https://www.cazypedia.org/index.php?title=Polysaccharide_Lyase_Family_7&feed=atom&action=historyPolysaccharide Lyase Family 7 - Revision history2024-03-29T08:21:34ZRevision history for this page on the wikiMediaWiki 1.35.10https://www.cazypedia.org/index.php?title=Polysaccharide_Lyase_Family_7&diff=16481&oldid=prevHarry Brumer: Text replacement - "\^\^\^(.*)\^\^\^" to "$1"2021-12-18T21:14:23Z<p>Text replacement - "\^\^\^(.*)\^\^\^" to "<a href="/index.php?title=User:$1&action=edit&redlink=1" class="new" title="User:$1 (page does not exist)">$1</a>"</p>
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<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>* [[Author]]s: <del class="diffchange diffchange-inline">^^^</del>Nadine Gerlach<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]]s: <ins class="diffchange diffchange-inline">[[User:Nadine Gerlach|</ins>Nadine Gerlach<ins class="diffchange diffchange-inline">]] </ins></div></td></tr>
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</table>Harry Brumerhttps://www.cazypedia.org/index.php?title=Polysaccharide_Lyase_Family_7&diff=15416&oldid=prevNadine Gerlach at 16:11, 20 June 20202020-06-20T16:11:07Z<p></p>
<table class="diff diff-contentalign-left diff-editfont-monospace" data-mw="interface">
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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>== 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="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>[[Image:PL7SF_Thomasetal2013.JPG|thumb|400px|'''Figure 2. Subfamilies of PL7s''' <cite>Thomas2013</cite>. Unrooted tree with bootstrap values after maximum likelihood analysis. Number refer to Uniprot accession numbers. Red dots indicate enzymes from ''Z. galactanivorans''. Pink triangles indicate enzymes characterized biochemically. Blue squares indicate that the structure of the protein has been solved.]]</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>[[Image:PL7SF_Thomasetal2013.JPG|thumb|400px|'''Figure 2. Subfamilies of PL7s''' <cite>Thomas2013</cite>. Unrooted tree with bootstrap values after maximum likelihood analysis. Number refer to Uniprot accession numbers. Red dots indicate enzymes from ''Z. galactanivorans''. Pink triangles indicate enzymes characterized biochemically. Blue squares indicate that the structure of the protein has been solved.]]</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>[[Polysaccharide_Lyases|Polysaccharide <del class="diffchange diffchange-inline">lyases</del>]] family 7 (PL7) contains five subfamilies (SF) based on their sequence similarities <cite>Lombard2010</cite>, plus a so far uncharacterized sixth subfamily, which consist only of marine representatives of the Flavobacteriaceae (Figure 2) <cite>Thomas2013</cite>. The substrate specificity depends on the source of alginate, i.e. derived from brown seaweed or mucoid bacteria ''Pseudomonas'' spp. and ''Azotobacter vinelandii'', as well as geographical and seasonal parameters. Alginate is a heteropolysaccharide, consisting of β-D-mannuronate (M) and α-L-guluronate (G). These monosaccharides can occur in homogenous and heterogenous blocks. In addition, bacterial alginate is often acetylated at the C2 and / or C3 of mannuronate, thereby shielding the substrate from degradation. Hence, PL7s can be mannuronate ([{{EClink}}4.2.2.3 EC 4.2.2.3]), guluronate ([{{EClink}}4.2.2.11 EC 4.2.2.11]) or mixed link (EC 4.2.2.-) specific lyases. Despite the preference for M- or G-enriched blocks, most PL7 also have a low to moderate activity at the other building block <cite>Thomas2013 Badur2015 Sim2017</cite>. PolyG specific PL7 have been found in the SF3 and SF5 <cite>Thomas2013</cite> with QIH in the second highly conserved region, while polyM specific PL7s are characterized by QVH <cite>Zhu2015 Deng2014</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>[[Polysaccharide_Lyases|Polysaccharide <ins class="diffchange diffchange-inline">lyase</ins>]] family 7 (PL7) contains five subfamilies (SF) based on their sequence similarities <cite>Lombard2010</cite>, plus a so far uncharacterized sixth subfamily, which consist only of marine representatives of the Flavobacteriaceae (Figure 2) <cite>Thomas2013</cite>. The substrate specificity depends on the source of alginate, i.e. derived from brown seaweed or mucoid bacteria ''Pseudomonas'' spp. and ''Azotobacter vinelandii'', as well as geographical and seasonal parameters. Alginate is a heteropolysaccharide, consisting of β-D-mannuronate (M) and α-L-guluronate (G). These monosaccharides can occur in homogenous and heterogenous blocks. In addition, bacterial alginate is often acetylated at the C2 and / or C3 of mannuronate, thereby shielding the substrate from degradation. Hence, PL7s can be mannuronate ([{{EClink}}4.2.2.3 EC 4.2.2.3]), guluronate ([{{EClink}}4.2.2.11 EC 4.2.2.11]) or mixed link (EC 4.2.2.-) specific lyases. Despite the preference for M- or G-enriched blocks, most PL7 also have a low to moderate activity at the other building block <cite>Thomas2013 Badur2015 Sim2017</cite>. PolyG specific PL7 have been found in the SF3 and SF5 <cite>Thomas2013</cite> with QIH in the second highly conserved region, while polyM specific PL7s are characterized by QVH <cite>Zhu2015 Deng2014</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>Nadine Gerlachhttps://www.cazypedia.org/index.php?title=Polysaccharide_Lyase_Family_7&diff=15415&oldid=prevNadine Gerlach at 16:10, 20 June 20202020-06-20T16:10:45Z<p></p>
<table class="diff diff-contentalign-left diff-editfont-monospace" data-mw="interface">
