https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_103&feed=atom&action=history
Glycoside Hydrolase Family 103 - Revision history
2024-03-28T10:52:54Z
Revision history for this page on the wiki
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Harry Brumer: Text replacement - "\^\^\^(.*)\^\^\^" to "$1"
2021-12-18T21:16:07Z
<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>* [[Author]]: <del class="diffchange diffchange-inline">^^^</del>Anthony Clarke<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>Anthony Clarke<ins class="diffchange diffchange-inline">|Anthony Clarke]]</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>Anthony Clarke<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>Anthony Clarke<ins class="diffchange diffchange-inline">|Anthony Clarke]]</ins></div></td></tr>
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Harry Brumer
https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_103&diff=7530&oldid=prev
Harry Brumer: updated CAZyDBlink
2012-09-10T16:45:48Z
<p>updated CAZyDBlink</p>
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</table>
Harry Brumer
https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_103&diff=4478&oldid=prev
Spencer Williams: /* Catalytic Residues */
2010-04-20T12:20:03Z
<p><span dir="auto"><span class="autocomment">Catalytic Residues</span></span></p>
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 12:20, 20 April 2010</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>[[Image:MltBmechanism.jpg|thumb|right|'''Figure 2.''' Reaction mechanism proposed for ''E. coli'' and ''P. aeruginosa'' MltB. (''click to enlarge'').]]As with other lytic transglycosylases (families [[GH23]], [[GH102]], and [[GH104]]), the GH103 enzymes are thought to possess a single catalytic [[general acid/base]] residue. This residue has been identified as Glu162 in MltB from both ''E. coli'' and ''P. aeruginosa'' and, indeed, its replacement abolishes catalytic activity <cite>4 5</cite>. The mechanism of action of family GH103 enzymes has been investigated the most compared to the lytic transglycosylases of the other families ([[GH23]],[[GH102]], and [[GH104]]). </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:MltBmechanism.jpg|thumb|right|'''Figure 2.''' Reaction mechanism proposed for ''E. coli'' and ''P. aeruginosa'' MltB. (''click to enlarge'').]]As with other lytic transglycosylases (families [[GH23]], [[GH102]], and [[GH104]]), the GH103 enzymes are thought to possess a single catalytic [[general acid/base]] residue. This residue has been identified as Glu162 in MltB from both ''E. coli'' and ''P. aeruginosa'' and, indeed, its replacement abolishes catalytic activity <cite>4 5</cite>. The mechanism of action of family GH103 enzymes has been investigated the most compared to the lytic transglycosylases of the other families ([[GH23]],[[GH102]], and [[GH104]]). </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>Examination of crystal structures of ''E. coli'' Slt35 (a soluble proteolytic derivative of MltB) and theoretical considerations led to the proposal of a mechanism that accommodates a single catalytic residue at its active site. Thus, based on the complexes formed with murodipeptide, chitobiose, and the inhibitor bulgecin, a two-step [[neighboring group participation]] mechanism involving substrate-assisted catalysis has been invoked analogous to the family [[GH18]] chitinases and chitobiases, family [[GH20]] ''N''-acetyl-β-hexosaminidases, and family [[GH23]] lytic transglycosylases <cite>6</cite>. Thus, the catalytic residue Glu162 is proposed to serve initially as a [[general acid]] to donate a proton to the glycosidic oxygen of the linkage to be cleaved. At the same time the MurNAc 2-acetamido group acts as a nucleophile and attacks the anomeric centre. The [[transition state]] leading to the [[intermediate]] possesses oxocarbenium ion character (Figure 2). In the second step abstraction of the C-6 hydroxyl proton of the oxazolinium species by Glu162 which now serves as a [[general base]] leads to nucleophilic attack and the formation of 1,6-anhydromuramic acid product, again through a [[transition state]] with [[oxocarbenium ion]] character. The β-hexosaminidase inhibitor NAG-thiazoline (Figure 2) was found to inhibit ''P. aeruginosa'' MltB thus supporting the proposal for the formation of an oxazolinium ion [[intermediate]] <cite>7</cite>, and the results of a site-directed mutagenesis study suggest that Ser216 orients the N-acetyl group on MurNAc at the -1 subsite of MltB for its participation in a substrate-assisted mechanism of action <cite>8</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>Examination of crystal structures of ''E. coli'' Slt35 (a soluble proteolytic derivative of MltB) and theoretical considerations led to the