https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_76&feed=atom&action=history
Glycoside Hydrolase Family 76 - Revision history
2024-03-29T07:45:08Z
Revision history for this page on the wiki
MediaWiki 1.35.10
https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_76&diff=16828&oldid=prev
Spencer Williams: /* Three-dimensional structures */
2022-05-05T11:00:47Z
<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">
<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 11:00, 5 May 2022</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l41" >Line 41:</td>
<td colspan="2" class="diff-lineno">Line 41:</td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 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>Three-dimensional structures are available for several bacterial members of GH76, including the catalytic domain of ''Bacillus circulans'' Aman6, ''Bacteroides thetaiotaomicron'' BT2949 and BT3792, ''Listeria innocua'' Clip11262 and ''Salegentibacter'' sp. Hel_I_6 ShGH76 (''see the [http://www.cazy.org/GH76_structure.html GH76 structure page in the CAZy Database]''). They have an (&alpha;/&alpha;)<sub>6</sub> fold. A complex of mannopentaose bound in the active site of ''Bacillus circulans'' GH76 defined the -4 to +1 subsites, and showed the sugar binding in the -1 subsite in a <sup>1</sup>''S''<sub>5</sub> conformation. A complex of the same enzyme with &alpha;-1,6-mannobiose showed the disaccharide binding in the -3/-2 subsites (unpublished, PDB ID [{{PDBlink}}4boj 4boj]). Several <del class="diffchange diffchange-inline">inhibtior complezes </del>have been reported. A complex with the inhibitor &alpha;-mannosyl-1,6-isofagomine revealed the inhibtior to bind in the -2/-1 subsites and displayed the isofagomine ring in a ''B''<sub>2,5</sub> conformation, with the nitrogen of the inhibitor hydrogen-bonded to the nucleophile (D124) <cite>Thompson2015</cite>. The S-linked analogue &alpha;-mannosyl-1,6-''S''-isofagomine (ManSIFG) bound with similar affinity to the enzyme and also in the -2/-1 subsites, but instead the inhibitor bound in a relaxed <sup>4</sup>''C''<sub>1</sub> conformation with the inhibitor nitrogen hydrogen bonded to the acid/base (D125) <cite>Belz2017</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>Three-dimensional structures are available for several bacterial members of GH76, including the catalytic domain of ''Bacillus circulans'' Aman6, ''Bacteroides thetaiotaomicron'' BT2949 and BT3792, ''Listeria innocua'' Clip11262 and ''Salegentibacter'' sp. Hel_I_6 ShGH76 (''see the [http://www.cazy.org/GH76_structure.html GH76 structure page in the CAZy Database]''). They have an (&alpha;/&alpha;)<sub>6</sub> fold. A complex of mannopentaose bound in the active site of ''Bacillus circulans'' GH76 defined the -4 to +1 subsites, and showed the sugar binding in the -1 subsite in a <sup>1</sup>''S''<sub>5</sub> conformation. A complex of the same enzyme with &alpha;-1,6-mannobiose showed the disaccharide binding in the -3/-2 subsites (unpublished, PDB ID [{{PDBlink}}4boj 4boj]). Several <ins class="diffchange diffchange-inline">inhibitor complexes </ins>have been reported. A complex with the inhibitor &alpha;-mannosyl-1,6-isofagomine revealed the inhibtior to bind in the -2/-1 subsites and displayed the isofagomine ring in a ''B''<sub>2,5</sub> conformation, with the nitrogen of the inhibitor hydrogen-bonded to the nucleophile (D124) <cite>Thompson2015</cite>. The S-linked analogue &alpha;-mannosyl-1,6-''S''-isofagomine (ManSIFG) bound with similar affinity to the enzyme and also in the -2/-1 subsites, but instead the inhibitor bound in a relaxed <sup>4</sup>''C''<sub>1</sub> conformation with the inhibitor nitrogen hydrogen bonded to the acid/base (D125) <cite>Belz2017</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>
Spencer Williams
https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_76&diff=16827&oldid=prev
Spencer Williams at 11:00, 5 May 2022
2022-05-05T11:00:20Z
<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 11:00, 5 May 2022</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l28" >Line 28:</td>
<td colspan="2" class="diff-lineno">Line 28:</td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Substrate specificities ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Substrate specificities ==</div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>[[Glycoside hydrolases]] of family GH76 are [[endo]]-acting &alpha;-mannanases. GH76 genes are found within bacteria and fungi. Bacterial GH76 enzymes cleave &alpha;-1,6-mannans, such as those found within the &alpha;-1,6-linked backbone of fungal mannoproteins and mycobacterial cell wall lipomannan, lipoarabinomannan and phosphatidylinositol mannosides. This family was originally created from the cloning and characterization of Aman6 from ''Bacillus circulans'' TN-31 <cite>Maruyama2000</cite>, which appears to be the same enzyme as that characterized much earlier by Ballou and co-workers <cite> Nakajima1976</cite>. A related protein, Emn, has been cloned from ''Bacillus circulans'' TN-31 genomic DNA <cite Angala2019>. Aman6 degrades &alpha;-1,6-mannan to a mixture of the mannobiose and mannotriose <cite>Maruyama2000</cite>; mannotriose is the minimum substrate for the enzyme <cite> Nakajima1976</cite>. A possible GH76 enzyme has been detected within ''Mycobacterium smegmatis'', which has the capacity to degrade α-1,6-mannooligosaccharides <cite>Yokoyama1989</cite>.