages. [[GH65]] contains mainly [[phosphorylases]]; maltose (Glc-&alpha;-1,4-Glc) phosphorylase (EC [{{EClink}}2.4.1.8 2.4.1.8]), trehalose (Glc-&alpha;1,&alpha;1-Glc) phosphorylase (EC [{{EClink}}2.4.1.64 2.4.1.64]), kojibiose (Glc-&alpha;-1,2-Glc) phosphorylase (EC [{{EClink}}2.4.1.230 2.4.1.230]), and trehalose 6-phosphate (Glc-&alpha;1,&alpha;1-Glc6P) phosphorylase (EC [{{EClink}}2.4.1.- 2.4.1.-]). <del class="diffchange diffchange-inline">Noticeably </del>&alpha;,&alpha;-trehalases (EC [{{EClink}}3.2.1.28 3.2.1.28]), a <del class="diffchange diffchange-inline">hydrolase</del>, are also [[GH65]] members.</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]] belonging to [[GH65]] act on substrates containing &alpha;-glucosidic linkages. [[GH65]] contains mainly [[phosphorylases]]; maltose (Glc-&alpha;-1,4-Glc) phosphorylase (EC [{{EClink}}2.4.1.8 2.4.1.8]), trehalose (Glc-&alpha;1,&alpha;1-Glc) phosphorylase (EC [{{EClink}}2.4.1.64 2.4.1.64]), kojibiose (Glc-&alpha;-1,2-Glc) phosphorylase (EC [{{EClink}}2.4.1.230 2.4.1.230]), and trehalose 6-phosphate (Glc-&alpha;1,&alpha;1-Glc6P) phosphorylase (EC [{{EClink}}2.4.1.- 2.4.1.-]). <ins class="diffchange diffchange-inline">Notably </ins>&alpha;,&alpha;-trehalases (EC [{{EClink}}3.2.1.28 3.2.1.28]), <ins class="diffchange diffchange-inline">which </ins>a <ins class="diffchange diffchange-inline">glycoside hydrolases</ins>, are also [[GH65]] members.</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>Phosphorolysis by [[GH65]] enzymes proceeds with [[inverting|inversion]] of anomeric configuration, as first shown by Fitting and Doudoroff <cite>Fitting1952</cite> using maltose phosphorylase from ''Neisseria meningitidis'', i.e. maltose + Pi &harr; &beta;-glucose 1-phosphate + glucose. The reaction mechanism for [[inverting]] [[GH65]] phosphorylase has been proposed to be similar to a [[general acid/base]]-catalysed one-step displacement mechanism for inverting [[glycoside hydrolases]] <cite>Egloff2001 Nakai2009</cite>. This mechanism involves direct nucleophilic attack by phosphate on the anomeric C1 carbon assisted by [[general acid]] catalysis involving protonation of the glycosidic oxygen. In this mechanism phosphate is the nucleophile, <del class="diffchange diffchange-inline">instead of </del>a water molecule activated by a [[general base]] catalyst in [[inverting]] [[glycoside hydrolases]]. <del class="diffchange diffchange-inline">Possibility </del>of [[general base]] assistance <del class="diffchange diffchange-inline">by </del>a histidine residue<del class="diffchange diffchange-inline">, which is located near </del>the phosphate, is also suggested <cite>Egloff2001</cite>. The inverting phosphorolysis catalyzed by GH65 enzyme is reversible, which confers the <del class="diffchange diffchange-inline">phosphorylase </del>with a capacity to effectively synthesize various &alpha;-glucosides from &beta;-glucose 1-phosphate as donor <del class="diffchange diffchange-inline">and </del>acceptor molecules. <del class="diffchange diffchange-inline">Noticeably </del>&beta;-glucosyl fluoride can be used as donor in the synthetic <del class="diffchange diffchange-inline">reaction instead of the &beta;-glucose 1-phosphate </del><cite>Tsumuraya1990</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>Phosphorolysis by [[GH65]] enzymes proceeds with [[inverting|inversion]] of anomeric configuration, as first shown by Fitting and Doudoroff <cite>Fitting1952</cite> using maltose phosphorylase from ''Neisseria meningitidis'', i.e. <ins class="diffchange diffchange-inline">the reaction catalyzed is: </ins>maltose + Pi &harr; &beta;-glucose 1-phosphate + glucose. The reaction mechanism for [[inverting]] [[GH65]] phosphorylase has been proposed to be similar to a [[general acid/base]]-catalysed one-step displacement mechanism for inverting [[glycoside hydrolases]] <cite>Egloff2001 Nakai2009</cite>. This mechanism involves direct nucleophilic attack by phosphate on the