proposal of a mechanism that accommodates a single catalytic residue at its active site. Thus, based on the complexes formed with murodipeptide, chitobiose, and the inhibitor bulgecin, a two-step [[neighboring group participation]] mechanism involving substrate-assisted catalysis has been invoked analogous to the family [[GH18]] chitinases and chitobiases, family [[GH20]] ''N''-acetyl-β-hexosaminidases, and family [[GH23]] lytic transglycosylases <cite>6</cite>. Thus, the catalytic residue Glu162 is proposed to serve initially as a [[general acid]] to donate a proton to the glycosidic oxygen of the linkage to be cleaved. At the same time the MurNAc 2-acetamido group acts as a nucleophile and attacks the anomeric centre. The [[transition state]] leading to the [[intermediate]] possesses <ins class="diffchange diffchange-inline">[[</ins>oxocarbenium ion<ins class="diffchange diffchange-inline">]] </ins>character (Figure 2). In the second step abstraction of the C-6 hydroxyl proton of the oxazolinium species by Glu162 which now serves as a [[general base]] leads to nucleophilic attack and the formation of 1,6-anhydromuramic acid product, again through a [[transition state]] with [[oxocarbenium ion]] character. The β-hexosaminidase inhibitor NAG-thiazoline (Figure 2) was found to inhibit ''P. aeruginosa'' MltB thus supporting the proposal for the formation of an <ins class="diffchange diffchange-inline">[[</ins>oxazolinium ion<ins class="diffchange diffchange-inline">]] </ins>[[intermediate]] <cite>7</cite>, and the results of a site-directed mutagenesis study suggest that Ser216 orients the N-acetyl group on MurNAc at the -1 subsite of MltB for its participation in a substrate-assisted mechanism of action <cite>8</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>
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Spencer Williams
https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_103&diff=4476&oldid=prev
Spencer Williams: /* Family Firsts */
2010-04-20T12:17:22Z
<p><span dir="auto"><span class="autocomment">Family Firsts</span></span></p>
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 12:17, 20 April 2010</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l46" >Line 46:</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>== Family Firsts ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Family Firsts ==</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>;First identification of lytic transglycosylase: MltB from ''E. coli'' <cite>2</cite>.</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>;First identification of lytic transglycosylase: MltB from ''E. coli'' <cite>2</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 [[catalytic nucleophile]] identification: Uses [[neighboring group participation <del class="diffchange diffchange-inline">mechanism</del>]].</div></td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>;First [[catalytic nucleophile]] identification: Uses [[neighboring group participation]] <ins class="diffchange diffchange-inline">mechanism</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>;First [[general acid/base]] residue identification: Inferred by X-ray crystallography of ''E. coli'' MltB <cite>5</cite>.</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>;First [[general acid/base]] residue identification: Inferred by X-ray crystallography of ''E. coli'' MltB <cite>5</cite>.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>;First 3-D structure: ''E. coli'' MltB <cite>5</cite>.</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>;First 3-D structure: ''E. coli'' MltB <cite>5</cite>.</div></td></tr>
</table>
Spencer Williams
https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_103&diff=4475&oldid=prev
Spencer Williams: /* Catalytic Residues */
2010-04-20T12:16:58Z
<p><span dir="auto"><span class="autocomment">Catalytic Residues</span></span></p>
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 12:16, 20 April 2010</td>
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<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>[[Image:MltBmechanism.jpg|thumb|right|'''Figure 2.''' Reaction mechanism proposed for ''E. coli'' and ''P. aeruginosa'' MltB. (''click to enlarge'').]]As with other lytic transglycosylases (families [[GH23]], [[GH102]], and [[GH104]]), the GH103 enzymes are thought to possess a single catalytic [[general acid/base]] residue. This residue has been identified as Glu162 in MltB from both ''E. coli'' and ''P. aeruginosa'' and, indeed, its replacement abolishes catalytic activity <cite>4 5</cite>. The mechanism of action of family GH103 enzymes has been investigated the most compared to the lytic transglycosylases of the other families ([[GH23]],[[GH102]], and [[GH104]]). </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:MltBmechanism.jpg|thumb|right|'''Figure 