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 16:10, 20 June 2020</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>== 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="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>[[Image:PL7SF_Thomasetal2013.JPG|thumb|400px|'''Figure 2. Subfamilies of PL7s''' <cite>Thomas2013</cite>. Unrooted tree with bootstrap values after maximum likelihood analysis. Number refer to Uniprot accession numbers. Red dots indicate enzymes from ''Z. galactanivorans''. Pink triangles indicate enzymes characterized biochemically. Blue squares indicate that the structure of the protein has been solved.]]</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>[[Image:PL7SF_Thomasetal2013.JPG|thumb|400px|'''Figure 2. Subfamilies of PL7s''' <cite>Thomas2013</cite>. Unrooted tree with bootstrap values after maximum likelihood analysis. Number refer to Uniprot accession numbers. Red dots indicate enzymes from ''Z. galactanivorans''. Pink triangles indicate enzymes characterized biochemically. Blue squares indicate that the structure of the protein has been solved.]]</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>Polysaccharide <del class="diffchange diffchange-inline">lyase </del>family 7 (PL7) contains five subfamilies (SF) based on their sequence similarities <cite>Lombard2010</cite>, plus a so far uncharacterized sixth subfamily, which consist only of marine representatives of the Flavobacteriaceae (Figure 2) <cite>Thomas2013</cite>. The substrate specificity depends on the source of alginate, i.e. derived from brown seaweed or mucoid bacteria ''Pseudomonas'' spp. and ''Azotobacter vinelandii'', as well as geographical and seasonal parameters. Alginate is a heteropolysaccharide, consisting of β-D-mannuronate (M) and α-L-guluronate (G). These monosaccharides can occur in homogenous and heterogenous blocks. In addition, bacterial alginate is often acetylated at the C2 and / or C3 of mannuronate, thereby shielding the substrate from degradation. Hence, PL7s can be mannuronate ([{{EClink}}4.2.2.3 EC 4.2.2.3]), guluronate ([{{EClink}}4.2.2.11 EC 4.2.2.11]) or mixed link (EC 4.2.2.-) specific lyases. Despite the preference for M- or G-enriched blocks, most PL7 also have a low to moderate activity at the other building block <cite>Thomas2013 Badur2015 Sim2017</cite>. PolyG specific PL7 have been found in the SF3 and SF5 <cite>Thomas2013</cite> with QIH in the second highly conserved region, while polyM specific PL7s are characterized by QVH <cite>Zhu2015 Deng2014</cite>.</div></td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins class="diffchange diffchange-inline">[[Polysaccharide_Lyases|</ins>Polysaccharide <ins class="diffchange diffchange-inline">lyases]] </ins>family 7 (PL7) contains five subfamilies (SF) based on their sequence similarities <cite>Lombard2010</cite>, plus a so far uncharacterized sixth subfamily, which consist only of marine representatives of the Flavobacteriaceae (Figure 2) <cite>Thomas2013</cite>. The substrate specificity depends on the source of alginate, i.e. derived from brown seaweed or mucoid bacteria ''Pseudomonas'' spp. and ''Azotobacter vinelandii'', as well as geographical and seasonal parameters. Alginate is a heteropolysaccharide, consisting of β-D-mannuronate (M) and α-L-guluronate (G). These monosaccharides can occur in homogenous and heterogenous blocks. In addition, bacterial alginate is often acetylated at the C2 and / or C3 of mannuronate, thereby shielding the substrate from degradation. Hence, PL7s can be mannuronate ([{{EClink}}4.2.2.3 EC 4.2.2.3]), guluronate ([{{EClink}}4.2.2.11 EC 4.2.2.11]) or mixed link (EC 4.2.2.-) specific lyases. Despite the preference for M- or G-enriched blocks, most PL7 also have a low to moderate activity at the other building block <cite>Thomas2013 Badur2015 Sim2017</cite>. PolyG specific PL7 have been found in the SF3 and SF5 <cite>Thomas2013</cite> with QIH in the second highly conserved region, while polyM specific PL7s are characterized by QVH <cite>Zhu2015 Deng2014</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>Nadine Gerlachhttps://www.cazypedia.org/index.php?title=Polysaccharide_Lyase_Family_7&diff=15414&oldid=prevNadine Gerlach at 16:09, 20 June 20202020-06-20T16:09:44Z<p></p>
<table class="diff diff-contentalign-left diff-editfont-monospace" data-mw="interface">
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 16:09, 20 June 2020</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>== 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>== Mechanism ==</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>[[Image:AlyPL7 MultipleSequenceAlignment.JPG|thumb|400px|'''Figure 1. Multiple protein sequence alignment of Aly PL7 ''' as well as a secondary structure prediction with the crystallized PL7 from ''Klabsiella pneumoniae'' ([{{PDBlink}}4OZX PDB ID 4OZX]). Conserved residues in the homologues are colored in red and (putative) catalytic residues are indicated by a star. The multiple protein sequence alignment was done with Espript3.0 <cite>Robert2014</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>[[Image:AlyPL7 MultipleSequenceAlignment.JPG|thumb|400px|'''Figure 1. Multiple protein sequence alignment of Aly PL7 ''' as well as a secondary structure prediction with the crystallized PL7 from ''Klabsiella pneumoniae'' ([{{PDBlink}}4OZX PDB ID 4OZX]). Conserved residues in the homologues are colored in red and (putative) catalytic residues are indicated by a star. The multiple protein sequence alignment was done with Espript3.0 <cite>Robert2014</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>Alginate [[lyases<del class="diffchange diffchange-inline">|Polysaccharide Lyases</del>]] (Alys) from all families ([[PL5]], [[PL6]], PL7, [[PL14]], [[PL15]], [[PL17]], and [[PL18]]), catalyze the depolymerization of alginate in three steps: (I) removal of the negative charge on the carboxylate anion, (II) general base-catalyzed abstraction of the proton on the C5 and (III) β-elimination of the 4-O-glycosidic bond <cite>Gacesa1986</cite>. Most PL7s are endo-active, i.e. acting within a poly- or oligosaccharide and releasing smaller alginate fragments. Some PL7 are exo-acting cleaving a monosaccharide from the non-reducing end of the polymer <cite>Thomas2013</cite>. In both modes of action, a new non-reducing end with a 4-deoxy-L-erythro-hex-4-en pyranosyl uronate residue (Δ) is formed.