</div></td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>[[Glycoside hydrolases]] of family GH76 are [[endo]]-acting &alpha;-mannanases. GH76 genes are found within bacteria and fungi. Bacterial GH76 enzymes cleave &alpha;-1,6-mannans, such as those found within the &alpha;-1,6-linked backbone of fungal mannoproteins and mycobacterial cell wall lipomannan, lipoarabinomannan and phosphatidylinositol mannosides. This family was originally created from the cloning and characterization of Aman6 from ''Bacillus circulans'' TN-31 <cite>Maruyama2000</cite>, which appears to be the same enzyme as that characterized much earlier by Ballou and co-workers <cite>Nakajima1976</cite>. A related protein, Emn, has been cloned from ''Bacillus circulans'' TN-31 genomic DNA <cite<ins class="diffchange diffchange-inline">></ins>Angala2019<ins class="diffchange diffchange-inline"></cite</ins>>. Aman6 degrades &alpha;-1,6-mannan to a mixture of the mannobiose and mannotriose <cite>Maruyama2000</cite>; mannotriose is the minimum substrate for the enzyme <cite> Nakajima1976</cite>. A possible GH76 enzyme has been detected within ''Mycobacterium smegmatis'', which has the capacity to degrade α-1,6-mannooligosaccharides <cite>Yokoyama1989</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> </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>Additional characterized GH76 enzymes include several from the gut bacterium ''Bacteroides thetaiotaomicron'' <cite>Cuskin2015</cite> and ShGH76 from the marine bacterium ''Salegentibacter'' sp Hel_I_6 <cite Solanki2022>. ''B. thetaiotaomicron'' expresses numerous GH76 enzymes. Several of these are found within polysaccharide utilization loci that are specifically up-regulated upon exposure to yeast α-mannan. Likewise the ''Salegentibacter'' genes reside in PUL-like clusters. These enzymes have the capacity to utilize unadorned linear &alpha;-1,6-mannan, but have little activity on highly branched wildtype &alpha;-mannan. Certain ''B. thetaiotaomicron'' GH76 enzymes are lipoenzymes that are associated with the cell surface, where they appear to act on large yeast mannan molecules that have undergone partial trimming to expose sections of the core &alpha;-1,6-mannan. Other periplasmic located GH76 enzymes have activity on shorter &alpha;-1,6-mannan fragments, which are obtained by importation of partially-digested fragments arising from the action of cell surface enzymes.</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>Additional characterized GH76 enzymes include several from the gut bacterium ''Bacteroides thetaiotaomicron'' <cite>Cuskin2015</cite> and ShGH76 from the marine bacterium ''Salegentibacter'' sp Hel_I_6 <cite<ins class="diffchange diffchange-inline">></ins>Solanki2022<ins class="diffchange diffchange-inline"></cite</ins>>. ''B. thetaiotaomicron'' expresses numerous GH76 enzymes. Several of these are found within polysaccharide utilization loci that are specifically up-regulated upon exposure to yeast α-mannan. Likewise the ''Salegentibacter'' genes reside in PUL-like clusters. These enzymes have the capacity to utilize unadorned linear &alpha;-1,6-mannan, but have little activity on highly branched wildtype &alpha;-mannan. Certain ''B. thetaiotaomicron'' GH76 enzymes are lipoenzymes that are associated with the cell surface, where they appear to act on large yeast mannan molecules that have undergone partial trimming to expose sections of the core &alpha;-1,6-mannan. Other periplasmic located GH76 enzymes have activity on shorter &alpha;-1,6-mannan fragments, which are obtained by importation of partially-digested fragments arising from the action of cell surface enzymes.</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>Fungal GH76 enzymes have been speculated to be involved in cross-linking of GPI-anchored proteins into the cell wall, where they are proposed to act as transglycosylases <cite>Kitagaki2002</cite>. DFG-5 from ''Neurospora crassa'' has an enzymatic activity and processes the α-1,6-mannose backbone of fungal N-linked galactomannan <cite Patel2022>. Cell wall glycoproteins co-purify with DFG-5 indicating a specific association between DFG-5 and cell wall glycoproteins. DFG-5 can discriminate between cell wall and secreted glycoproteins, and does not bind to the N-linked galactomannans on secreted glycoproteins. </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>Fungal GH76 enzymes have been speculated to be involved in cross-linking of GPI-anchored proteins into the cell wall, where they are proposed to act as transglycosylases <cite>Kitagaki2002</cite>. DFG-5 from ''Neurospora crassa'' has an enzymatic activity and processes the α-1,6-mannose backbone of fungal N-linked galactomannan <cite<ins class="diffchange diffchange-inline">></ins>Patel2022<ins class="diffchange diffchange-inline"></cite</ins>>. Cell wall glycoproteins co-purify with DFG-5 indicating a specific association between DFG-5 and cell wall glycoproteins. DFG-5 can discriminate between cell wall and secreted glycoproteins, and does not bind to the N-linked galactomannans on secreted glycoproteins. </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>