2.''' Reaction mechanism proposed for ''E. coli'' and ''P. aeruginosa'' MltB. (''click to enlarge'').]]As with other lytic transglycosylases (families [[GH23]], [[GH102]], and [[GH104]]), the GH103 enzymes are thought to possess a single catalytic [[general acid/base]] residue. This residue has been identified as Glu162 in MltB from both ''E. coli'' and ''P. aeruginosa'' and, indeed, its replacement abolishes catalytic activity <cite>4 5</cite>. The mechanism of action of family GH103 enzymes has been investigated the most compared to the lytic transglycosylases of the other families ([[GH23]],[[GH102]], and [[GH104]]). </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>Examination of crystal structures of ''E. coli'' Slt35 (a soluble proteolytic derivative of MltB) and theoretical considerations led to the proposal of a mechanism that accommodates a single catalytic residue at its active site. Thus, based on the complexes formed with murodipeptide, chitobiose, and the inhibitor bulgecin, a two-step [[neighboring group participation <del class="diffchange diffchange-inline">mechanism</del>]] involving substrate-assisted catalysis has been invoked analogous to the family [[GH18]] chitinases and chitobiases, family [[GH20]] ''N''-acetyl-β-hexosaminidases, and family [[GH23]] lytic transglycosylases <cite>6</cite>. Thus, the catalytic residue Glu162 is proposed to serve initially as a [[general acid]] to donate a proton to the glycosidic oxygen of the linkage to be cleaved. At the same time the MurNAc 2-acetamido group acts as a nucleophile and attacks the anomeric centre. The [[transition state]] leading to the [[intermediate]] possesses oxocarbenium ion character (Figure 2). In the second step abstraction of the C-6 hydroxyl proton of the oxazolinium species by Glu162 which now serves as a [[general base]] leads to nucleophilic attack and the formation of 1,6-anhydromuramic acid product, again through a [[transition state]] with [[oxocarbenium ion]] character. The β-hexosaminidase inhibitor NAG-thiazoline (Figure 2) was found to inhibit ''P. aeruginosa'' MltB thus supporting the proposal for the formation of an oxazolinium ion [[intermediate]] <cite>7</cite>, and the results of a site-directed mutagenesis study suggest that Ser216 orients the N-acetyl group on MurNAc at the -1 subsite of MltB for its participation in a substrate-assisted mechanism of action <cite>8</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>Examination of crystal structures of ''E. coli'' Slt35 (a soluble proteolytic derivative of MltB) and theoretical considerations led to the proposal of a mechanism that accommodates a single catalytic residue at its active site. Thus, based on the complexes formed with murodipeptide, chitobiose, and the inhibitor bulgecin, a two-step [[neighboring group participation]] <ins class="diffchange diffchange-inline">mechanism </ins>involving substrate-assisted catalysis has been invoked analogous to the family [[GH18]] chitinases and chitobiases, family [[GH20]] ''N''-acetyl-β-hexosaminidases, and family [[GH23]] lytic transglycosylases <cite>6</cite>. Thus, the catalytic residue Glu162 is proposed to serve initially as a [[general acid]] to donate a proton to the glycosidic oxygen of the linkage to be cleaved. At the same time the MurNAc 2-acetamido group acts as a nucleophile and attacks the anomeric centre. The [[transition state]] leading to the [[intermediate]] possesses oxocarbenium ion character (Figure 2). In the second step abstraction of the C-6 hydroxyl proton of the oxazolinium species by Glu162 which now serves as a [[general base]] leads to nucleophilic attack and the formation of 1,6-anhydromuramic acid product, again through a [[transition state]] with [[oxocarbenium ion]] character. The β-hexosaminidase inhibitor NAG-thiazoline (Figure 2) was found to inhibit ''P. aeruginosa'' MltB thus supporting the proposal for the formation of an oxazolinium ion [[intermediate]] <cite>7</cite>, and the results of a site-directed mutagenesis study suggest that Ser216 orients the N-acetyl group on MurNAc at the -1 subsite of MltB for its participation in a substrate-assisted mechanism of action <cite>8</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>
</table>
Spencer Williams
https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_103&diff=4473&oldid=prev
Spencer Williams at 12:15, 20 April 2010
2010-04-20T12:15:50Z
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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 12:15, 20 April 2010</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l31" >Line 31:</td>
