https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_97&feed=atom&action=history
Glycoside Hydrolase Family 97 - Revision history
2024-03-29T10:05:08Z
Revision history for this page on the wiki
MediaWiki 1.35.10
https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_97&diff=16694&oldid=prev
Harry Brumer: Text replacement - "\^\^\^(.*)\^\^\^" to "$1"
2021-12-18T21:20:39Z
<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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Harry Brumer
https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_97&diff=6829&oldid=prev
Harry Brumer: updated reference identifiers to standard AuthorYear format to make future editing easier
2011-05-27T12:30:39Z
<p>updated reference identifiers to standard AuthorYear format to make future editing easier</p>
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<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><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>
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<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Substrate specificities ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Substrate specificities ==</div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>Family 97 [[glycoside hydrolases]] hydrolyse α-linked D-glycosides; the two enzymes from this family that have been characterised to date have α-glucosidase (EC 3.2.1.20) and α-galactosidase (EC 3.2.1.22) activity <cite><del class="diffchange diffchange-inline">REF1</del></cite>. The α-glucosidase from ''Bacteroides thetaiotaomicron'' has been characterised in the most detail, and has been demonstrated to hydrolyse substrates ranging from maltose to maltoheptaose in length, and those containing α-1,6-, α-1,3- and α-1,2-, as well as α-1,4-linkages <cite><del class="diffchange diffchange-inline">REF2;REF3</del></cite>.</div></td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>Family 97 [[glycoside hydrolases]] hydrolyse α-linked D-glycosides; the two enzymes from this family that have been characterised to date have α-glucosidase (EC 3.2.1.20) and α-galactosidase (EC 3.2.1.22) activity <cite><ins class="diffchange diffchange-inline">Gloster2008</ins></cite>. The α-glucosidase from ''Bacteroides thetaiotaomicron'' has been characterised in the most detail, and has been demonstrated to hydrolyse substrates ranging from maltose to maltoheptaose in length, and those containing α-1,6-, α-1,3- and α-1,2-, as well as α-1,4-linkages <cite><ins class="diffchange diffchange-inline">Smith1991 Kitamura2008</ins></cite>.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== 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 GH97 is unusual as it contains both [[retaining]] and [[inverting]] enzymes, as shown unequivocally by NMR <cite><del class="diffchange diffchange-inline">REF1</del></cite> and HPLC <cite><del class="diffchange diffchange-inline">REF3</del></cite> analyses, by characterization of two enzymes from ''Bacteroides thetaiotaomicron''. Catalysis is dependent on the presence of calcium, which coordinates the C2-OH group of the substrate in the -1 subsite, as well as four glutamate residues in the active site <cite><del class="diffchange diffchange-inline">REF1</del></cite>. One of the glutamate residues coordinated by the calcium ion is predicted to be the [[general acid/base]] residue, which may receive acid assistance from the calcium during hydrolysis.</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 GH97 is unusual as it contains both [[retaining]] and [[inverting]] enzymes, as shown unequivocally by NMR <cite><ins class="diffchange diffchange-inline">Gloster2008</ins></cite> and HPLC <cite><ins class="diffchange diffchange-inline">Kitamura2008</ins></cite> analyses, by characterization of two enzymes from ''Bacteroides thetaiotaomicron''. Catalysis is dependent on the presence of calcium, which coordinates the C2-OH group of the substrate in the -1 subsite, as well as four glutamate residues in the active site <cite><ins class="diffchange diffchange-inline">Gloster2008</ins></cite>. One of the glutamate residues coordinated by the calcium ion is predicted to be the [[general acid/base]] residue, which may receive acid assistance from the calcium during hydrolysis.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Catalytic Residues ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Catalytic Residues ==</div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>The constellation of glutamate residues (five in total, four of which coordinate the calcium ion) in the active site of the only ([[inverting]]) GH97 enzyme whose structure has been solved to date, has made the assignment of catalytic residues difficult. Analysis of sequence alignments, structural alignments with family [[GH27]], and a mutant tested with substrates with different leaving group abilities, has provided a likely candidate for the [[general acid]] residue in this [[inverting]] enzyme or as the [[general acid/base]] in the [[retaining]] members of the family <cite><del class="diffchange diffchange-inline">REF1</del></cite>. It is possible that the calcium ion provides acid assistance to the acid/base during hydrolysis. The [[general base]] for the [[inverting]] enzyme has also been predicted on the basis of its position in the active site; in addition it coordinates a water molecule that is situated in a position primed for nucleophilic attack, and mutation causes the enzyme to be virtually inactive. Although a structure has not been solved for a retaining enzyme, the [[catalytic nucleophile]] for the [[retaining]] enzymes has been predicted based on sequence alignments, and similarity to [[GH27]] enzymes, to be an aspartate residue <cite><del class="diffchange diffchange-inline">REF1</del></cite>.