anomeric <ins class="diffchange diffchange-inline">(</ins>C1<ins class="diffchange diffchange-inline">) </ins>carbon assisted by [[general acid]] catalysis involving protonation of the glycosidic oxygen. In this mechanism<ins class="diffchange diffchange-inline">, </ins>phosphate is the nucleophile, <ins class="diffchange diffchange-inline">rather than </ins>a water molecule activated by a [[general base]] catalyst <ins class="diffchange diffchange-inline">as </ins>in [[inverting]] [[glycoside hydrolases]]. <ins class="diffchange diffchange-inline">The possibility </ins>of [[general base]] assistance <ins class="diffchange diffchange-inline">in the phosphorylases of this family, via </ins>a histidine residue <ins class="diffchange diffchange-inline">proximal to </ins>the phosphate <ins class="diffchange diffchange-inline">nucleophile</ins>, is also suggested <cite>Egloff2001</cite>. The inverting phosphorolysis catalyzed by GH65 enzyme is <ins class="diffchange diffchange-inline">readily </ins>reversible, which confers the <ins class="diffchange diffchange-inline">phosphorylases </ins>with a capacity to effectively synthesize various &alpha;-glucosides from &beta;-glucose 1-phosphate as <ins class="diffchange diffchange-inline">a glycosyl </ins>donor<ins class="diffchange diffchange-inline">, together with various </ins>acceptor molecules. <ins class="diffchange diffchange-inline">Notably </ins>&beta;-glucosyl fluoride can <ins class="diffchange diffchange-inline">also </ins>be used as donor in the synthetic <ins class="diffchange diffchange-inline">reactions </ins><cite>Tsumuraya1990</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>
</table>
Harry Brumer
https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_65&diff=6856&oldid=prev
Shinya Fushinobu: /* Three-dimensional structures */
2011-06-01T04:45:38Z
<p><span dir="auto"><span class="autocomment">Three-dimensional structures</span></span></p>
<table class="diff diff-contentalign-left diff-editfont-monospace" data-mw="interface">
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 04:45, 1 June 2011</td>
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<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Three-dimensional structures ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Three-dimensional structures ==</div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>[[Image:MalPstructure.png|'''Figure 1:''' Dimer structure of ''L. brevis'' maltose phosphorylase. <span style="color:#0000ff">An N-terminal complex &beta; sandwich domain is in blue</span>, <span style="color:#00cc00">a helical <del class="diffchange diffchange-inline">linkers </del>in green</span>, <span style="color:#999900">an (&alpha;/&alpha;)<sub>6</sub> barrel catalytic domain is in yellow </span> and <span style="color:#ff0000"> a C-terminal &beta; sheet domain is in red </span>. <span style="color:#ff00ff">A phosphate molecule bound to chain B is shown as magenta spheres</span>.|frame|right]]</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>[[Image:MalPstructure.png|'''Figure 1:''' Dimer structure of ''L. brevis'' maltose phosphorylase. <span style="color:#0000ff">An N-terminal complex &beta; sandwich domain is in blue</span>, <span style="color:#00cc00">a helical <ins class="diffchange diffchange-inline">linker is </ins>in green</span>, <span style="color:#999900">an (&alpha;/&alpha;)<sub>6</sub> barrel catalytic domain is in yellow </span> and <span style="color:#ff0000"> a C-terminal &beta; sheet domain is in red </span>. <span style="color:#ff00ff">A phosphate molecule bound to chain B is shown as magenta spheres</span>.