</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>Alginate [[<ins class="diffchange diffchange-inline">Polysaccharide_Lyases|</ins>lyases]] (Alys) from all families ([[PL5]], [[PL6]], PL7, [[PL14]], [[PL15]], [[PL17]], and [[PL18]]), catalyze the depolymerization of alginate in three steps: (I) removal of the negative charge on the carboxylate anion, (II) general base-catalyzed abstraction of the proton on the C5 and (III) β-elimination of the 4-O-glycosidic bond <cite>Gacesa1986</cite>. Most PL7s are endo-active, i.e. acting within a poly- or oligosaccharide and releasing smaller alginate fragments. Some PL7 are exo-acting cleaving a monosaccharide from the non-reducing end of the polymer <cite>Thomas2013</cite>. In both modes of action, a new non-reducing end with a 4-deoxy-L-erythro-hex-4-en pyranosyl uronate residue (Δ) is formed.</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>Some marine PL7 alginate lyases require a calcium cation for substrate recognition and binding <cite>Thomas2013</cite>. Ca<sup>2+</sup> is weakening the ionic interactions between substrate (polyanion) and PL7 (polycation) by reducing the surface density of the alginate charge and therefore increasing the enzyme activity <cite>Favorov1979</cite>. However, there have also been reports of mono- or divalent (metal) cations not increasing or even decreasing enzymatic activity <cite>Jagtap2014 Badur2015</cite>. Therefore, it is not clear if Ca<sup>2+</sup> is required for recognition and / or binding of alginate PL7s. Nevertheless, one could speculate if cations like Ca<sup>2+</sup> are creating a more accessible form of alginate. In the presence of divalent cations, the confirmation of alginate is changed due to cross linkages with guluronate residues from opposing chains forming a so-called egg box model <cite>Grant1973</cite>. Thereby, the 3D confirmation of alginate is changed, forming hydrogels which might be an easier target for the enzyme in the marine environment thanits dissolved form.</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>Some marine PL7 alginate lyases require a calcium cation for substrate recognition and binding <cite>Thomas2013</cite>. Ca<sup>2+</sup> is weakening the ionic interactions between substrate (polyanion) and PL7 (polycation) by reducing the surface density of the alginate charge and therefore increasing the enzyme activity <cite>Favorov1979</cite>. However, there have also been reports of mono- or divalent (metal) cations not increasing or even decreasing enzymatic activity <cite>Jagtap2014 Badur2015</cite>. Therefore, it is not clear if Ca<sup>2+</sup> is required for recognition and / or binding of alginate PL7s. Nevertheless, one could speculate if cations like Ca<sup>2+</sup> are creating a more accessible form of alginate. In the presence of divalent cations, the confirmation of alginate is changed due to cross linkages with guluronate residues from opposing chains forming a so-called egg box model <cite>Grant1973</cite>. Thereby, the 3D confirmation of alginate is changed, forming hydrogels which might be an easier target for the enzyme in the marine environment thanits dissolved form.</div></td></tr>
</table>Nadine Gerlachhttps://www.cazypedia.org/index.php?title=Polysaccharide_Lyase_Family_7&diff=15413&oldid=prevNadine Gerlach at 16:07, 20 June 20202020-06-20T16:07:31Z<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 16:07, 20 June 2020</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;"><div>== 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>== Mechanism ==</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>[[Image:AlyPL7 MultipleSequenceAlignment.JPG|thumb|400px|'''Figure 1. Multiple protein sequence alignment of Aly PL7 ''' as well as a secondary structure prediction with the crystallized PL7 from ''Klabsiella pneumoniae'' ([{{PDBlink}}4OZX PDB ID 4OZX]). Conserved residues in the homologues are colored in red and (putative) catalytic residues are indicated by a star. The multiple protein sequence alignment was done with Espript3.0 <cite>Robert2014</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>[[Image:AlyPL7 MultipleSequenceAlignment.JPG|thumb|400px|'''Figure 1. Multiple protein sequence alignment of Aly PL7 ''' as well as a secondary structure prediction with the crystallized PL7 from ''Klabsiella pneumoniae'' ([{{PDBlink}}4OZX PDB ID 4OZX]). Conserved residues in the homologues are colored in red and (putative) catalytic residues are indicated by a star. The multiple protein sequence alignment was done with Espript3.0 <cite>Robert2014</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>Alginate lyases (Alys) from all families ([[PL5]], [[PL6]], PL7, [[PL14]], [[PL15]], [[PL17]], and [[PL18]]), catalyze the depolymerization of alginate in three steps: (I) removal of the negative charge on the carboxylate anion, (II) general base-catalyzed abstraction of the proton on the C5 and (III) β-elimination of the 4-O-glycosidic bond <cite>Gacesa1986</cite>. Most PL7s are endo-active, i.e. acting within a poly- or oligosaccharide and releasing smaller alginate fragments. Some PL7 are exo-acting cleaving a monosaccharide from the non-reducing end of the polymer <cite>Thomas2013</cite>. In both modes of action, a new non-reducing end with a 4-deoxy-L-erythro-hex-4-en pyranosyl uronate residue (Δ) is formed.