</div></td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>The constellation of glutamate residues (five in total, four of which coordinate the calcium ion) in the active site of the only ([[inverting]]) GH97 enzyme whose structure has been solved to date, has made the assignment of catalytic residues difficult. Analysis of sequence alignments, structural alignments with family [[GH27]], and a mutant tested with substrates with different leaving group abilities, has provided a likely candidate for the [[general acid]] residue in this [[inverting]] enzyme or as the [[general acid/base]] in the [[retaining]] members of the family <cite><ins class="diffchange diffchange-inline">Gloster2008</ins></cite>. It is possible that the calcium ion provides acid assistance to the acid/base during hydrolysis. The [[general base]] for the [[inverting]] enzyme has also been predicted on the basis of its position in the active site; in addition it coordinates a water molecule that is situated in a position primed for nucleophilic attack, and mutation causes the enzyme to be virtually inactive. Although a structure has not been solved for a retaining enzyme, the [[catalytic nucleophile]] for the [[retaining]] enzymes has been predicted based on sequence alignments, and similarity to [[GH27]] enzymes, to be an aspartate residue <cite><ins class="diffchange diffchange-inline">Gloster2008</ins></cite>.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Three-dimensional structures ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Three-dimensional structures ==</div></td></tr>
<tr><td 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>There has been one structure solved, using X-ray crystallography, for a member of family GH97 (which inverts stereochemistry). This is an enzyme from ''Bacteroides thetaiotaomicron'', SusB, which is involved in the degradation of starch in the human gut. The tertiary structure of the GH97 enzyme revealed three domains; an N-terminal β-super-sandwich domain, followed by a canonical (β/α)8 barrel (which houses the catalytic domain) and a C-terminal β-sheet domain <cite><del class="diffchange diffchange-inline">REF1;REF3</del></cite>. There have also been complexes solved with the inhibitors acarbose <cite><del class="diffchange diffchange-inline">REF3</del></cite>, deoxynojirimycin and castanospermine <cite><del class="diffchange diffchange-inline">REF1</del></cite>. Structural alignments show similarity to families [[GH27]] and [[GH36]] (as predicted previously by a bioinformatics study <cite><del class="diffchange diffchange-inline">REF4</del></cite>).</div></td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>There has been one structure solved, using X-ray crystallography, for a member of family GH97 (which inverts stereochemistry). This is an enzyme from ''Bacteroides thetaiotaomicron'', SusB, which is involved in the degradation of starch in the human gut. The tertiary structure of the GH97 enzyme revealed three domains; an N-terminal β-super-sandwich domain, followed by a canonical (β/α)8 barrel (which houses the catalytic domain) and a C-terminal β-sheet domain <cite><ins class="diffchange diffchange-inline">Gloster2008 Kitamura2008</ins></cite>. There have also been complexes solved with the inhibitors acarbose <cite><ins class="diffchange diffchange-inline">Kitamura2008</ins></cite>, deoxynojirimycin and castanospermine <cite><ins class="diffchange diffchange-inline">Gloster2008</ins></cite>. Structural alignments show similarity to families [[GH27]] and [[GH36]] (as predicted previously by a bioinformatics study <cite><ins class="diffchange diffchange-inline">Naumoff2005</ins></cite>).</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Family Firsts ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Family Firsts ==</div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>;First sterochemistry determination: Two GH97 members from ''Bacteroides thetaiotaomicron'' were shown to differ in stereochemical outcome, by NMR <cite><del class="diffchange diffchange-inline">REF1</del></cite> and HPLC <cite><del class="diffchange diffchange-inline">REF3</del></cite> analyses, demonstrating that the family contains enzymes that hydrolyse with both retention and inversion of anomeric stereochemistry.</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 sterochemistry determination: Two GH97 members from ''Bacteroides thetaiotaomicron'' were shown to differ in stereochemical outcome, by NMR <cite><ins class="diffchange diffchange-inline">Gloster2008</ins></cite> and HPLC <cite><ins class="diffchange diffchange-inline">Kitamura2008</ins></cite> analyses, demonstrating that the family contains enzymes that hydrolyse with both retention and inversion of anomeric stereochemistry.