</table>
Spencer Williams
https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_76&diff=16826&oldid=prev
Spencer Williams at 10:59, 5 May 2022
2022-05-05T10:59:08Z
<p></p>
<table class="diff diff-contentalign-left diff-editfont-monospace" data-mw="interface">
<col class="diff-marker" />
<col class="diff-content" />
<col class="diff-marker" />
<col class="diff-content" />
<tr class="diff-title" lang="en-CA">
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">← Older revision</td>
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 10:59, 5 May 2022</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l28" >Line 28:</td>
<td colspan="2" class="diff-lineno">Line 28:</td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Substrate specificities ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Substrate specificities ==</div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>[[Glycoside hydrolases]] of family GH76 are [[endo]]-acting &alpha;-mannanases. GH76 genes are found within bacteria and fungi. Bacterial GH76 enzymes cleave &alpha;-1,6-mannans, such as those found within the &alpha;-1,6-linked backbone of fungal mannoproteins and mycobacterial cell wall lipomannan and <del class="diffchange diffchange-inline">lipoarabinomannan</del>. This family was originally created from the cloning and characterization of Aman6 from ''Bacillus circulans'' TN-31 <cite>Maruyama2000</cite>, which appears to be the same enzyme as that characterized much earlier by Ballou and co-workers <cite> Nakajima1976</cite>. Aman6 degrades &alpha;-1,6-mannan to a mixture of the mannobiose and mannotriose <cite>Maruyama2000</cite>; mannotriose is the minimum substrate for the enzyme <cite> Nakajima1976</cite>. A possible GH76 enzyme has been detected within ''Mycobacterium smegmatis'', which has the capacity to degrade α-1,6-mannooligosaccharides <cite>Yokoyama1989</cite>.</div></td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>[[Glycoside hydrolases]] of family GH76 are [[endo]]-acting &alpha;-mannanases. GH76 genes are found within bacteria and fungi. Bacterial GH76 enzymes cleave &alpha;-1,6-mannans, such as those found within the &alpha;-1,6-linked backbone of fungal mannoproteins and mycobacterial cell wall lipomannan<ins class="diffchange diffchange-inline">, lipoarabinomannan </ins>and <ins class="diffchange diffchange-inline">phosphatidylinositol mannosides</ins>. This family was originally created from the cloning and characterization of Aman6 from ''Bacillus circulans'' TN-31 <cite>Maruyama2000</cite>, which appears to be the same enzyme as that characterized much earlier by Ballou and co-workers <cite> Nakajima1976</cite<ins class="diffchange diffchange-inline">>. A related protein, Emn, has been cloned from ''Bacillus circulans'' TN-31 genomic DNA <cite Angala2019</ins>>. Aman6 degrades &alpha;-1,6-mannan to a mixture of the mannobiose and mannotriose <cite>Maruyama2000</cite>; mannotriose is the minimum substrate for the enzyme <cite> Nakajima1976</cite>. A possible GH76 enzyme has been detected within ''Mycobacterium smegmatis'', which has the capacity to degrade α-1,6-mannooligosaccharides <cite>Yokoyama1989</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> </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>Additional characterized GH76 enzymes include several from ''Bacteroides thetaiotaomicron'' <cite>Cuskin2015</cite>. ''B. thetaiotaomicron'' expresses numerous GH76 enzymes. Several of these are found within polysaccharide utilization loci that are specifically up-regulated upon exposure to yeast α-mannan. These enzymes have the capacity to utilize unadorned linear &alpha;-1,6-mannan, but have little activity on highly branched wildtype &alpha;-mannan. Certain ''B. thetaiotaomicron'' GH76 enzymes are lipoenzymes that are associated with the cell surface, where they appear to act on large yeast mannan molecules that have undergone partial trimming to expose sections of the core &alpha;-1,6-mannan. Other periplasmic located GH76 enzymes have activity on shorter &alpha;-1,6-mannan fragments, which are obtained by importation of partially-digested fragments arising from the action of cell surface enzymes.</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>Additional characterized GH76 enzymes include several from <ins class="diffchange diffchange-inline">the gut bacterium </ins>''Bacteroides thetaiotaomicron'' <cite>Cuskin2015</cite<ins class="diffchange diffchange-inline">> and ShGH76 from the marine bacterium ''Salegentibacter'' sp Hel_I_6 <cite Solanki2022</ins>>. ''B. thetaiotaomicron'' expresses numerous GH76 enzymes. Several of these are found within polysaccharide utilization loci that are specifically up-regulated upon exposure to yeast α-mannan<ins class="diffchange diffchange-inline">. Likewise the ''Salegentibacter'' genes reside in PUL-like clusters</ins>. These enzymes have the capacity to utilize unadorned linear &alpha;-1,6-mannan, but have little activity on highly branched wildtype &alpha;-mannan. Certain ''B. thetaiotaomicron'' GH76 enzymes are lipoenzymes that are associated with the cell surface, where they appear to act on large yeast mannan molecules that have undergone partial trimming to expose sections of the core &alpha;-1,6-mannan. Other periplasmic located GH76 enzymes have activity on shorter &alpha;-1,6-mannan fragments, which are obtained by importation of partially-digested fragments arising from the action of cell surface enzymes.