<td colspan="2" class="diff-lineno">Line 31:</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>[[Image:LTreaction.jpg|thumb|right|'''Figure 1.''' Reaction catalyzed by family GH103 enzymes. LT, lytic transglycosylase. (''click to enlarge'').]]The glycoside hydrolases of this family are lytic <del class="diffchange diffchange-inline">transglyosylases </del>(also referred to as peptidoglycan lyases) of bacterial origin and they constitute family 3 of the classification scheme of Blackburn and Clarke <cite>1</cite>. The prototype for this family is membrane-bound lytic transglycosylase B (MltB) from ''Escherichia coli'' <cite>2</cite>. These enzymes cleave the β-1,4 linkage between ''N''-acetylmuramoyl and ''N''-acetylglucosaminyl residues in peptidoglycan (Figure 1)<del class="diffchange diffchange-inline">, </del> No other activities have been observed.</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:LTreaction.jpg|thumb|right|'''Figure 1.''' Reaction catalyzed by family GH103 enzymes. LT, lytic transglycosylase. (''click to enlarge'').]]The <ins class="diffchange diffchange-inline">[[</ins>glycoside hydrolases<ins class="diffchange diffchange-inline">]] </ins>of this family are <ins class="diffchange diffchange-inline">in fact </ins>lytic <ins class="diffchange diffchange-inline">transglycosylases </ins>(also referred to as peptidoglycan lyases) of bacterial origin and they constitute family 3 of the classification scheme of Blackburn and Clarke <cite>1</cite>. The prototype for this family is membrane-bound lytic transglycosylase B (MltB) from ''Escherichia coli'' <cite>2</cite>. These enzymes cleave the β-1,4 linkage between ''N''-acetylmuramoyl and ''N''-acetylglucosaminyl residues in peptidoglycan (Figure 1)<ins class="diffchange diffchange-inline">. </ins> No other activities have been observed.</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>The lytic transglycosidases, strictly speaking, are retaining enzymes. However, they are not hydrolases but rather catalyse an intramolecular glycosyl <del class="diffchange diffchange-inline">transferase </del>reaction onto the C-6 hydroxyl group of the muramoyl residue leading to the generation of a terminal 1,6-<del class="diffchange diffchange-inline">anhdyromuramoyl </del>product (Figure 1) <del class="diffchange diffchange-inline">thus lacking </del>a reducing end <cite>3</cite>. No detailed analyses involving both steady state and pre-steady state kinetic studies have been reported, but the Michaelis Menten (''K''<sub>M</sub> and ''V''<sub>max</sub>) parameters have been estimated for ''Pseudomonas aeruginosa'' MltB acting on insoluble peptidoglycan sacculi <cite>4</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 lytic transglycosidases, strictly speaking, are <ins class="diffchange diffchange-inline">[[</ins>retaining<ins class="diffchange diffchange-inline">]] </ins>enzymes. However, they are not hydrolases but rather catalyse an intramolecular glycosyl <ins class="diffchange diffchange-inline">transfer </ins>reaction onto the C-6 hydroxyl group of the muramoyl residue leading to the generation of a terminal 1,6-<ins class="diffchange diffchange-inline">anhydromuramoyl </ins>product (Figure 1) <ins class="diffchange diffchange-inline">that lacks </ins>a reducing end <cite>3</cite>. No detailed analyses involving both steady state and pre-steady state kinetic studies have been reported, but the Michaelis<ins class="diffchange diffchange-inline">-</ins>Menten (''K''<sub>M</sub> and ''V''<sub>max</sub>) parameters have been estimated for ''Pseudomonas aeruginosa'' MltB acting on insoluble peptidoglycan sacculi <cite>4</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>[[Image:MltBmechanism.jpg|thumb|right|'''Figure 2.''' Reaction mechanism proposed for ''E. coli'' and ''P. aeruginosa'' MltB. (''click to enlarge'').]]As with other lytic transglycosylases (families [[GH23]], [[GH102]], and [[GH104]]), the GH103 enzymes are thought to possess a single catalytic acid/base residue. This residue has been identified as Glu162 in MltB from both ''E. coli'' and ''P. aeruginosa'' and, indeed, its replacement abolishes catalytic activity <cite>4 5</cite>. The mechanism of action of family GH103 enzymes has been investigated the most compared to the lytic transglycosylases of the other families ([[GH23]],[[GH102]], and [[GH104]]). </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:MltBmechanism.jpg|thumb|right|'''Figure 2.''' Reaction mechanism proposed for ''E. coli'' and ''P. aeruginosa'' MltB. (''click to enlarge'').]]As with other lytic transglycosylases (families [[GH23]], [[GH102]], and [[GH104]]), the GH103 enzymes are thought to possess a single catalytic <ins class="diffchange diffchange-inline">[[general </ins>acid/base<ins class="diffchange diffchange-inline">]] </ins>residue. This residue has been identified as Glu162 in MltB from both ''E. coli'' and ''P. aeruginosa'' and, indeed, its replacement