</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: Not proven unequivocally (although has been predicted using structure and sequence alignments, see <cite><del class="diffchange diffchange-inline">REF1</del></cite>).</div></td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>;First [[catalytic nucleophile]] identification: Not proven unequivocally (although has been predicted using structure and sequence alignments, see <cite><ins class="diffchange diffchange-inline">Gloster2008</ins></cite>).</div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>;First [[general acid/base]] residue identification: Not proven unequivocally (although has been predicted using structure and sequence alignments, see <cite><del class="diffchange diffchange-inline">REF1</del></cite>).</div></td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>;First [[general acid/base]] residue identification: Not proven unequivocally (although has been predicted using structure and sequence alignments, see <cite><ins class="diffchange diffchange-inline">Gloster2008</ins></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 3-D structure: A GH97 member from ''Bacteroides thetaiotaomicron'', SusB, was solved using X-ray crystallography by two groups <cite><del class="diffchange diffchange-inline">REF1;REF3</del></cite>.</div></td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>;First 3-D structure: A GH97 member from ''Bacteroides thetaiotaomicron'', SusB, was solved using X-ray crystallography by two groups <cite><ins class="diffchange diffchange-inline">Gloster2008 Kitamura2008</ins></cite>.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== 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 class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; 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="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">REF1 </del>pmid=18848471</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">Gloster2008 </ins>pmid=18848471</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">REF2 </del>pmid=1708385</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">Smith1991 </ins>pmid=1708385</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">REF3 </del>pmid=18981178</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">Kitamura2008 </ins>pmid=18981178</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">REF4 </del>pmid=16131397</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">Naumoff2005 </ins>pmid=16131397</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|GH097]]</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|GH097]]</div></td></tr>
</table>
Harry Brumer
https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_97&diff=2879&oldid=prev
Harry Brumer at 14:15, 8 November 2009
2009-11-08T14:15:58Z
<p></p>
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 14:15, 8 November 2009</td>
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<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;">{{CuratorApproved}}</ins></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>* [[Author]]: ^^^Tracey Gloster^^^</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>* [[Author]]: ^^^Tracey Gloster^^^</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>* [[Responsible Curator]]: ^^^Gideon Davies^^^</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>* [[Responsible Curator]]: ^^^Gideon Davies^^^</div></td></tr>
</table>
Harry Brumer
https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_97&diff=2221&oldid=prev
Spencer Williams: grammatical editing
2009-10-14T00:08:57Z
<p>grammatical editing</p>
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<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'>−</td><td style="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;"><!-- The data in the table below should be updated by the Author/Curator according to current information on the family --></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><div style="float:right"></div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div><div style="float:right"></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>{| {{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>
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<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Substrate specificities ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Substrate specificities ==</div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>Family 97 [[glycoside hydrolases]] hydrolyse α-linked D-<del class="diffchange diffchange-inline">glycosidic substrates</del>; the two enzymes from this family that have been characterised to date have α-glucosidase (EC 3.2.1.20) and α-galactosidase (EC 3.2.1.22) activity <cite>REF1</cite>. The <del class="diffchange diffchange-inline">alpha</del>-glucosidase from ''Bacteroides thetaiotaomicron'' has been characterised in the most detail, and has been demonstrated to hydrolyse substrates ranging from maltose to maltoheptaose in length, <del class="diffchange diffchange-inline"> </del>and