</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>Fungal GH76 enzymes have been speculated to be involved in cross-linking of GPI-anchored proteins into the cell wall, where they are proposed to act as transglycosylases <cite>Kitagaki2002</cite>. <del class="diffchange diffchange-inline">No biochemical data </del>has <del class="diffchange diffchange-inline">been obtained for any </del>fungal <del class="diffchange diffchange-inline">GH76 enzyme in support of </del>the <del class="diffchange diffchange-inline">so</del>-<del class="diffchange diffchange-inline">called anchorage hypothesis</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>Fungal GH76 enzymes have been speculated to be involved in cross-linking of GPI-anchored proteins into the cell wall, where they are proposed to act as transglycosylases <cite>Kitagaki2002</cite>. <ins class="diffchange diffchange-inline">DFG-5 from ''Neurospora crassa'' </ins>has <ins class="diffchange diffchange-inline">an enzymatic activity and processes the α-1,6-mannose backbone of </ins>fungal <ins class="diffchange diffchange-inline">N-linked galactomannan <cite Patel2022>. Cell wall glycoproteins co-purify with DFG-5 indicating a specific association between DFG-5 and cell wall glycoproteins. DFG-5 can discriminate between cell wall and secreted glycoproteins, and does not bind to </ins>the <ins class="diffchange diffchange-inline">N</ins>-<ins class="diffchange diffchange-inline">linked galactomannans on secreted glycoproteins</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>== Kinetics and Mechanism ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Kinetics and Mechanism ==</div></td></tr>
<tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l41" >Line 41:</td>
<td colspan="2" class="diff-lineno">Line 41:</td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 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>Three-dimensional structures are available for several bacterial members of GH76, including the catalytic domain of ''Bacillus circulans'' Aman6, ''Bacteroides thetaiotaomicron'' BT2949 and BT3792, <del class="diffchange diffchange-inline">and </del>''Listeria innocua'' Clip11262 (''see the [http://www.cazy.org/GH76_structure.html GH76 structure page in the CAZy Database]''). They have an (&alpha;/&alpha;)<sub>6</sub> fold. A complex of mannopentaose bound in the active site of ''Bacillus circulans'' GH76 defined the -4 to +1 subsites, and showed the sugar binding in the -1 subsite in a <sup>1</sup>''S''<sub>5</sub> conformation. A complex of the same enzyme with &alpha;-1,6-mannobiose showed the disaccharide binding in the -3/-2 subsites (unpublished, PDB ID [{{PDBlink}}4boj 4boj]). Several inhibtior complezes have been reported. A complex with the inhibitor &alpha;-mannosyl-1,6-isofagomine revealed the inhibtior to bind in the -2/-1 subsites and displayed the isofagomine ring in a ''B''<sub>2,5</sub> conformation, with the nitrogen of the inhibitor hydrogen-bonded to the nucleophile (D124) <cite>Thompson2015</cite>. The S-linked analogue &alpha;-mannosyl-1,6-''S''-isofagomine (ManSIFG) bound with similar affinity to the enzyme and also in the -2/-1 subsites, but instead the inhibitor bound in a relaxed <sup>4</sup>''C''<sub>1</sub> conformation with the inhibitor nitrogen hydrogen bonded to the acid/base (D125) <cite>Belz2017</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>Three-dimensional structures are available for several bacterial members of GH76, including the catalytic domain of ''Bacillus circulans'' Aman6, ''Bacteroides thetaiotaomicron'' BT2949 and BT3792, ''Listeria innocua'' Clip11262 <ins class="diffchange diffchange-inline">and ''Salegentibacter'' sp. Hel_I_6 ShGH76 </ins>(''see the [http://www.cazy.org/GH76_structure.html GH76 structure page in the CAZy Database]''). They have an (&alpha;/&alpha;)<sub>6</sub> fold. A complex of mannopentaose bound in the active site of ''Bacillus circulans'' GH76 defined the -4 to +1 subsites, and showed the sugar binding in the -1 subsite in a <sup>1</sup>''S''<sub>5</sub> conformation. A complex of the same enzyme with &alpha;-1,6-mannobiose showed the disaccharide binding in the -3/-2 subsites (unpublished, PDB ID [{{PDBlink}}4boj 4boj]). Several inhibtior complezes have been reported. A complex with the inhibitor &alpha;-mannosyl-1,6-isofagomine revealed the inhibtior to bind in the -2/-1 subsites and displayed the isofagomine ring in a ''B''<sub>2,5</sub> conformation, with the nitrogen of the inhibitor hydrogen-bonded to the nucleophile (D124) <cite>Thompson2015</cite>. The S-linked analogue &alpha;-mannosyl-1,6-''S''-isofagomine (ManSIFG) bound with similar affinity to the enzyme and also in the -2/-1 subsites, but instead the inhibitor bound in a relaxed <sup>4</sup>''C''<sub>1</sub> conformation with the inhibitor nitrogen hydrogen bonded to the acid/base (D125) <cite>Belz2017</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 colspan="2" class="diff-lineno" id="mw-diff-left-l61" >Line 61:</td>