|frame|right]]</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>The three-dimensional structure of ''L. brevis'' maltose phosphorylase (PDB ID [{{PDBlink}}1h54 1h54]) was firstly determined <cite>Egloff2001</cite>. ''L. brevis'' maltose phosphorylase is a dimeric enzyme ('''Figure 1'''). The monomer structure consists of an N-terminal complex &beta; sandwich domain, a helical linker, an (&alpha;/&alpha;)<sub>6</sub> barrel catalytic domain, and a C-terminal &beta; sheet domain. The structure of (&alpha;/&alpha;)<sub>6</sub> barrel domain is similar to [[GH15]] glucoamylase (EC [{{EClink}}3.2.1.28 3.2.1.28]) <cite>Aleshin1992</cite>. [[GH15]] and [[GH65]] together constitute glycoside hydrolase clan L <cite>Cantarel2009</cite>. [[GH94]] phosphorylases and a [[GH95]] fucosidase were also shown to be structurally similar to [[GH65]] <cite>Hidaka2004 Nagae2007</cite>.</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>The three-dimensional structure of ''L. brevis'' maltose phosphorylase (PDB ID [{{PDBlink}}1h54 1h54]) was firstly determined <cite>Egloff2001</cite>. ''L. brevis'' maltose phosphorylase is a dimeric enzyme ('''Figure 1'''). The monomer structure consists of an N-terminal complex &beta; sandwich domain, a helical linker, an (&alpha;/&alpha;)<sub>6</sub> barrel catalytic domain, and a C-terminal &beta; sheet domain. The structure of (&alpha;/&alpha;)<sub>6</sub> barrel domain is similar to [[GH15]] glucoamylase (EC [{{EClink}}3.2.1.28 3.2.1.28]) <cite>Aleshin1992</cite>. [[GH15]] and [[GH65]] together constitute glycoside hydrolase clan L <cite>Cantarel2009</cite>. [[GH94]] phosphorylases and a [[GH95]] fucosidase were also shown to be structurally similar to [[GH65]] <cite>Hidaka2004 Nagae2007</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>
</table>
Shinya Fushinobu
https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_65&diff=6854&oldid=prev
Shinya Fushinobu at 04:42, 1 June 2011
2011-06-01T04:42:42Z
<p></p>
<table class="diff diff-contentalign-left diff-editfont-monospace" data-mw="interface">
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 04:42, 1 June 2011</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]] belonging to [[GH65]] act on substrates containing <del class="diffchange diffchange-inline">α</del>-glucosidic linkages. [[GH65]] contains mainly [[phosphorylases]]; maltose (Glc-<del class="diffchange diffchange-inline">α</del>-1,4-Glc) phosphorylase (EC [{{EClink}}2.4.1.8 2.4.1.8]), trehalose (Glc-<del class="diffchange diffchange-inline">α1</del>,<del class="diffchange diffchange-inline">α1</del>-Glc) phosphorylase (EC [{{EClink}}2.4.1.64 2.4.1.64]), kojibiose (Glc-<del class="diffchange diffchange-inline">α</del>-1,2-Glc) phosphorylase (EC [{{EClink}}2.4.1.230 2.4.1.230]), and trehalose 6-phosphate (Glc-<del class="diffchange diffchange-inline">α1</del>,<del class="diffchange diffchange-inline">α1</del>-Glc6P) phosphorylase (EC [{{EClink}}2.4.1.- 2.4.1.-]). Noticeably <del class="diffchange diffchange-inline">α</del>,<del class="diffchange diffchange-inline">α</del>-trehalases (EC [{{EClink}}3.2.1.28 3.2.1.28]), a hydrolase, are also [[GH65]] members.</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]] belonging to [[GH65]] act on substrates containing <ins class="diffchange diffchange-inline">&alpha;</ins>-glucosidic linkages. [[GH65]] contains mainly [[phosphorylases]]; maltose (Glc-<ins class="diffchange diffchange-inline">&alpha;</ins>-1,4-Glc) phosphorylase (EC [{{EClink}}2.4.1.8 2.4.1.8]), trehalose (Glc-<ins class="diffchange diffchange-inline">&alpha;1</ins>,<ins class="diffchange diffchange-inline">&alpha;1</ins>-Glc) phosphorylase (EC [{{EClink}}2.4.1.64 2.4.1.64]), kojibiose (Glc-<ins class="diffchange diffchange-inline">&alpha;</ins>-1,2-Glc) phosphorylase (EC [{{EClink}}2.4.1.230 2.4.1.230]), and trehalose 6-phosphate (Glc-<ins class="diffchange diffchange-inline">&alpha;1</ins>,<ins class="diffchange diffchange-inline">&alpha;1</ins>-Glc6P) phosphorylase (EC [{{EClink}}2.4.1.- 2.4.1.-]). Noticeably <ins class="diffchange diffchange-inline">&alpha;</ins>,<ins class="diffchange diffchange-inline">&alpha;</ins>-trehalases (EC [{{EClink}}3.2.1.28 3.2.1.28]), a hydrolase, are also [[GH65]] members.