those containing α-1,6-, α-1,3- and α-1,2-, as well as α-1,4-<del class="diffchange diffchange-inline">, </del>linkages <cite>REF2;REF3</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 97 [[glycoside hydrolases]] hydrolyse α-linked D-<ins class="diffchange diffchange-inline">glycosides</ins>; the two enzymes from this family that have been characterised to date have α-glucosidase (EC 3.2.1.20) and α-galactosidase (EC 3.2.1.22) activity <cite>REF1</cite>. The <ins class="diffchange diffchange-inline">α</ins>-glucosidase from ''Bacteroides thetaiotaomicron'' has been characterised in the most detail, and has been demonstrated to hydrolyse substrates ranging from maltose to maltoheptaose in length, and those containing α-1,6-, α-1,3- and α-1,2-, as well as α-1,4-linkages <cite>REF2;REF3</cite>.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Kinetics and Mechanism ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Kinetics and Mechanism ==</div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>Family GH97 is unusual as it contains both [[retaining]] and [[inverting]] enzymes, as shown unequivocally by NMR <cite>REF1</cite> and HPLC <cite>REF3</cite>, by characterization of two enzymes from ''Bacteroides thetaiotaomicron''. <del class="diffchange diffchange-inline">Both mechanisms are strongly </del>dependent on the presence of calcium, which coordinates the C2-OH group of the substrate in the -1 subsite, as well as four glutamate residues in the active site <cite>REF1</cite>. One of the glutamate residues coordinated by the calcium ion is predicted to be the [[general acid/base]] residue, which may receive acid assistance from the calcium during hydrolysis.</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 GH97 is unusual as it contains both [[retaining]] and [[inverting]] enzymes, as shown unequivocally by NMR <cite>REF1</cite> and HPLC <cite>REF3</cite> <ins class="diffchange diffchange-inline">analyses</ins>, by characterization of two enzymes from ''Bacteroides thetaiotaomicron''. <ins class="diffchange diffchange-inline">Catalysis is </ins>dependent on the presence of calcium, which coordinates the C2-OH group of the substrate in the -1 subsite, as well as four glutamate residues in the active site <cite>REF1</cite>. One of the glutamate residues coordinated by the calcium ion is predicted to be the [[general acid/base]] residue, which may receive acid assistance from the calcium during hydrolysis.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Catalytic Residues ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Catalytic Residues ==</div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>The constellation of glutamate residues (five in total, four of which coordinate the calcium ion) in the active site of the only ([[inverting]]) GH97 enzyme solved to date <del class="diffchange diffchange-inline"> </del>has made the assignment of catalytic residues difficult. Analysis of sequence alignments, structural alignments with family [[GH27]], and a mutant tested with substrates with different leaving group <del class="diffchange diffchange-inline">capacities</del>, has provided a likely candidate <del class="diffchange diffchange-inline">to act as </del>the [[general acid]] in this [[inverting]] enzyme or as the [[general acid/base]] in the [[retaining]] members of the family <cite>REF1</cite>. It is possible the calcium ion provides acid assistance to the acid/base during hydrolysis. The [[general base]] for the [[inverting]] enzyme has also been predicted on the basis of position in the active site; in addition it coordinates a water molecule in a <del class="diffchange diffchange-inline">prime </del>position for nucleophilic attack, and mutation causes the enzyme to be virtually inactive. Although a structure has not been solved for a retaining enzyme, the [[catalytic nucleophile]] for the [[retaining]] enzymes has been predicted based on sequence alignments and similarity to [[GH27]] enzymes to be <del class="diffchange diffchange-inline"> </del>an aspartate residue <cite>REF1</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 constellation of glutamate residues (five in total, four of which coordinate the calcium ion) in the active site of the only ([[inverting]]) GH97 enzyme <ins class="diffchange diffchange-inline">whose structure has been </ins>solved to date<ins class="diffchange diffchange-inline">, </ins>has made the assignment of catalytic residues difficult. Analysis of sequence alignments, structural alignments with family [[GH27]], and a mutant tested with substrates with different leaving group <ins class="diffchange diffchange-inline">abilities</ins>, has provided a likely candidate <ins class="diffchange diffchange-inline">for </ins>the [[general acid]] <ins class="diffchange diffchange-inline">residue </ins>in this [[inverting]] enzyme or as the [[general acid/base]] in the [[retaining]] members of the family <cite>REF1</cite>. It is possible <ins class="diffchange diffchange-inline">that </ins>the calcium ion provides acid assistance to the acid/base during hydrolysis. The [[general base]] for the [[inverting]] enzyme has also been predicted on the basis of <ins class="diffchange