<td colspan="2" class="diff-lineno">Line 61:</td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>#Thompson2015 pmid=25772148</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>#Thompson2015 pmid=25772148</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>#Belz2017 pmid=28766587</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>#Belz2017 pmid=28766587</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;">#Angala2019 pmid=31835712</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;">#Solanki2022 pmid=35414716</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;">#Patel2022 pmid=35306147</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> </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|GH076]]</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|GH076]]</div></td></tr>
</table>
Spencer Williams
https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_76&diff=16491&oldid=prev
Harry Brumer: Text replacement - "\^\^\^(.*)\^\^\^" to "$1"
2021-12-18T21:14:35Z
<p>Text replacement - "\^\^\^(.*)\^\^\^" to "<a href="/index.php?title=User:$1&action=edit&redlink=1" class="new" title="User:$1 (page does not exist)">$1</a>"</p>
<table class="diff diff-contentalign-left diff-editfont-monospace" data-mw="interface">
<col class="diff-marker" />
<col class="diff-content" />
<col class="diff-marker" />
<col class="diff-content" />
<tr class="diff-title" lang="en-CA">
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">← Older revision</td>
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 21:14, 18 December 2021</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l1" >Line 1:</td>
<td colspan="2" class="diff-lineno">Line 1:</td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>{{CuratorApproved}}</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>{{CuratorApproved}}</div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>* [[Author]]: <del class="diffchange diffchange-inline">^^^</del>Spencer Williams<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:Spencer Williams|</ins>Spencer Williams<ins class="diffchange diffchange-inline">]]</ins></div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>* [[Responsible Curator]]s: <del class="diffchange diffchange-inline">^^^</del>Gideon Davies<del class="diffchange diffchange-inline">^^^ </del>and <del class="diffchange diffchange-inline">^^^</del>Harry Gilbert<del class="diffchange diffchange-inline">^^^</del></div></td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>* [[Responsible Curator]]s: <ins class="diffchange diffchange-inline">[[User:</ins>Gideon Davies<ins class="diffchange diffchange-inline">|Gideon Davies]] </ins>and <ins class="diffchange diffchange-inline">[[User:</ins>Harry Gilbert<ins class="diffchange diffchange-inline">|Harry Gilbert]]</ins></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>----</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>----</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
</table>
Harry Brumer
https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_76&diff=11756&oldid=prev
Spencer Williams: /* Three-dimensional structures */
2017-10-19T00:15:03Z
<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">
<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 00:15, 19 October 2017</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l41" >Line 41:</td>
<td colspan="2" class="diff-lineno">Line 41:</td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 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>Three-dimensional structures are available for several bacterial members of GH76, including the catalytic domain of ''Bacillus circulans'' Aman6, ''Bacteroides thetaiotaomicron'' BT2949 and BT3792, and ''Listeria innocua'' Clip11262 (''see the [http://www.cazy.org/GH76_structure.html GH76 structure page in the CAZy Database]''). They have an (&alpha;/&alpha;)<sub>6</sub> fold. A complex of mannopentaose bound in the active site of ''Bacillus circulans'' GH76 defined the -4 to +1 subsites, and showed the sugar binding in the -1 subsite in a <sup>1</sup>''S''<sub>5</sub> conformation. A complex of the same enzyme with &alpha;-1,6-mannobiose showed the disaccharide binding in the -3/-2 subsites (unpublished, PDB ID [{{PDBlink}}4boj 4boj]). Several inhibtior complezes have been reported. A complex with the inhibitor &alpha;-mannosyl-1,6-isofagomine revealed the inhibtior to bind <del class="diffchange diffchange-inline">int he </del>-2/-1 subsites and displayed the isofagomine ring in a ''B''<sub>2,5</sub> conformation, with the nitrogen of the inhibitor hydrogen-bonded to the nucleophile (D124) <cite>Thompson2015</cite>. The S-linked analogue &alpha;-mannosyl-1,6-''S''-isofagomine (ManSIFG) bound with similar affinity to the enzyme and in the -2/-<del class="diffchange diffchange-inline">2 substites as well</del>, but <del class="diffchange diffchange-inline">revealed an interaction of </del>the inhibitor <del class="diffchange diffchange-inline">nitrogen with the acid/base (D125) and </del>a relaxed <sup>4</sup>''C''<sub>1</sub> conformation <cite>Belz2017</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>Three-dimensional structures are available for several bacterial members of GH76, including the catalytic domain of ''Bacillus circulans'' Aman6, ''Bacteroides thetaiotaomicron'' BT2949 and BT3792, and ''Listeria innocua'' Clip11262 (''see the [http://www.cazy.org/GH76_structure.html GH76 structure page in the CAZy Database]''). They have an (&alpha;/&alpha;)<sub>6</sub> fold. A complex of mannopentaose bound in the active site of ''Bacillus circulans'' GH76 defined the -4 to +1 subsites, and showed the sugar binding in the -1 subsite in a <sup>1</sup>''S''<sub>5</sub> conformation. A complex of the same enzyme with &alpha;-1,6-mannobiose showed the disaccharide binding in the -3/-2 subsites (unpublished, PDB ID [{{PDBlink}}4boj 4boj]). Several inhibtior complezes have been reported. A complex with the inhibitor &alpha;-mannosyl-1,6-isofagomine revealed the inhibtior to bind <ins class="diffchange diffchange-inline">in the </ins>-2/-1 subsites and displayed the isofagomine ring in a ''B''<sub>2,5</sub> conformation, with the nitrogen of the inhibitor hydrogen-bonded to the nucleophile (D124) <cite>Thompson2015</cite>. The S-linked analogue &alpha;-mannosyl-1,6-''S''-isofagomine (ManSIFG) bound with similar affinity to the enzyme and <ins class="diffchange diffchange-inline">also </ins>in the -2/-<ins class="diffchange diffchange-inline">1 subsites</ins>, but <ins class="diffchange diffchange-inline">instead </ins>the inhibitor <ins class="diffchange diffchange-inline">bound in </ins>a relaxed <sup>4</sup>''C''<sub>1</sub> conformation <ins class="diffchange diffchange-inline">with the inhibitor nitrogen hydrogen bonded to the acid/base (D125) </ins><cite>Belz2017</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>
Spencer Williams
https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_76&diff=11755&oldid=prev
Spencer Williams at 00:13, 19 October 2017
2017-10-19T00:13:22Z
<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 00:13, 19 October 2017</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l41" >Line 41:</td>
<td colspan="2" class="diff-lineno">Line 41:</td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 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>Three-dimensional structures are available for several bacterial members of GH76, including the catalytic domain of ''Bacillus circulans'' Aman6, ''Bacteroides thetaiotaomicron'' BT2949 and BT3792, and ''Listeria innocua'' Clip11262 (''see the [http://www.cazy.org/GH76_structure.html GH76 structure page in the CAZy Database]''). They have an (&alpha;/&alpha;)<sub>6</sub> fold. A complex of mannopentaose bound in the active site of ''Bacillus circulans'' GH76 defined the -4 to +1 subsites, and showed the sugar binding in the -1 subsite in a <sup>1</sup>''S''<sub>5</sub> conformation <del class="diffchange diffchange-inline">and a </del>complex with the inhibitor &alpha;-mannosyl-1,6-isofagomine displayed the isofagomine ring in a ''B''<sub>2,5</sub> conformation <cite>Thompson2015</cite>. <del class="diffchange diffchange-inline">A complex of the same enzyme with </del>&alpha;-1,6-<del class="diffchange diffchange-inline">mannobiose showed </del>the <del class="diffchange diffchange-inline">disaccharide binding </del>in the -<del class="diffchange diffchange-inline">3</del>/-2 <del class="diffchange diffchange-inline">subsites </del>(<del class="diffchange diffchange-inline">unpublished, PDB ID [{{PDBlink}}4boj 4boj]</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>Three-dimensional structures are available for several bacterial members of GH76, including the catalytic domain of ''Bacillus circulans'' Aman6, ''Bacteroides thetaiotaomicron'' BT2949 and BT3792, and ''Listeria innocua'' Clip11262 (''see the [http://www.cazy.org/GH76_structure.html GH76 structure page in the CAZy Database]''). They have an (&alpha;/&alpha;)<sub>6</sub> fold. A complex of mannopentaose bound in the active site of ''Bacillus circulans'' GH76 defined the -4 to +1 subsites, and showed the sugar binding in the -1 subsite in a <sup>1</sup>''S''<sub>5</sub> conformation<ins class="diffchange diffchange-inline">. A complex of the same enzyme with &alpha;-1,6-mannobiose showed the disaccharide binding in the -3/-2 subsites (unpublished, PDB ID [{{PDBlink}}4boj 4boj]). Several inhibtior complezes have been reported. A </ins>complex with the inhibitor &alpha;-mannosyl-1,6-isofagomine <ins class="diffchange diffchange-inline">revealed the inhibtior to bind int he -2/-1 subsites and </ins>displayed the isofagomine ring in a ''B''<sub>2,5</sub> conformation<ins class="diffchange diffchange-inline">, with the nitrogen of the inhibitor hydrogen-bonded to the nucleophile (D124) </ins><cite>Thompson2015</cite>. <ins class="diffchange diffchange-inline">The S-linked analogue </ins>&alpha;<ins class="diffchange diffchange-inline">-mannosyl</ins>-1,6-<ins class="diffchange diffchange-inline">''S''-isofagomine (ManSIFG) bound with similar affinity to </ins>the <ins class="diffchange diffchange-inline">enzyme and </ins>in the -<ins class="diffchange diffchange-inline">2</ins>/-2 <ins class="diffchange diffchange-inline">substites as well, but revealed an interaction of the inhibitor nitrogen with the acid/base </ins>(<ins class="diffchange diffchange-inline">D125</ins>) <ins class="diffchange diffchange-inline">and a relaxed <sup>4</sup>''C''<sub>1</sub> conformation <cite>Belz2017</cite></ins>. </div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Family Firsts ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Family Firsts ==</div></td></tr>