abolishes catalytic activity <cite>4 5</cite>. The mechanism of action of family GH103 enzymes has been investigated the most compared to the lytic transglycosylases of the other families ([[GH23]],[[GH102]], and [[GH104]]). </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>Examination of crystal structures of ''E. coli'' Slt35 (a soluble proteolytic derivative of MltB) and theoretical considerations led to the proposal of a mechanism that accommodates a single catalytic at its active site. Thus, based on the complexes formed with murodipeptide, chitobiose, and the inhibitor bulgecin, a <del class="diffchange diffchange-inline"> </del>substrate-assisted <del class="diffchange diffchange-inline">mechanism </del>has been invoked analogous to the family [[GH18]] chitinases and chitobiases, family [[GH20]] ''N''-acetyl-β-hexosaminidases, and family [[GH23]] lytic transglycosylases <cite>6</cite>. Thus, the catalytic Glu162 is proposed to serve initially as <del class="diffchange diffchange-inline">an </del>acid <del class="diffchange diffchange-inline">catalyst </del>to donate a proton to the glycosidic oxygen of the linkage to be cleaved leading to the <del class="diffchange diffchange-inline">formation of an </del>intermediate <del class="diffchange diffchange-inline">with </del>oxocarbenium ion character (Figure 2). <del class="diffchange diffchange-inline"> </del>In the <del class="diffchange diffchange-inline">absence of an anion/nucleophile in close proximity to stabilize this oxocarbenium intermediate, the lytic transglycosylases would employ anchimeric assistance of the MurNAc 2-acetamido group resulting in the formation an oxazolinium ion intermediate. This would be followed by </del>abstraction of the C-6 hydroxyl proton of the oxazolinium species <del class="diffchange diffchange-inline">involving </del>Glu162 which now serves as <del class="diffchange diffchange-inline">the </del>base <del class="diffchange diffchange-inline">catalyst leading </del>to nucleophilic attack and the formation of 1,6-anhydromuramic acid product. The β-hexosaminidase inhibitor NAG-thiazoline (Figure 2) was found to inhibit ''P. aeruginosa'' MltB thus supporting the proposal for the formation of an oxazolinium ion intermediate <cite>7</cite>, and the results of a site-directed mutagenesis study suggest that Ser216 orients the N-acetyl group on MurNAc at the -1 subsite of MltB for its participation in a substrate-assisted mechanism of action <cite>8</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>Examination of crystal structures of ''E. coli'' Slt35 (a soluble proteolytic derivative of MltB) and theoretical considerations led to the proposal of a mechanism that accommodates a single catalytic <ins class="diffchange diffchange-inline">residue </ins>at its active site. Thus, based on the complexes formed with murodipeptide, chitobiose, and the inhibitor bulgecin, a <ins class="diffchange diffchange-inline">two-step [[neighboring group participation mechanism]] involving </ins>substrate-assisted <ins class="diffchange diffchange-inline">catalysis </ins>has been invoked analogous to the family [[GH18]] chitinases and chitobiases, family [[GH20]] ''N''-acetyl-β-hexosaminidases, and family [[GH23]] lytic transglycosylases <cite>6</cite>. Thus, the catalytic <ins class="diffchange diffchange-inline">residue </ins>Glu162 is proposed to serve initially as <ins class="diffchange diffchange-inline">a [[general </ins>acid<ins class="diffchange diffchange-inline">]] </ins>to donate a proton to the glycosidic oxygen of the linkage to be cleaved<ins class="diffchange diffchange-inline">. At the same time the MurNAc 2-acetamido group acts as a nucleophile and attacks the anomeric centre. The [[transition state]] </ins>leading to the <ins class="diffchange diffchange-inline">[[</ins>intermediate<ins class="diffchange diffchange-inline">]] possesses </ins>oxocarbenium ion character (Figure 2). In the <ins class="diffchange diffchange-inline">second step </ins>abstraction of the C-6 hydroxyl proton of the oxazolinium species <ins class="diffchange diffchange-inline">by </ins>Glu162 which now serves as <ins class="diffchange diffchange-inline">a [[general </ins>base<ins class="diffchange diffchange-inline">]] leads </ins>to nucleophilic attack and the formation of 1,6-anhydromuramic acid product<ins class="diffchange diffchange-inline">, again through a [[transition state]] with [[oxocarbenium ion]] character</ins>. The β-hexosaminidase inhibitor NAG-thiazoline (Figure 2) was found to inhibit ''P. aeruginosa'' MltB thus supporting the proposal for the formation of an oxazolinium ion <ins class="diffchange diffchange-inline">[[</ins>intermediate<ins class="diffchange diffchange-inline">]] </ins><cite>7</cite>, and the results of a site-directed mutagenesis study suggest that Ser216 orients the N-acetyl group on MurNAc at the -1 subsite of MltB for its participation in a substrate-assisted mechanism of action <cite>8</cite>.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Three-dimensional structures ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Three-dimensional structures ==</div></td></tr>
<tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l46" >Line 46:</td>
<td colspan="2" class="diff-lineno">Line 46:</td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Family Firsts ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Family Firsts ==</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>;First identification of lytic transglycosylase: MltB from ''E. coli'' <cite>2</cite>.</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>;First identification of lytic transglycosylase: MltB from ''E. coli'' <cite>2</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 catalytic nucleophile identification: <del class="diffchange diffchange-inline">Not applicable for lytic transglycosylases</del>.</div></td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>;First <ins class="diffchange diffchange-inline">[[</ins>catalytic nucleophile<ins class="diffchange diffchange-inline">]] </ins>identification: <ins class="diffchange diffchange-inline">Uses [[neighboring group participation mechanism]]</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>;First general acid/base residue identification: Inferred by X-ray crystallography of ''E. coli'' MltB <cite>5</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 <ins class="diffchange diffchange-inline">[[</ins>general acid/base<ins class="diffchange diffchange-inline">]] </ins>residue identification: Inferred by X-ray crystallography of ''E. coli'' MltB <cite>5</cite>.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>;First 3-D structure: ''E. coli'' MltB <cite>5</cite>.</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>;First 3-D structure: ''E. coli'' MltB <cite>5</cite>.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>;First identification as a lipoprotein: ''E. coli'' MltB <cite>9</cite>.</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>;First identification as a lipoprotein: ''E. coli'' MltB <cite>9</cite>.</div></td></tr>
</table>
Spencer Williams
https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_103&diff=4099&oldid=prev
Harry Brumer at 17:50, 22 February 2010
2010-02-22T17:50:41Z
<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;">← Older revision</td>
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 17:50, 22 February 2010</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l9" >Line 9:</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>{| {{Prettytable}} </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>{| {{Prettytable}} </div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|-</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|-</div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family <del class="diffchange diffchange-inline">GHnn</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>|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family <ins class="diffchange diffchange-inline">GH103</ins>'''</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|-</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|-</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|'''Clan''' </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>|'''Clan''' </div></td></tr>
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<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|-</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|-</div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>| colspan="2" |http://www.cazy.org/fam/<del class="diffchange diffchange-inline">GHnn</del>.html</div></td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>| colspan="2" |http://www.cazy.org/fam/<ins class="diffchange diffchange-inline">GH103</ins>.html</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|}</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|}</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div></div></div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div></div></div></td></tr>
</table>
Harry Brumer
https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_103&diff=4098&oldid=prev
Harry Brumer at 17:50, 22 February 2010
2010-02-22T17:50:10Z