diffchange-inline">its </ins>position in the active site; in addition it coordinates a water molecule <ins class="diffchange diffchange-inline">that is situated </ins>in a position <ins class="diffchange diffchange-inline">primed </ins>for nucleophilic attack, and mutation causes the enzyme to be virtually inactive. Although a structure has not been solved for a retaining enzyme, the [[catalytic nucleophile]] for the [[retaining]] enzymes has been predicted based on sequence alignments<ins class="diffchange diffchange-inline">, </ins>and similarity to [[GH27]] enzymes<ins class="diffchange diffchange-inline">, </ins>to be an aspartate residue <cite>REF1</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-l39" >Line 39:</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>== Family Firsts ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Family Firsts ==</div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>;First sterochemistry determination: Two GH97 members from ''Bacteroides thetaiotaomicron'' were shown to differ in stereochemical outcome, by NMR <cite>REF1</cite> and HPLC <cite>REF3</cite>, demonstrating the family contains enzymes <del class="diffchange diffchange-inline">which </del>hydrolyse with both retention and inversion of stereochemistry.</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 sterochemistry determination: Two GH97 members from ''Bacteroides thetaiotaomicron'' were shown to differ in stereochemical outcome, by NMR <cite>REF1</cite> and HPLC <cite>REF3</cite> <ins class="diffchange diffchange-inline">analyses</ins>, demonstrating <ins class="diffchange diffchange-inline">that </ins>the family contains enzymes <ins class="diffchange diffchange-inline">that </ins>hydrolyse with both retention and inversion of <ins class="diffchange diffchange-inline">anomeric </ins>stereochemistry.</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 [[catalytic nucleophile]] identification: Not proven unequivocally (although has been predicted using structure and sequence alignments, see <cite>REF1</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 [[catalytic nucleophile]] identification: Not proven unequivocally (although has been predicted using structure and sequence alignments, see <cite>REF1</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 [[general acid/base]] residue identification: Not proven unequivocally (although has been predicted using structure and sequence alignments, see <cite>REF1</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: Not proven unequivocally (although has been predicted using structure and sequence alignments, see <cite>REF1</cite>).</div></td></tr>
<tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l53" >Line 53:</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></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="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;"><!-- ATTN CURATOR: Please delete the "<nowiki>" and "</nowiki>" tags below when you are ready for the page to be included in the "GH Families" category, which is linked on the Main Page; ALSO: REPLACE "nnn" with the family number) --></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>[[Category:Glycoside Hydrolase Families|GH097]]</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|GH097]]</div></td></tr>
</table>
Spencer Williams
https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_97&diff=2182&oldid=prev
Harry Brumer: /* Three-dimensional structures */
2009-10-06T05:39:51Z
<p><span dir="auto"><span class="autocomment">Three-dimensional structures</span></span></p>
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<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 05:39, 6 October 2009</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l36" >Line 36:</td>
<td colspan="2" class="diff-lineno">Line 36:</td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 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>There has been one structure solved, using X-ray crystallography, for a member of family GH97 (which inverts stereochemistry). This is an enzyme from ''Bacteroides thetaiotaomicron'', SusB, which is involved in the degradation of starch <del class="diffchange diffchange-inline">degradation </del>in the human gut. The tertiary structure of the GH97 enzyme revealed three domains; an N-terminal β-super-sandwich domain, followed by a canonical (β/α)8 barrel (which houses the catalytic domain) and a C-terminal β-sheet domain <cite>REF1;REF3</cite>. There have also been complexes solved with the inhibitors acarbose <cite>REF3</cite>, deoxynojirimycin and castanospermine <cite>REF1</cite>. Structural alignments show similarity to families GH27 and GH36 (as predicted previously by a bioinformatics study <cite>REF4</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>There has been one structure solved, using X-ray crystallography, for a member of family GH97 (which inverts stereochemistry). This is an enzyme from ''Bacteroides thetaiotaomicron'', SusB, which is involved in the degradation of starch in the human gut. The tertiary structure of the GH97 enzyme revealed three domains; an N-terminal β-super-sandwich domain, followed by a canonical (β/α)8 barrel (which houses the catalytic domain) and a C-terminal β-sheet domain <cite>REF1;REF3</cite>. There have also been complexes solved with the inhibitors acarbose <cite>REF3</cite>, deoxynojirimycin and castanospermine <cite>REF1</cite>. Structural alignments show similarity to families <ins class="diffchange diffchange-inline">[[</ins>GH27<ins class="diffchange diffchange-inline">]] </ins>and <ins class="diffchange diffchange-inline">[[</ins>GH36<ins class="diffchange diffchange-inline">]] </ins>(as predicted previously by a bioinformatics study <cite>REF4</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> </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>