</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>Phosphorolysis by [[GH65]] enzymes proceeds with [[inverting|inversion]] of anomeric configuration, as first shown by Fitting and Doudoroff <cite>Fitting1952</cite> using maltose phosphorylase from ''Neisseria meningitidis'', i.e. maltose + Pi <del class="diffchange diffchange-inline">↔ β</del>-glucose 1-phosphate + glucose. The reaction mechanism for [[inverting]] [[GH65]] phosphorylase has been proposed to be similar to a [[general acid/base]]-catalysed one-step displacement mechanism for inverting [[glycoside hydrolases]] <cite>Nakai2009</cite>. This mechanism <del class="diffchange diffchange-inline">was first proposed for [[inverting]] [[GH94]] phosphorylases (previously classified into glycoside transferase family 36) <cite>Hidaka2004</cite>, and </del>involves direct nucleophilic attack by phosphate on the anomeric C1 carbon assisted by [[general acid]] catalysis involving protonation of the glycosidic oxygen. In this mechanism phosphate is the nucleophile, instead of a water molecule activated by a [[general base]] catalyst in [[inverting]] [[glycoside hydrolases]]. The inverting phosphorolysis catalyzed by GH65 enzyme is reversible, which confers the phosphorylase with a capacity to effectively synthesize various <del class="diffchange diffchange-inline">α</del>-glucosides from <del class="diffchange diffchange-inline">β</del>-glucose 1-phosphate as donor and acceptor molecules. Noticeably <del class="diffchange diffchange-inline">β</del>-glucosyl fluoride can be used as donor in the synthetic reaction instead of the <del class="diffchange diffchange-inline">β</del>-glucose 1-phosphate <cite>Tsumuraya1990</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>Phosphorolysis by [[GH65]] enzymes proceeds with [[inverting|inversion]] of anomeric configuration, as first shown by Fitting and Doudoroff <cite>Fitting1952</cite> using maltose phosphorylase from ''Neisseria meningitidis'', i.e. maltose + Pi <ins class="diffchange diffchange-inline">&harr; &beta;</ins>-glucose 1-phosphate + glucose. The reaction mechanism for [[inverting]] [[GH65]] phosphorylase has been proposed to be similar to a [[general acid/base]]-catalysed one-step displacement mechanism for inverting [[glycoside hydrolases]] <cite><ins class="diffchange diffchange-inline">Egloff2001 </ins>Nakai2009</cite>. This mechanism involves direct nucleophilic attack by phosphate on the anomeric C1 carbon assisted by [[general acid]] catalysis involving protonation of the glycosidic oxygen. In this mechanism phosphate is the nucleophile, instead of a water molecule activated by a [[general base]] catalyst in [[inverting]] [[glycoside hydrolases]]<ins class="diffchange diffchange-inline">. Possibility of [[general base]] assistance by a histidine residue, which is located near the phosphate, is also suggested <cite>Egloff2001</cite></ins>. The inverting phosphorolysis catalyzed by GH65 enzyme is reversible, which confers the phosphorylase with a capacity to effectively synthesize various <ins class="diffchange diffchange-inline">&alpha;</ins>-glucosides from <ins class="diffchange diffchange-inline">&beta;</ins>-glucose 1-phosphate as donor and acceptor molecules. Noticeably <ins class="diffchange diffchange-inline">&beta;</ins>-glucosyl fluoride can be used as donor in the synthetic reaction instead of the <ins class="diffchange diffchange-inline">&beta;</ins>-glucose 1-phosphate <cite>Tsumuraya1990</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>The [[general acid]] catalyst was first predicted by superimposing the active site structure of maltose phosphorylase from ''Lactobacillus brevis'' <cite>Egloff2001</cite> with a catalytic (<del class="diffchange diffchange-inline">α</del>/<del class="diffchange diffchange-inline">α</del>)<sub>6</sub> barrel domain of GH15 glucoamylase (EC [{{EClink}}3.2.1.28 3.2.1.28]) from ''Aspergillus awamori'' <cite>Aleshin1992</cite>. Considering the similarities of the active site structure, Glu487 of ''L. brevis'' maltose phosphorylase was estimated as the [[general acid]]. Additionally it had been proved by site-direct mutagenesis on Glu487 of ''Paenibacillus'' sp. maltose phosphorylase <cite>Hidaka2005</cite>, which corresponds to the Glu487 of ''L. brevis'' maltose phosphorylase.