<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 17:50, 22 February 2010</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;"><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="background-color: #f8f9fa; color: #202122; font-size: 88%; 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 lytic transglycosidases, strictly speaking, are retaining enzymes. However, they are not hydrolases but rather catalyse an intramolecular glycosyl transferase reaction onto the C-6 hydroxyl group of the muramoyl residue leading to the generation of a terminal 1,6-anhdyromuramoyl product (Figure 1) thus lacking a reducing end <cite>3</cite>. No detailed analyses involving both steady state and pre-steady state kinetic studies have been reported, but the Michaelis Menten (''K''<sub>M</sub> and ''V''<sub>max</sub>) parameters have been estimated for ''Pseudomonas aeruginosa'' MltB acting on insoluble peptidoglycan sacculi <cite>4</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 lytic transglycosidases, strictly speaking, are retaining enzymes. However, they are not hydrolases but rather catalyse an intramolecular glycosyl transferase reaction onto the C-6 hydroxyl group of the muramoyl residue leading to the generation of a terminal 1,6-anhdyromuramoyl product (Figure 1) thus lacking a reducing end <cite>3</cite>. No detailed analyses involving both steady state and pre-steady state kinetic studies have been reported, but the Michaelis Menten (''K''<sub>M</sub> and ''V''<sub>max</sub>) parameters have been estimated for ''Pseudomonas aeruginosa'' MltB acting on insoluble peptidoglycan sacculi <cite>4</cite>.</div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div><del style="font-weight: bold; text-decoration: none;"></del></div></td><td colspan="2"> </td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 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 colspan="2" class="diff-lineno" id="mw-diff-left-l41" >Line 41:</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;"></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>Examination of crystal structures of ''E. coli'' Slt35 (a soluble proteolytic derivative of MltB) and theoretical considerations led to the proposal of a mechanism that accommodates a single catalytic at its active site. Thus, based on the complexes formed with murodipeptide, chitobiose, and the inhibitor bulgecin, a substrate-assisted mechanism has been invoked analogous to the family [[GH18]] chitinases and chitobiases, family [[GH20]] ''N''-acetyl-β-hexosaminidases, and family [[GH23]] lytic transglycosylases <cite>6</cite>. Thus, the catalytic Glu162 is proposed to serve initially as an acid catalyst to donate a proton to the glycosidic oxygen of the linkage to be cleaved leading to the formation of an intermediate with oxocarbenium ion character (Figure 2). In the absence of an anion/nucleophile in close proximity to stabilize this oxocarbenium intermediate, the lytic transglycosylases would employ anchimeric assistance of the MurNAc 2-acetamido group resulting in the formation an oxazolinium ion intermediate. This would be followed by abstraction of the C-6 hydroxyl proton of the oxazolinium species involving Glu162 which now serves as the base catalyst leading to nucleophilic attack and the formation of 1,6-anhydromuramic acid product. The β-hexosaminidase inhibitor NAG-thiazoline (Figure 2) was found to inhibit ''P. aeruginosa'' MltB thus supporting the proposal for the formation of an oxazolinium ion intermediate <cite>7</cite>, and the results of a site-directed mutagenesis study suggest that Ser216 orients the N-acetyl group on MurNAc at the -1 subsite of MltB for its participation in a substrate-assisted mechanism of action <cite>8</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>Examination of crystal structures of ''E. coli'' Slt35 (a soluble proteolytic derivative of MltB) and theoretical considerations led to the proposal of a mechanism that accommodates a single catalytic at its active site. Thus, based on the complexes formed with murodipeptide, chitobiose, and the inhibitor bulgecin, a substrate-assisted mechanism has been invoked analogous to the family [[GH18]] chitinases and chitobiases, family [[GH20]] ''N''-acetyl-β-hexosaminidases, and family [[GH23]] lytic transglycosylases <cite>6</cite>. Thus, the catalytic Glu162 is proposed to serve initially as an acid catalyst to donate a proton to the glycosidic oxygen of the linkage to be cleaved leading to the formation of an intermediate with oxocarbenium ion character (Figure 2). In the absence of an anion/nucleophile in close proximity to stabilize this oxocarbenium intermediate, the lytic transglycosylases would employ anchimeric assistance of the MurNAc 2-acetamido group resulting in the formation an oxazolinium ion intermediate. This would be followed by abstraction of the C-6 hydroxyl proton of the oxazolinium species involving Glu162 which now serves as the base catalyst leading to nucleophilic attack and the formation of 1,6-anhydromuramic acid product. The β-hexosaminidase inhibitor NAG-thiazoline (Figure 2) was found to inhibit ''P. aeruginosa'' MltB thus supporting the proposal for the formation of an oxazolinium ion intermediate <cite>7</cite>, and the results of a site-directed mutagenesis study suggest that Ser216 orients the N-acetyl group on MurNAc at the -1 subsite of MltB for its participation in a substrate-assisted mechanism of action <cite>8</cite>.