</table>
Harry Brumer
https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_97&diff=2181&oldid=prev
Harry Brumer: /* Catalytic Residues */
2009-10-06T05:38:55Z
<p><span dir="auto"><span class="autocomment">Catalytic Residues</span></span></p>
<table class="diff diff-contentalign-left diff-editfont-monospace" data-mw="interface">
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">← Older revision</td>
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 05:38, 6 October 2009</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l33" >Line 33:</td>
<td colspan="2" class="diff-lineno">Line 33:</td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Catalytic Residues ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Catalytic Residues ==</div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>The constellation of glutamate residues (five in total, four of which coordinate the calcium ion) in the active site of the only ([[inverting]]) GH97 enzyme solved to date has made the assignment of catalytic residues difficult. Analysis of sequence alignments, structural alignments with family GH27, and a mutant tested with substrates with different leaving group capacities, has provided a likely candidate to act as the [[general acid]] in this [[inverting]] enzyme or as the [[general acid/base]] in the [[retaining]] members of the family <cite>REF1</cite>. It is possible the calcium ion provides acid assistance to the acid/base during hydrolysis. The [[general base]] for the [[inverting]] enzyme has also been predicted on the basis of position in the active site; in addition it coordinates a water molecule in a prime position for nucleophilic attack, and mutation causes the enzyme to be virtually inactive. Although a structure has not been solved for a retaining enzyme, the [[catalytic nucleophile]] for the [[retaining]] enzymes has been predicted based on sequence alignments and similarity to GH27 enzymes to be an aspartate residue <cite>REF1</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 constellation of glutamate residues (five in total, four of which coordinate the calcium ion) in the active site of the only ([[inverting]]) GH97 enzyme solved to date has made the assignment of catalytic residues difficult. Analysis of sequence alignments, structural alignments with family <ins class="diffchange diffchange-inline">[[</ins>GH27<ins class="diffchange diffchange-inline">]]</ins>, and a mutant tested with substrates with different leaving group capacities, has provided a likely candidate to act as the [[general acid]] in this [[inverting]] enzyme or as the [[general acid/base]] in the [[retaining]] members of the family <cite>REF1</cite>. It is possible the calcium ion provides acid assistance to the acid/base during hydrolysis. The [[general base]] for the [[inverting]] enzyme has also been predicted on the basis of position in the active site; in addition it coordinates a water molecule in a prime position for nucleophilic attack, and mutation causes the enzyme to be virtually inactive. Although a structure has not been solved for a retaining enzyme, the [[catalytic nucleophile]] for the [[retaining]] enzymes has been predicted based on sequence alignments and similarity to <ins class="diffchange diffchange-inline">[[</ins>GH27<ins class="diffchange diffchange-inline">]] </ins>enzymes to be an aspartate residue <cite>REF1</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>
Harry Brumer
https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_97&diff=2180&oldid=prev
Harry Brumer at 05:37, 6 October 2009
2009-10-06T05:37:24Z
<p></p>
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 05:37, 6 October 2009</td>
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<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div><del style="font-weight: bold; text-decoration: none;"><!-- CURATORS: Please delete the {{UnderConstruction}} tag below when the page is ready for wider public consumption --></del></div></td><td colspan="2"> </td></tr>
<tr><td class='diff-marker'>−</td><td style="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>* [[Author]]: ^^^Tracey Gloster^^^</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>* [[Author]]: ^^^Tracey Gloster^^^</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>* [[Responsible Curator]]: ^^^Gideon Davies^^^</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>* [[Responsible Curator]]: ^^^Gideon Davies^^^</div></td></tr>
</table>
Harry Brumer
https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_97&diff=2179&oldid=prev