</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 [[general acid]] catalyst was first predicted by superimposing the active site structure of maltose phosphorylase from ''Lactobacillus brevis'' <cite>Egloff2001</cite> with a catalytic (<ins class="diffchange diffchange-inline">&alpha;</ins>/<ins class="diffchange diffchange-inline">&alpha;</ins>)<sub>6</sub> barrel domain of GH15 glucoamylase (EC [{{EClink}}3.2.1.28 3.2.1.28]) from ''Aspergillus awamori'' <cite>Aleshin1992</cite>. Considering the similarities of the active site structure, Glu487 of ''L. brevis'' maltose phosphorylase was estimated as the [[general acid]]. Additionally it had been proved by site-direct mutagenesis on Glu487 of ''Paenibacillus'' sp. maltose phosphorylase <cite>Hidaka2005</cite>, which corresponds to the Glu487 of ''L. brevis'' maltose phosphorylase<ins class="diffchange diffchange-inline">. A histidine located near the phosphate (His671 in ''L. brevis'' maltose phosphorylase) could assist the catalysis as a [[general base]] <cite>Egloff2001</cite>, but no experimental evidences are shown</ins>.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Three-dimensional structures ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Three-dimensional structures ==</div></td></tr>
<tr><td class='diff-marker'>−</td><td style="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 of ''L. brevis'' maltose phosphorylase (PDB ID [{{PDBlink}}1h54 1h54]) was determined <cite>Egloff2001</cite> and <del class="diffchange diffchange-inline">shows similarities with the </del>(<del class="diffchange diffchange-inline">α</del>/<del class="diffchange diffchange-inline">α</del>)<sub>6</sub> barrel <del class="diffchange diffchange-inline">fold of </del>[[GH15]] glucoamylase (EC [{{EClink}}3.2.1.28 3.2.1.28]) <cite>Aleshin1992</cite><del class="diffchange diffchange-inline">, </del>[[<del class="diffchange diffchange-inline">GH94</del>]] <del class="diffchange diffchange-inline">cellobiose phosphorylase (EC </del>[<del class="diffchange diffchange-inline">{{EClink}}2.4.1.20 2.4.1.20</del>]<del class="diffchange diffchange-inline">) </del><cite><del class="diffchange diffchange-inline">Hidaka2006</del></cite><del class="diffchange diffchange-inline">, and </del>[[GH94]] <del class="diffchange diffchange-inline">chitobiose phosphorylase (EC [{{EClink}}2.4.1.- 2.4.1.-]) <cite>Hidaka2004</cite>. </del>[[<del class="diffchange diffchange-inline">GH15</del>]] <del class="diffchange diffchange-inline">and </del>[[GH65]] <del class="diffchange diffchange-inline">together constitute glycoside hydrolase clan L </del><cite><del class="diffchange diffchange-inline">Cantarel2009</del></cite>.</div></td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins class="diffchange diffchange-inline">[[Image:MalPstructure.png|'''Figure 1:''' Dimer structure of ''L. brevis'' maltose phosphorylase. <span style="color:#0000ff">An N-terminal complex &beta; sandwich domain is in blue</span>, <span style="color:#00cc00">a helical linkers in green</span>, <span style="color:#999900">an (&alpha;/&alpha;)<sub>6</sub> barrel catalytic domain is in yellow </span> and <span style="color:#ff0000"> a C-terminal &beta; sheet domain is in red </span>. <span style="color:#ff00ff">A phosphate molecule bound to chain B is shown as magenta spheres</span>.