</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>Alginate <ins class="diffchange diffchange-inline">[[</ins>lyases<ins class="diffchange diffchange-inline">|Polysaccharide Lyases]] </ins>(Alys) from all families ([[PL5]], [[PL6]], PL7, [[PL14]], [[PL15]], [[PL17]], and [[PL18]]), catalyze the depolymerization of alginate in three steps: (I) removal of the negative charge on the carboxylate anion, (II) general base-catalyzed abstraction of the proton on the C5 and (III) β-elimination of the 4-O-glycosidic bond <cite>Gacesa1986</cite>. Most PL7s are endo-active, i.e. acting within a poly- or oligosaccharide and releasing smaller alginate fragments. Some PL7 are exo-acting cleaving a monosaccharide from the non-reducing end of the polymer <cite>Thomas2013</cite>. In both modes of action, a new non-reducing end with a 4-deoxy-L-erythro-hex-4-en pyranosyl uronate residue (Δ) is formed.</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>Some marine PL7 alginate lyases require a calcium cation for substrate recognition and binding <cite>Thomas2013</cite>. Ca<sup>2+</sup> is weakening the ionic interactions between substrate (polyanion) and PL7 (polycation) by reducing the surface density of the alginate charge and therefore increasing the enzyme activity <cite>Favorov1979</cite>. However, there have also been reports of mono- or divalent (metal) cations not increasing or even decreasing enzymatic activity <cite>Jagtap2014 Badur2015</cite>. Therefore, it is not clear if Ca<sup>2+</sup> is required for recognition and / or binding of alginate PL7s. Nevertheless, one could speculate if cations like Ca<sup>2+</sup> are creating a more accessible form of alginate. In the presence of divalent cations, the confirmation of alginate is changed due to cross linkages with guluronate residues from opposing chains forming a so-called egg box model <cite>Grant1973</cite>. Thereby, the 3D confirmation of alginate is changed, forming hydrogels which might be an easier target for the enzyme in the marine environment thanits dissolved form.</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>Some marine PL7 alginate lyases require a calcium cation for substrate recognition and binding <cite>Thomas2013</cite>. Ca<sup>2+</sup> is weakening the ionic interactions between substrate (polyanion) and PL7 (polycation) by reducing the surface density of the alginate charge and therefore increasing the enzyme activity <cite>Favorov1979</cite>. However, there have also been reports of mono- or divalent (metal) cations not increasing or even decreasing enzymatic activity <cite>Jagtap2014 Badur2015</cite>. Therefore, it is not clear if Ca<sup>2+</sup> is required for recognition and / or binding of alginate PL7s. Nevertheless, one could speculate if cations like Ca<sup>2+</sup> are creating a more accessible form of alginate. In the presence of divalent cations, the confirmation of alginate is changed due to cross linkages with guluronate residues from opposing chains forming a so-called egg box model <cite>Grant1973</cite>. Thereby, the 3D confirmation of alginate is changed, forming hydrogels which might be an easier target for the enzyme in the marine environment thanits dissolved form.</div></td></tr>
</table>Nadine Gerlachhttps://www.cazypedia.org/index.php?title=Polysaccharide_Lyase_Family_7&diff=15412&oldid=prevNadine Gerlach at 16:05, 20 June 20202020-06-20T16:05:34Z<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 16:05, 20 June 2020</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;"><div>== 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>== Mechanism ==</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>[[Image:AlyPL7 MultipleSequenceAlignment.JPG|thumb|400px|'''Figure 1. Multiple protein sequence alignment of Aly PL7 ''' as well as a secondary structure prediction with the crystallized PL7 from ''Klabsiella pneumoniae'' ([{{PDBlink}}4OZX PDB ID 4OZX]). Conserved residues in the homologues are colored in red and (putative) catalytic residues are indicated by a star. The multiple protein sequence alignment was done with Espript3.0 <cite>Robert2014</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>[[Image:AlyPL7 MultipleSequenceAlignment.JPG|thumb|400px|'''Figure 1. Multiple protein sequence alignment of Aly PL7 ''' as well as a secondary structure prediction with the crystallized PL7 from ''Klabsiella pneumoniae'' ([{{PDBlink}}4OZX PDB ID 4OZX]). Conserved residues in the homologues are colored in red and (putative) catalytic residues are indicated by a star. The multiple protein sequence alignment was done with Espript3.0 <cite>Robert2014</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>Alginate <del class="diffchange diffchange-inline">[[https://www.cazypedia.org/index.php/Polysaccharide_Lyases]] </del>(Alys) from all families ([[PL5]], [[PL6]], PL7, [[PL14]], [[PL15]], [[PL17]], and [[PL18]]), catalyze the depolymerization of alginate in three steps: (I) removal of the negative charge on the carboxylate anion, (II) general base-catalyzed abstraction of the proton on the C5 and (III) β-elimination of the 4-O-glycosidic bond <cite>Gacesa1986</cite>. Most PL7s are endo-active, i.e. acting within a poly- or oligosaccharide and releasing smaller alginate fragments. Some PL7 are exo-acting cleaving a monosaccharide from the non-reducing end of the polymer <cite>Thomas2013</cite>. In both modes of action, a new non-reducing end with a 4-deoxy-L-erythro-hex-4-en pyranosyl uronate residue (Δ) is formed.</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>Alginate <ins class="diffchange diffchange-inline">lyases </ins>(Alys) from all families ([[PL5]], [[PL6]], PL7, [[PL14]], [[PL15]], [[PL17]], and [[PL18]]), catalyze the depolymerization of alginate in three steps: (I) removal of the negative charge on the carboxylate anion, (II) general base-catalyzed abstraction of the proton on the C5 and (III) β-elimination of the 4-O-glycosidic bond <cite>Gacesa1986</cite>. Most PL7s are endo-active, i.e. acting within a poly- or oligosaccharide and releasing smaller alginate fragments. Some PL7 are exo-acting cleaving a monosaccharide from the non-reducing end of the polymer <cite>Thomas2013</cite>. In both modes of action, a new non-reducing end with a 4-deoxy-L-erythro-hex-4-en pyranosyl uronate residue (Δ) is formed.