Harry Brumer at 05:36, 6 October 2009
2009-10-06T05:36:54Z
<p></p>
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 05:36, 6 October 2009</td>
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<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div><!-- ATTN CURATOR: Please delete the "<nowiki>" and "</nowiki>" tags below when you are ready for the page to be included in the "GH Families" category, which is linked on the Main Page; ALSO: REPLACE "nnn" with the family number) --></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><!-- ATTN CURATOR: Please delete the "<nowiki>" and "</nowiki>" tags below when you are ready for the page to be included in the "GH Families" category, which is linked on the Main Page; ALSO: REPLACE "nnn" with the family number) --></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>[[Category:Glycoside Hydrolase Families|<del class="diffchange diffchange-inline">GH97</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>[[Category:Glycoside Hydrolase Families|<ins class="diffchange diffchange-inline">GH097</ins>]]</div></td></tr>
</table>
Harry Brumer
https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_97&diff=2173&oldid=prev
Gideon Davies at 19:10, 5 October 2009
2009-10-05T19:10:45Z
<p></p>
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 19:10, 5 October 2009</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><!-- CURATORS: Please delete the {{UnderConstruction}} tag below when the page is ready for wider public consumption --></div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div><!-- CURATORS: Please delete the {{UnderConstruction}} tag below when the page is ready for wider public consumption --></div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div><del class="diffchange diffchange-inline">{{UnderConstruction}}</del></div></td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div> </div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>* [[Author]]: ^^^Tracey Gloster^^^</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>* [[Author]]: ^^^Tracey Gloster^^^</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>* [[Responsible Curator]]: ^^^Gideon Davies^^^</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>* [[Responsible Curator]]: ^^^Gideon Davies^^^</div></td></tr>
<tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l29" >Line 29:</td>
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<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Substrate specificities ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Substrate specificities ==</div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>Family 97 [[glycoside hydrolases]] hydrolyse α-linked substrates; the two enzymes from this family that have been characterised to date have α-glucosidase (EC 3.2.1.20) and α-galactosidase (EC 3.2.1.22) activity <cite>REF1</cite>. The alpha-glucosidase from ''Bacteroides thetaiotaomicron'' has been characterised in the most detail, and has been demonstrated to hydrolyse substrates ranging from maltose to maltoheptaose in length, and those containing α-1,6-, α-1,3- and α-1,2-, as well as α-1,4-, linkages <cite>REF2;REF3</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 97 [[glycoside hydrolases]] hydrolyse α-linked <ins class="diffchange diffchange-inline">D-glycosidic </ins>substrates; the two enzymes from this family that have been characterised to date have α-glucosidase (EC 3.2.1.20) and α-galactosidase (EC 3.2.1.22) activity <cite>REF1</cite>. The alpha-glucosidase from ''Bacteroides thetaiotaomicron'' has been characterised in the most detail, and has been demonstrated to hydrolyse substrates ranging from maltose to maltoheptaose in length, and those containing α-1,6-, α-1,3- and α-1,2-, as well as α-1,4-, linkages <cite>REF2;REF3</cite>.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Kinetics and Mechanism ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Kinetics and Mechanism ==</div></td></tr>
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<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Catalytic Residues ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Catalytic Residues ==</div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>The constellation of glutamate residues in the active site of the only ([[inverting]]) GH97 enzyme solved to date <del class="diffchange diffchange-inline">(five in total, four of which coordinate the calcium ion) </del>has made the assignment of catalytic residues difficult. Analysis of sequence alignments, structural alignments with family GH27, and a mutant tested with substrates with different leaving group capacities, has provided a likely candidate to act as the [[general acid]] in this [[inverting]] enzyme or as the [[general acid/base]] in the [[retaining]] members of the family <cite>REF1</cite>. It is possible the calcium ion provides acid assistance to the acid/base during hydrolysis. The [[general base]] for the [[inverting]] enzyme has also been predicted on the basis of position in the active site; in addition it coordinates a water molecule in a prime position for nucleophilic attack, and mutation causes the enzyme to be