|frame|right]]</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>The three-dimensional structure of ''L. brevis'' maltose phosphorylase (PDB ID [{{PDBlink}}1h54 1h54]) was <ins class="diffchange diffchange-inline">firstly </ins>determined <cite>Egloff2001</cite><ins class="diffchange diffchange-inline">. ''L. brevis'' maltose phosphorylase is a dimeric enzyme ('''Figure 1'''). The monomer structure consists of an N-terminal complex &beta; sandwich domain, a helical linker, an (&alpha;/&alpha;)<sub>6</sub> barrel catalytic domain, </ins>and <ins class="diffchange diffchange-inline">a C-terminal &beta; sheet domain. The structure of </ins>(<ins class="diffchange diffchange-inline">&alpha;</ins>/<ins class="diffchange diffchange-inline">&alpha;</ins>)<sub>6</sub> barrel <ins class="diffchange diffchange-inline">domain is similar to </ins>[[GH15]] glucoamylase (EC [{{EClink}}3.2.1.28 3.2.1.28]) <cite>Aleshin1992</cite><ins class="diffchange diffchange-inline">. </ins>[[<ins class="diffchange diffchange-inline">GH15</ins>]] <ins class="diffchange diffchange-inline">and [</ins>[<ins class="diffchange diffchange-inline">GH65]</ins>] <ins class="diffchange diffchange-inline">together constitute glycoside hydrolase clan L </ins><cite><ins class="diffchange diffchange-inline">Cantarel2009</ins></cite><ins class="diffchange diffchange-inline">. </ins>[[GH94]] <ins class="diffchange diffchange-inline">phosphorylases and a </ins>[[<ins class="diffchange diffchange-inline">GH95</ins>]] <ins class="diffchange diffchange-inline">fucosidase were also shown to be structurally similar to </ins>[[GH65]] <cite><ins class="diffchange diffchange-inline">Hidaka2004 Nagae2007</ins></cite>.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Family Firsts ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Family Firsts ==</div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>;First stereochemistry determination: <del class="diffchange diffchange-inline">maltose </del>phosphorylase (EC [{{EClink}}2.4.1.8 2.4.1.8]) from ''Neisseria meningitidis'' <cite>Fitting1952</cite>.</div></td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>;First stereochemistry determination: <ins class="diffchange diffchange-inline">Maltose </ins>phosphorylase (EC [{{EClink}}2.4.1.8 2.4.1.8]) from ''Neisseria meningitidis'' <cite>Fitting1952</cite>.</div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>;First sequence identification: <del class="diffchange diffchange-inline">maltose </del>phosphorylase (EC [{{EClink}}2.4.1.8 2.4.1.8]) from ''Lactobacillus sanfranciscensis'' DSM 20451T <cite>Ehrmann1998</cite></div></td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>;First sequence identification: <ins class="diffchange diffchange-inline">Maltose </ins>phosphorylase (EC [{{EClink}}2.4.1.8 2.4.1.8]) from ''Lactobacillus sanfranciscensis'' DSM 20451T <cite>Ehrmann1998</cite></div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>: <del class="diffchange diffchange-inline">trehalose </del>phosphorylase (EC [{{EClink}}2.4.1.64 2.4.1.64]) from ''Thermoanaerobacter brockii'' ATCC 35047 <cite> Maruta2002</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">Trehalose </ins>phosphorylase (EC [{{EClink}}2.4.1.64 2.4.1.64]) from ''Thermoanaerobacter brockii'' ATCC 35047 <cite> Maruta2002</cite></div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>: <del class="diffchange diffchange-inline">kojibiose </del>phosphorylase (EC [{{EClink}}2.4.1.230 2.4.1.230]) from ''Thermoanaerobacter brockii'' ATCC 35047 <cite>Yamatomo2004</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">Kojibiose </ins>phosphorylase (EC [{{EClink}}2.4.1.230 2.4.1.230]) from ''Thermoanaerobacter brockii'' ATCC 35047 <cite>Yamatomo2004</cite></div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>: <del class="diffchange diffchange-inline">trehalose </del>6-phosphate phosphorylase (EC [{{EClink}}2.4.1.- 2.4.1.-]) from ''Lactococcus lactis'' ssp. ''lactis'' 19435 <cite> Andersson2001</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">Trehalose </ins>6-phosphate phosphorylase (EC [{{EClink}}2.4.1.- 2.4.1.