</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>Some marine PL7 alginate lyases require a calcium cation for substrate recognition and binding <cite>Thomas2013</cite>. Ca<sup>2+</sup> is weakening the ionic interactions between substrate (polyanion) and PL7 (polycation) by reducing the surface density of the alginate charge and therefore increasing the enzyme activity <cite>Favorov1979</cite>. However, there have also been reports of mono- or divalent (metal) cations not increasing or even decreasing enzymatic activity <cite>Jagtap2014 Badur2015</cite>. Therefore, it is not clear if Ca<sup>2+</sup> is required for recognition and / or binding of alginate PL7s. Nevertheless, one could speculate if cations like Ca<sup>2+</sup> are creating a more accessible form of alginate. In the presence of divalent cations, the confirmation of alginate is changed due to cross linkages with guluronate residues from opposing chains forming a so-called egg box model <cite>Grant1973</cite>. Thereby, the 3D confirmation of alginate is changed, forming hydrogels which might be an easier target for the enzyme in the marine environment thanits dissolved form.</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>Some marine PL7 alginate lyases require a calcium cation for substrate recognition and binding <cite>Thomas2013</cite>. Ca<sup>2+</sup> is weakening the ionic interactions between substrate (polyanion) and PL7 (polycation) by reducing the surface density of the alginate charge and therefore increasing the enzyme activity <cite>Favorov1979</cite>. However, there have also been reports of mono- or divalent (metal) cations not increasing or even decreasing enzymatic activity <cite>Jagtap2014 Badur2015</cite>. Therefore, it is not clear if Ca<sup>2+</sup> is required for recognition and / or binding of alginate PL7s. Nevertheless, one could speculate if cations like Ca<sup>2+</sup> are creating a more accessible form of alginate. In the presence of divalent cations, the confirmation of alginate is changed due to cross linkages with guluronate residues from opposing chains forming a so-called egg box model <cite>Grant1973</cite>. Thereby, the 3D confirmation of alginate is changed, forming hydrogels which might be an easier target for the enzyme in the marine environment thanits dissolved form.</div></td></tr>
</table>Nadine Gerlachhttps://www.cazypedia.org/index.php?title=Polysaccharide_Lyase_Family_7&diff=15411&oldid=prevNadine Gerlach at 16:00, 20 June 20202020-06-20T16:00:45Z<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 16:00, 20 June 2020</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;"><div>== 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>== Mechanism ==</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>[[Image:AlyPL7 MultipleSequenceAlignment.JPG|thumb|400px|'''Figure 1. Multiple protein sequence alignment of Aly PL7 ''' as well as a secondary structure prediction with the crystallized PL7 from ''Klabsiella pneumoniae'' ([{{PDBlink}}4OZX PDB ID 4OZX]). Conserved residues in the homologues are colored in red and (putative) catalytic residues are indicated by a star. The multiple protein sequence alignment was done with Espript3.0 <cite>Robert2014</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>[[Image:AlyPL7 MultipleSequenceAlignment.JPG|thumb|400px|'''Figure 1. Multiple protein sequence alignment of Aly PL7 ''' as well as a secondary structure prediction with the crystallized PL7 from ''Klabsiella pneumoniae'' ([{{PDBlink}}4OZX PDB ID 4OZX]). Conserved residues in the homologues are colored in red and (putative) catalytic residues are indicated by a star. The multiple protein sequence alignment was done with Espript3.0 <cite>Robert2014</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>Alginate [[<del class="diffchange diffchange-inline">lyases]</del>https://www.cazypedia.org/index.php/Polysaccharide_Lyases] (Alys) from all families ([[PL5]], [[PL6]], PL7, [[PL14]], [[PL15]], [[PL17]], and [[PL18]]), catalyze the depolymerization of alginate in three steps: (I) removal of the negative charge on the carboxylate anion, (II) general base-catalyzed abstraction of the proton on the C5 and (III) β-elimination of the 4-O-glycosidic bond <cite>Gacesa1986</cite>. Most PL7s are endo-active, i.e. acting within a poly- or oligosaccharide and releasing smaller alginate fragments. Some PL7 are exo-acting cleaving a monosaccharide from the non-reducing end of the polymer <cite>Thomas2013</cite>. In both modes of action, a new non-reducing end with a 4-deoxy-L-erythro-hex-4-en pyranosyl uronate residue (Δ) is formed.</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>Alginate [[https://www.cazypedia.org/index.php/Polysaccharide_Lyases<ins class="diffchange diffchange-inline">]</ins>] (Alys) from all families ([[PL5]], [[PL6]], PL7, [[PL14]], [[PL15]], [[PL17]], and [[PL18]]), catalyze the depolymerization of alginate in three steps: (I) removal of the negative charge on the carboxylate anion, (II) general base-catalyzed abstraction of the proton on the C5 and (III) β-elimination of the 4-O-glycosidic bond <cite>Gacesa1986</cite>. Most PL7s are endo-active, i.e. acting within a poly- or oligosaccharide and releasing smaller alginate fragments. Some PL7 are exo-acting cleaving a monosaccharide from the non-reducing end of the polymer <cite>Thomas2013</cite>. In both modes of action, a new non-reducing end with a 4-deoxy-L-erythro-hex-4-en pyranosyl uronate residue (Δ) is formed.