</div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div><del style="font-weight: bold; text-decoration: none;"></del></div></td><td colspan="2"> </td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 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>Three-dimensional structures are available for several family GH103 enzymes, the first solved being that of ''E. coli'' MltB (Slt35) <cite>5</cite>. The catalytic domain of the enyzmes possesses the well characterized α+β "lysozyme fold." </div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>Three-dimensional structures are available for several family GH103 enzymes, the first solved being that of ''E. coli'' MltB (Slt35) <cite>5</cite>. The catalytic domain of the enyzmes possesses the well characterized α+β "lysozyme fold." </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;"></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-l55" >Line 55:</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>;First identification of localization to outer membrane: ''E. coli'' MltB <cite>9</cite>.</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>;First identification of localization to outer membrane: ''E. coli'' MltB <cite>9</cite>.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>;Frist demonstration of molecular interactions between GH103 enzymes and penicillin-binding proteins:''E. coli'' MltB <cite>10</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>;Frist demonstration of molecular interactions between GH103 enzymes and penicillin-binding proteins:''E. coli'' MltB <cite>10</cite>.</div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div><del style="font-weight: bold; text-decoration: none;"></del></div></td><td colspan="2"> </td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 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-l69" >Line 69:</td>
<td colspan="2" class="diff-lineno">Line 65:</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>#9 pmid=7476170</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>#9 pmid=7476170</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>#10 pmid=9158739</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>#10 pmid=9158739</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></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|GH103]]</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|GH103]]</div></td></tr>
</table>
Harry Brumer
https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_103&diff=4051&oldid=prev
Anthony Clarke at 03:09, 20 February 2010
2010-02-20T03:09:33Z
<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 03:09, 20 February 2010</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l12" >Line 12:</td>
<td colspan="2" class="diff-lineno">Line 12:</td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|-</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|-</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|'''Clan''' </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>|'''Clan''' </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">None</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">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>α+β "lysozyme fold"</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>α+β "lysozyme fold"</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|-</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|-</div></td></tr>
</table>
Anthony Clarke
https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_103&diff=4048&oldid=prev
Anthony Clarke at 03:07, 20 February 2010
2010-02-20T03:07:42Z
<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 03:07, 20 February 2010</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l12" >Line 12:</td>
<td colspan="2" class="diff-lineno">Line 12:</td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|-</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|-</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|'''Clan''' </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>|'''Clan''' </div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>|<del class="diffchange diffchange-inline">GH-x</del></div></td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>|<ins class="diffchange diffchange-inline">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>α+β "lysozyme fold"</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>α+β "lysozyme fold"</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|-</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|-</div></td></tr>
</table>
Anthony Clarke