</table>
Spencer Williams
https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_76&diff=11754&oldid=prev
Spencer Williams at 04:10, 14 October 2017
2017-10-14T04:10:19Z
<p></p>
<table class="diff diff-contentalign-left diff-editfont-monospace" data-mw="interface">
<col class="diff-marker" />
<col class="diff-content" />
<col class="diff-marker" />
<col class="diff-content" />
<tr class="diff-title" lang="en-CA">
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">← Older revision</td>
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 04:10, 14 October 2017</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l60" >Line 60:</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>#Cuskin2015 pmid=25567280</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>#Cuskin2015 pmid=25567280</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>#Thompson2015 pmid=25772148</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>#Thompson2015 pmid=25772148</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;">#Belz2017 pmid=28766587</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> </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|GH076]]</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|GH076]]</div></td></tr>
</table>
Spencer Williams
https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_76&diff=11384&oldid=prev
Spencer Williams at 03:04, 22 January 2017
2017-01-22T03:04:53Z
<p></p>
<table class="diff diff-contentalign-left diff-editfont-monospace" data-mw="interface">
<col class="diff-marker" />
<col class="diff-content" />
<col class="diff-marker" />
<col class="diff-content" />
<tr class="diff-title" lang="en-CA">
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">← Older revision</td>
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 03:04, 22 January 2017</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l35" >Line 35:</td>
<td colspan="2" class="diff-lineno">Line 35:</td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== 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>Family GH76 [[endo]]-&alpha;-mannosidases are [[retaining]] enzymes, as first shown by <sup>1</sup>H NMR analysis of the hydrolysis of 4-nitrophenyl &alpha;-mannosyl-1,6-&alpha;-mannopyranoside by a ''Bacteroides thetaiotaomicron'' &alpha;-mannanase <cite>Cuskin2015</cite>. GH76 enzymes are believed to proceed through a [[classical Koshland double-displacement mechanism]]. Crystallographic evidence from a binary complexes of the catalytic domain of ''Bacillus circulans'' Aman6 with substrate and inhibitors <del class="diffchange diffchange-inline">and </del>complemented by quantum mechanics/molecular mechanics calculations of preferred conformations on-enzyme supports a <sup>1</sup>''S''<sub>5</sub>&rarr;''B''<sub>2,5</sub><sup>‡</sup>&rarr;<sup>O</sup>''S''<sub>2</sub> conformational reaction coordinate <cite>Thompson2015</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>Family GH76 [[endo]]-&alpha;-mannosidases are [[retaining]] enzymes, as first shown by <sup>1</sup>H NMR analysis of the hydrolysis of 4-nitrophenyl &alpha;-mannosyl-1,6-&alpha;-mannopyranoside by a ''Bacteroides thetaiotaomicron'' &alpha;-mannanase <cite>Cuskin2015</cite>. GH76 enzymes are believed to proceed through a [[classical Koshland double-displacement mechanism]]. Crystallographic evidence from a binary complexes of the catalytic domain of ''Bacillus circulans'' Aman6 with substrate and inhibitors<ins class="diffchange diffchange-inline">, </ins>complemented by quantum mechanics/molecular mechanics calculations of preferred conformations on-enzyme supports a <sup>1</sup>''S''<sub>5</sub>&rarr;''B''<sub>2,5</sub><sup>‡</sup>&rarr;<sup>O</sup>''S''<sub>2</sub> conformational reaction coordinate <cite>Thompson2015</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>
Spencer Williams
https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_76&diff=10587&oldid=prev
Spencer Williams: /* Catalytic Residues */
2015-03-18T21:55:50Z
<p><span dir="auto"><span class="autocomment">Catalytic Residues</span></span></p>
<table class="diff diff-contentalign-left diff-editfont-monospace" data-mw="interface">
<col class="diff-marker" />
<col class="diff-content" />
<col class="diff-marker" />
<col class="diff-content" />
<tr class="diff-title" lang="en-CA">
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">← Older revision</td>
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 21:55, 18 March 2015</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l38" >Line 38:</td>
<td colspan="2" class="diff-lineno">Line 38:</td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 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>Inspection of the X-ray structure of ''Bacteroides thetaiotaomicron'' BT3792 revealed two consecutive asparate residues, D258 and D259, that were predicted to be catalytic residues <cite>Cuskin2015</cite>. The equivalent pair of conserved aspartic acid residues (D124 and D125 in the catalytic domain of ''Bacillus circulans'' Aman6) were identified as [[nucleophile]] and [[general acid/base]], respectively, based on X-ray analysis of substrate and inhibitor complexes, dovetailed with kinetic analysis of mutants <cite>Thompson2015</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>Inspection of the X-ray structure of ''Bacteroides thetaiotaomicron'' BT3792 revealed two consecutive asparate residues, D258 and D259, that were predicted to be catalytic residues <cite>Cuskin2015</cite>. The equivalent pair of conserved aspartic acid residues (D124 and D125 in the catalytic domain of ''Bacillus circulans'' Aman6) were identified as [[<ins class="diffchange diffchange-inline">catalytic </ins>nucleophile]] and [[general acid/base]], respectively, based on X-ray analysis of substrate and inhibitor complexes, dovetailed with kinetic analysis of mutants <cite>Thompson2015</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_76&diff=10586&oldid=prev