</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>Some marine PL7 alginate lyases require a calcium cation for substrate recognition and binding <cite>Thomas2013</cite>. Ca<sup>2+</sup> is weakening the ionic interactions between substrate (polyanion) and PL7 (polycation) by reducing the surface density of the alginate charge and therefore increasing the enzyme activity <cite>Favorov1979</cite>. However, there have also been reports of mono- or divalent (metal) cations not increasing or even decreasing enzymatic activity <cite>Jagtap2014 Badur2015</cite>. Therefore, it is not clear if Ca<sup>2+</sup> is required for recognition and / or binding of alginate PL7s. Nevertheless, one could speculate if cations like Ca<sup>2+</sup> are creating a more accessible form of alginate. In the presence of divalent cations, the confirmation of alginate is changed due to cross linkages with guluronate residues from opposing chains forming a so-called egg box model <cite>Grant1973</cite>. Thereby, the 3D confirmation of alginate is changed, forming hydrogels which might be an easier target for the enzyme in the marine environment thanits dissolved form.</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>Some marine PL7 alginate lyases require a calcium cation for substrate recognition and binding <cite>Thomas2013</cite>. Ca<sup>2+</sup> is weakening the ionic interactions between substrate (polyanion) and PL7 (polycation) by reducing the surface density of the alginate charge and therefore increasing the enzyme activity <cite>Favorov1979</cite>. However, there have also been reports of mono- or divalent (metal) cations not increasing or even decreasing enzymatic activity <cite>Jagtap2014 Badur2015</cite>. Therefore, it is not clear if Ca<sup>2+</sup> is required for recognition and / or binding of alginate PL7s. Nevertheless, one could speculate if cations like Ca<sup>2+</sup> are creating a more accessible form of alginate. In the presence of divalent cations, the confirmation of alginate is changed due to cross linkages with guluronate residues from opposing chains forming a so-called egg box model <cite>Grant1973</cite>. Thereby, the 3D confirmation of alginate is changed, forming hydrogels which might be an easier target for the enzyme in the marine environment thanits dissolved form.</div></td></tr>
</table>Nadine Gerlachhttps://www.cazypedia.org/index.php?title=Polysaccharide_Lyase_Family_7&diff=15410&oldid=prevNadine Gerlach at 15:57, 20 June 20202020-06-20T15:57:54Z<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 15:57, 20 June 2020</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;"><div>== 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>== Mechanism ==</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>[[Image:AlyPL7 MultipleSequenceAlignment.JPG|thumb|400px|'''Figure 1. Multiple protein sequence alignment of Aly PL7 ''' as well as a secondary structure prediction with the crystallized PL7 from ''Klabsiella pneumoniae'' ([{{PDBlink}}4OZX PDB ID 4OZX]). Conserved residues in the homologues are colored in red and (putative) catalytic residues are indicated by a star. The multiple protein sequence alignment was done with Espript3.0 <cite>Robert2014</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>[[Image:AlyPL7 MultipleSequenceAlignment.JPG|thumb|400px|'''Figure 1. Multiple protein sequence alignment of Aly PL7 ''' as well as a secondary structure prediction with the crystallized PL7 from ''Klabsiella pneumoniae'' ([{{PDBlink}}4OZX PDB ID 4OZX]). Conserved residues in the homologues are colored in red and (putative) catalytic residues are indicated by a star. The multiple protein sequence alignment was done with Espript3.0 <cite>Robert2014</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>Alginate lyases (Alys) from all families ([[PL5]], [[PL6]], PL7, [[PL14]], [[PL15]], [[PL17]], and [[PL18]]), catalyze the depolymerization of alginate in three steps: (I) removal of the negative charge on the carboxylate anion, (II) general base-catalyzed abstraction of the proton on the C5 and (III) β-elimination of the 4-O-glycosidic bond <cite>Gacesa1986</cite>. Most PL7s are endo-active, i.e. acting within a poly- or oligosaccharide and releasing smaller alginate fragments. Some PL7 are exo-acting cleaving a monosaccharide from the non-reducing end of the polymer <cite>Thomas2013</cite>. In both modes of action, a new non-reducing end with a 4-deoxy-L-erythro-hex-4-en pyranosyl uronate residue (Δ) is formed.</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>Alginate <ins class="diffchange diffchange-inline">[[</ins>lyases<ins class="diffchange diffchange-inline">]https://www.cazypedia.org/index.php/Polysaccharide_Lyases] </ins>(Alys) from all families ([[PL5]], [[PL6]], PL7, [[PL14]], [[PL15]], [[PL17]], and [[PL18]]), catalyze the depolymerization of alginate in three steps: (I) removal of the negative charge on the carboxylate anion, (II) general base-catalyzed abstraction of the proton on the C5 and (III) β-elimination of the 4-O-glycosidic bond <cite>Gacesa1986</cite>. Most PL7s are endo-active, i.e. acting within a poly- or oligosaccharide and releasing smaller alginate fragments. Some PL7 are exo-acting cleaving a monosaccharide from the non-reducing end of the polymer <cite>Thomas2013</cite>. In both modes of action, a new non-reducing end with a 4-deoxy-L-erythro-hex-4-en pyranosyl uronate residue (Δ) is formed.