-]) from ''Lactococcus lactis'' ssp. ''lactis'' 19435 <cite> Andersson2001</cite></div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>: <del class="diffchange diffchange-inline">α</del>,<del class="diffchange diffchange-inline">α</del>-<del class="diffchange diffchange-inline">trehalase </del>(EC [{{EClink}}3.2.1.28 3.2.1.28]) from ''Saccharomyces cerevisiae'' S288C <cite>Destruelle1995</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">&alpha;</ins>,<ins class="diffchange diffchange-inline">&alpha;</ins>-<ins class="diffchange diffchange-inline">Trehalase </ins>(EC [{{EClink}}3.2.1.28 3.2.1.28]) from ''Saccharomyces cerevisiae'' S288C <cite>Destruelle1995</cite>.</div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>;First [[general acid]] residue identification: <del class="diffchange diffchange-inline">maltose </del>phosphorylase (EC [{{EClink}}2.4.1.8 2.4.1.8]) from ''Lactobacillus brevis'' by X-ray structure analysis <cite>Egloff2001</cite> and confirmed by mutagenesis for ''Paenibacillus'' sp. maltose phosphorylase (EC [{{EClink}}2.4.1.8 2.4.1.8]) <cite>Hidaka2005</cite>.</div></td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>;First [[general acid]] residue identification: <ins class="diffchange diffchange-inline">Maltose </ins>phosphorylase (EC [{{EClink}}2.4.1.8 2.4.1.8]) from ''Lactobacillus brevis'' by X-ray structure analysis <cite>Egloff2001</cite> and confirmed by mutagenesis for ''Paenibacillus'' sp. maltose phosphorylase (EC [{{EClink}}2.4.1.8 2.4.1.8]) <cite>Hidaka2005</cite>.</div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>;First three-dimentional structure determination: <del class="diffchange diffchange-inline">maltose </del>phosphorylase (EC [{{EClink}}2.4.1.8 2.4.1.8]) from ''Lactobacillus brevis'' <cite>Egloff2001</cite>.</div></td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>;First three-dimentional structure determination: <ins class="diffchange diffchange-inline">Maltose </ins>phosphorylase (EC [{{EClink}}2.4.1.8 2.4.1.8]) from ''Lactobacillus brevis'' <cite>Egloff2001</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>== References ==</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>== References ==</div></td></tr>
<tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l59" >Line 59:</td>
<td colspan="2" class="diff-lineno">Line 60:</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>#Aleshin1992 pmid=1527049</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>#Aleshin1992 pmid=1527049</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>#Hidaka2005 Hidaka Y, Hatada Y, Akita M, Yoshida M, Nakamura N, Takada M, Nakakuki T, Ito S, and Horikoshi K. ''Maltose phosphorylase from a deep-sea Paenibacillus sp.: Enzymatic properties and nucleotide and amino-acid sequences.'' Enzyme and Microbial Technology, Volume 37, Issue 2, 1 July 2005, Pages 185-194. [http://dx.doi.org/10.1016/j.enzmictec.2005.02.010 doi:10.1016/j.enzmictec.2005.02.010]</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>#Hidaka2005 Hidaka Y, Hatada Y, Akita M, Yoshida M, Nakamura N, Takada M, Nakakuki T, Ito S, and Horikoshi K. ''Maltose phosphorylase from a deep-sea Paenibacillus sp.: Enzymatic properties and nucleotide and amino-acid sequences.'' Enzyme and Microbial Technology, Volume 37, Issue 2, 1 July 2005, Pages 185-194. [http://dx.doi.org/10.1016/j.enzmictec.2005.02.010 doi:10.1016/j.enzmictec.2005.02.010]</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;">#Hidaka2006 pmid=16646954</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>#Cantarel2009 pmid=18838391</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>#Cantarel2009 pmid=18838391</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;">#Nagae2007 pmid=17459873</ins></div></td></tr>
<tr><td colspan="2"> </td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;"></ins></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>#Ehrmann1998 pmid=9851037</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>#Ehrmann1998 pmid=9851037</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>#Maruta2002 pmid=12400703</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>#Maruta2002 pmid=12400703</div></td></tr>
</table>
Shinya Fushinobu