virtually inactive. Although a structure has not been solved for a retaining enzyme, the [[catalytic nucleophile]] for the [[retaining]] enzymes has been predicted based on sequence alignments and similarity to GH27 enzymes to be an aspartate residue <cite>REF1</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 constellation of glutamate residues <ins class="diffchange diffchange-inline">(five in total, four of which coordinate the calcium ion) </ins>in the active site of the only ([[inverting]]) GH97 enzyme solved to date <ins class="diffchange diffchange-inline"> </ins>has made the assignment of catalytic residues difficult. Analysis of sequence alignments, structural alignments with family GH27, and a mutant tested with substrates with different leaving group capacities, has provided a likely candidate to act as the [[general acid]] in this [[inverting]] enzyme or as the [[general acid/base]] in the [[retaining]] members of the family <cite>REF1</cite>. It is possible the calcium ion provides acid assistance to the acid/base during hydrolysis. The [[general base]] for the [[inverting]] enzyme has also been predicted on the basis of position in the active site; in addition it coordinates a water molecule in a prime position for nucleophilic attack, and mutation causes the enzyme to be virtually inactive. Although a structure has not been solved for a retaining enzyme, the [[catalytic nucleophile]] for the [[retaining]] enzymes has been predicted based on sequence alignments and similarity to GH27 enzymes to be an aspartate residue <cite>REF1</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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<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 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><!-- ATTN CURATOR: Please delete the "<nowiki>" and "</nowiki>" tags below when you are ready for the page to be included in the "GH Families" category, which is linked on the Main Page; ALSO: REPLACE "nnn" with the family number) --></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><!-- ATTN CURATOR: Please delete the "<nowiki>" and "</nowiki>" tags below when you are ready for the page to be included in the "GH Families" category, which is linked on the Main Page; ALSO: REPLACE "nnn" with the family number) --></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"><nowiki></del>[[Category:Glycoside Hydrolase Families|<del class="diffchange diffchange-inline">GHnnn</del>]]<del class="diffchange diffchange-inline"></nowiki></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>[[Category:Glycoside Hydrolase Families|<ins class="diffchange diffchange-inline">GH97</ins>]]</div></td></tr>
</table>
Gideon Davies
https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_97&diff=2163&oldid=prev
Spencer Williams: /* Family Firsts */
2009-10-03T04:15:39Z
<p><span dir="auto"><span class="autocomment">Family Firsts</span></span></p>
<table class="diff diff-contentalign-left diff-editfont-monospace" data-mw="interface">
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">← Older revision</td>
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 04:15, 3 October 2009</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l43" >Line 43:</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 sterochemistry determination: Two GH97 members from ''Bacteroides thetaiotaomicron'' were shown to differ in stereochemical outcome, by NMR <cite>REF1</cite> and HPLC <cite>REF3</cite>, demonstrating the family contains enzymes which hydrolyse with both retention and inversion of stereochemistry.</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>;First sterochemistry determination: Two GH97 members from ''Bacteroides thetaiotaomicron'' were shown to differ in stereochemical outcome, by NMR <cite>REF1</cite> and HPLC <cite>REF3</cite>, demonstrating the family contains enzymes which hydrolyse with both retention and inversion of stereochemistry.</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: Not proven unequivocally (although has been predicted using structure and sequence alignments, see <cite>REF1</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>catalytic nucleophile<ins class="diffchange diffchange-inline">]] </ins>identification: Not proven unequivocally (although has been predicted using structure and sequence alignments, see <cite>REF1</cite>).</div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>;First general acid/base residue identification: Not proven unequivocally (although has been predicted using structure and sequence alignments, see <cite>REF1</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: Not proven unequivocally (although has been predicted using structure and sequence alignments, see <cite>REF1</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: A GH97 member from ''Bacteroides thetaiotaomicron'', SusB, was solved using X-ray crystallography by two groups <cite>REF1;REF3</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: A GH97 member from ''Bacteroides thetaiotaomicron'', SusB, was solved using X-ray crystallography by two groups <cite>REF1;REF3</cite>.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
</table>
Spencer Williams