</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>Some marine PL7 alginate lyases require a calcium cation for substrate recognition and binding <cite>Thomas2013</cite>. Ca<sup>2+</sup> is weakening the ionic interactions between substrate (polyanion) and PL7 (polycation) by reducing the surface density of the alginate charge and therefore increasing the enzyme activity <cite>Favorov1979</cite>. However, there have also been reports of mono- or divalent (metal) cations not increasing or even decreasing enzymatic activity <cite>Jagtap2014 Badur2015</cite>. Therefore, it is not clear if Ca<sup>2+</sup> is required for recognition and / or binding of alginate PL7s. Nevertheless, one could speculate if cations like Ca<sup>2+</sup> are creating a more accessible form of alginate. In the presence of divalent cations, the confirmation of alginate is changed due to cross linkages with guluronate residues from opposing chains forming a so-called egg box model <cite>Grant1973</cite>. Thereby, the 3D confirmation of alginate is changed, forming hydrogels which might be an easier target for the enzyme in the marine environment thanits dissolved form.</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>Some marine PL7 alginate lyases require a calcium cation for substrate recognition and binding <cite>Thomas2013</cite>. Ca<sup>2+</sup> is weakening the ionic interactions between substrate (polyanion) and PL7 (polycation) by reducing the surface density of the alginate charge and therefore increasing the enzyme activity <cite>Favorov1979</cite>. However, there have also been reports of mono- or divalent (metal) cations not increasing or even decreasing enzymatic activity <cite>Jagtap2014 Badur2015</cite>. Therefore, it is not clear if Ca<sup>2+</sup> is required for recognition and / or binding of alginate PL7s. Nevertheless, one could speculate if cations like Ca<sup>2+</sup> are creating a more accessible form of alginate. In the presence of divalent cations, the confirmation of alginate is changed due to cross linkages with guluronate residues from opposing chains forming a so-called egg box model <cite>Grant1973</cite>. Thereby, the 3D confirmation of alginate is changed, forming hydrogels which might be an easier target for the enzyme in the marine environment thanits dissolved form.</div></td></tr>
</table>Nadine Gerlachhttps://www.cazypedia.org/index.php?title=Polysaccharide_Lyase_Family_7&diff=15398&oldid=prevNadine Gerlach at 12:34, 18 June 20202020-06-18T12:34:44Z<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 12:34, 18 June 2020</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l31" >Line 31:</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>Alginate lyases (Alys) from all families ([[PL5]], [[PL6]], PL7, [[PL14]], [[PL15]], [[PL17]], and [[PL18]]), catalyze the depolymerization of alginate in three steps: (I) removal of the negative charge on the carboxylate anion, (II) general base-catalyzed abstraction of the proton on the C5 and (III) β-elimination of the 4-O-glycosidic bond <cite>Gacesa1986</cite>. Most PL7s are endo-active, i.e. acting within a poly- or oligosaccharide and releasing smaller alginate fragments. Some PL7 are exo-acting cleaving a monosaccharide from the non-reducing end of the polymer <cite>Thomas2013</cite>. In both modes of action, a new non-reducing end with a 4-deoxy-L-erythro-hex-4-en pyranosyl uronate residue (Δ) is formed.</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>Alginate lyases (Alys) from all families ([[PL5]], [[PL6]], PL7, [[PL14]], [[PL15]], [[PL17]], and [[PL18]]), catalyze the depolymerization of alginate in three steps: (I) removal of the negative charge on the carboxylate anion, (II) general base-catalyzed abstraction of the proton on the C5 and (III) β-elimination of the 4-O-glycosidic bond <cite>Gacesa1986</cite>. Most PL7s are endo-active, i.e. acting within a poly- or oligosaccharide and releasing smaller alginate fragments. Some PL7 are exo-acting cleaving a monosaccharide from the non-reducing end of the polymer <cite>Thomas2013</cite>. In both modes of action, a new non-reducing end with a 4-deoxy-L-erythro-hex-4-en pyranosyl uronate residue (Δ) is formed.</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>Some marine PL7 alginate lyases require a calcium cation for substrate recognition and binding <cite>Thomas2013</cite>. Ca<sup>2+</sup> is weakening the ionic interactions between substrate (polyanion) and PL7 (polycation) by reducing the surface density of the alginate charge and therefore increasing the enzyme activity <cite>Favorov1979</cite>. However, there have also been reports of mono- or divalent (metal) cations not increasing or even decreasing enzymatic activity <cite>Jagtap2014 Badur2015</cite>. Therefore, it is not clear if Ca<sup>2+</sup> is required for recognition and / or binding of alginate <del class="diffchange diffchange-inline">t </del>PL7s. Nevertheless, one could speculate if cations like Ca<sup>2+</sup> are creating a more accessible form of alginate. In the presence of divalent cations, the confirmation of alginate is changed due to cross linkages with guluronate residues from opposing chains forming a so-called egg box model <cite>Grant1973</cite>. Thereby, the 3D confirmation of alginate is changed, forming hydrogels which might be an easier target for the enzyme in the marine environment thanits dissolved form.</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>Some marine PL7 alginate lyases require a calcium cation for substrate recognition and binding <cite>Thomas2013</cite>. Ca<sup>2+</sup> is weakening the ionic interactions between substrate (polyanion) and PL7 (polycation) by reducing the surface density of the alginate charge and therefore increasing the enzyme activity <cite>Favorov1979</cite>. However, there have also been reports of mono- or divalent (metal) cations not increasing or even decreasing enzymatic activity <cite>Jagtap2014 Badur2015</cite>. Therefore, it is not clear if Ca<sup>2+</sup> is required for recognition and / or binding of alginate PL7s. Nevertheless, one could speculate if cations like Ca<sup>2+</sup> are creating a more accessible form of alginate. In the presence of divalent cations, the confirmation of alginate is changed due to cross linkages with guluronate residues from opposing chains forming a so-called egg box model <cite>Grant1973</cite>. Thereby, the 3D confirmation of alginate is changed, forming hydrogels which might be an easier target for the enzyme in the marine environment thanits dissolved form.</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 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>== Kinetics and catalytic residues ==</div></td></tr>