Spencer Williams at 21:54, 18 March 2015
2015-03-18T21:54:04Z
<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 21:54, 18 March 2015</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l35" >Line 35:</td>
<td colspan="2" class="diff-lineno">Line 35:</td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== 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>Family GH76 [[endo]]-&alpha;-mannosidases are [[retaining]] enzymes, as first shown by <sup>1</sup>H NMR analysis of the hydrolysis of 4-nitrophenyl &alpha;-mannosyl-1,6-&alpha;-mannopyranoside by a ''Bacteroides thetaiotaomicron'' &alpha;-mannanase <cite>Cuskin2015</cite>. GH76 enzymes are believed to proceed through a [[classical Koshland double-displacement mechanism]]. Crystallographic evidence from a binary complexes of ''<del class="diffchange diffchange-inline">B. </del>circulans'' <del class="diffchange diffchange-inline">GH76 </del>with substrate and inhibitors and complemented by quantum mechanics/molecular mechanics calculations of preferred conformations on-enzyme supports a <sup>1</sup>''S''<sub>5</sub>&rarr;''B''<sub>2,5</sub><sup>‡</sup>&rarr;<sup>O</sup>''S''<sub>2</sub> conformational reaction coordinate <cite>Thompson2015</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>Family GH76 [[endo]]-&alpha;-mannosidases are [[retaining]] enzymes, as first shown by <sup>1</sup>H NMR analysis of the hydrolysis of 4-nitrophenyl &alpha;-mannosyl-1,6-&alpha;-mannopyranoside by a ''Bacteroides thetaiotaomicron'' &alpha;-mannanase <cite>Cuskin2015</cite>. GH76 enzymes are believed to proceed through a [[classical Koshland double-displacement mechanism]]. Crystallographic evidence from a binary complexes <ins class="diffchange diffchange-inline">of the catalytic domain </ins>of ''<ins class="diffchange diffchange-inline">Bacillus </ins>circulans'' <ins class="diffchange diffchange-inline">Aman6 </ins>with substrate and inhibitors and complemented by quantum mechanics/molecular mechanics calculations of preferred conformations on-enzyme supports a <sup>1</sup>''S''<sub>5</sub>&rarr;''B''<sub>2,5</sub><sup>‡</sup>&rarr;<sup>O</sup>''S''<sub>2</sub> conformational reaction coordinate <cite>Thompson2015</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 colspan="2" class="diff-lineno" id="mw-diff-left-l41" >Line 41:</td>
<td colspan="2" class="diff-lineno">Line 41:</td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 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>Three-dimensional structures are available for several bacterial members of GH76, including ''Bacillus circulans'', ''Bacteroides thetaiotaomicron'' and ''Listeria innocua'' Clip11262 (''see the [http://www.cazy.org/GH76_structure.html GH76 structure page in the CAZy Database]''). They have an (&alpha;/&alpha;)<sub>6</sub> fold. A complex of mannopentaose bound in the active site of ''Bacillus circulans'' GH76 defined the -4 to +1 subsites, and showed the sugar binding in the -1 subsite in a <sup>1</sup>''S''<sub>5</sub> conformation and a complex with the inhibitor &alpha;-mannosyl-1,6-isofagomine displayed the isofagomine ring in a ''B''<sub>2,5</sub> conformation <cite>Thompson2015</cite>. A complex of the same enzyme with &alpha;-1,6-mannobiose showed the disaccharide binding in the -3/-2 subsites (unpublished, PDB ID [{{PDBlink}}4boj 4boj]).</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>Three-dimensional structures are available for several bacterial members of GH76, including <ins class="diffchange diffchange-inline">the catalytic domain of </ins>''Bacillus circulans'' <ins class="diffchange diffchange-inline">Aman6</ins>, ''Bacteroides thetaiotaomicron'' <ins class="diffchange diffchange-inline">BT2949 and BT3792, </ins>and ''Listeria innocua'' Clip11262 (''see the [http://www.cazy.org/GH76_structure.html GH76 structure page in the CAZy Database]''). They have an (&alpha;/&alpha;)<sub>6</sub> fold. A complex of mannopentaose bound in the active site of ''Bacillus circulans'' GH76 defined the -4 to +1 subsites, and showed the sugar binding in the -1 subsite in a <sup>1</sup>''S''<sub>5</sub> conformation and a complex with the inhibitor &alpha;-mannosyl-1,6-isofagomine displayed the isofagomine ring in a ''B''<sub>2,5</sub> conformation <cite>Thompson2015</cite>. A complex of the same enzyme with &alpha;-1,6-mannobiose showed the disaccharide binding in the -3/-2 subsites (unpublished, PDB ID [{{PDBlink}}4boj 4boj]).</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Family Firsts ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Family Firsts ==</div></td></tr>
</table>
Spencer Williams