</table>Nadine Gerlachhttps://www.cazypedia.org/index.php?title=Polysaccharide_Lyase_Family_7&diff=15397&oldid=prevNadine Gerlach at 12:30, 18 June 20202020-06-18T12:30:38Z<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 12:30, 18 June 2020</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l31" >Line 31:</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>Alginate lyases (Alys) from all families ([[PL5]], [[PL6]], PL7, [[PL14]], [[PL15]], [[PL17]], and [[PL18]]), catalyze the depolymerization of alginate in three steps: (I) removal of the negative charge on the carboxylate anion, (II) general base-catalyzed abstraction of the proton on the C5 and (III) β-elimination of the 4-O-glycosidic bond <cite>Gacesa1986</cite>. Most PL7s are endo-active, i.e. acting within a poly- or oligosaccharide and releasing smaller alginate fragments. Some PL7 are exo-acting cleaving a monosaccharide from the non-reducing end of the polymer <cite>Thomas2013</cite>. In both modes of action, a new non-reducing end with a 4-deoxy-L-erythro-hex-4-en pyranosyl uronate residue (Δ) is formed.</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>Alginate lyases (Alys) from all families ([[PL5]], [[PL6]], PL7, [[PL14]], [[PL15]], [[PL17]], and [[PL18]]), catalyze the depolymerization of alginate in three steps: (I) removal of the negative charge on the carboxylate anion, (II) general base-catalyzed abstraction of the proton on the C5 and (III) β-elimination of the 4-O-glycosidic bond <cite>Gacesa1986</cite>. Most PL7s are endo-active, i.e. acting within a poly- or oligosaccharide and releasing smaller alginate fragments. Some PL7 are exo-acting cleaving a monosaccharide from the non-reducing end of the polymer <cite>Thomas2013</cite>. In both modes of action, a new non-reducing end with a 4-deoxy-L-erythro-hex-4-en pyranosyl uronate residue (Δ) is formed.</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>Some marine PL7 alginate lyases require a calcium cation for substrate recognition and binding <cite>Thomas2013</cite>. Ca<sup>2+</sup> is weakening the ionic interactions between substrate (polyanion) and PL7 (polycation) by reducing the surface density of the alginate<del class="diffchange diffchange-inline">, </del>charge and therefore increasing the enzyme activity <cite>Favorov1979</cite>. However, there have also been reports <del class="diffchange diffchange-inline">where </del>mono- or divalent (metal) cations <del class="diffchange diffchange-inline">did </del>not <del class="diffchange diffchange-inline">increase </del>or even <del class="diffchange diffchange-inline">decreased </del>enzymatic activity <cite>Jagtap2014 Badur2015</cite>. Therefore, it is not clear if Ca<sup>2+</sup> is required for recognition and / or binding. <del class="diffchange diffchange-inline">However</del>, one could speculate if cations like Ca<sup>2+</sup> are creating a more accessible form of alginate. In the presence of divalent cations, the confirmation of alginate is changed due to cross linkages with guluronate residues from opposing chains forming a so-called egg box model <cite>Grant1973</cite>. Thereby, the 3D confirmation of alginate is changed, forming hydrogels which might be an easier target in the marine environment <del class="diffchange diffchange-inline">as its </del>dissolved form.</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>Some marine PL7 alginate lyases require a calcium cation for substrate recognition and binding <cite>Thomas2013</cite>. Ca<sup>2+</sup> is weakening the ionic interactions between substrate (polyanion) and PL7 (polycation) by reducing the surface density of the alginate charge and therefore increasing the enzyme activity <cite>Favorov1979</cite>. However, there have also been reports <ins class="diffchange diffchange-inline">of </ins>mono- or divalent (metal) cations not <ins class="diffchange diffchange-inline">increasing </ins>or even <ins class="diffchange diffchange-inline">decreasing </ins>enzymatic activity <cite>Jagtap2014 Badur2015</cite>. Therefore, it is not clear if Ca<sup>2+</sup> is required for recognition and / or binding <ins class="diffchange diffchange-inline">of alginate t PL7s</ins>. <ins class="diffchange diffchange-inline">Nevertheless</ins>, one could speculate if cations like Ca<sup>2+</sup> are creating a more accessible form of alginate. In the presence of divalent cations, the confirmation of alginate is changed due to cross linkages with guluronate residues from opposing chains forming a so-called egg box model <cite>Grant1973</cite>. Thereby, the 3D confirmation of alginate is changed, forming hydrogels which might be an easier target <ins class="diffchange diffchange-inline">for the enzyme </ins>in the marine environment <ins class="diffchange diffchange-inline">thanits </ins>dissolved form.</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 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>== Kinetics and 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>Several structural and biochemical analyses of wild type and mutated PL7s revealed five residues forming the active site: arginine (R), glutamine (Q), histidine (H), tyrosine (Y) <cite>Preston2000 Yamasaki200 Yamasaki2005</cite>, which are present in three highly conserved regions: R*ELR*ML, VIIGQ(I/V)H, YFKAG*Y*Q respectively (Figure 1) <cite>Wong2000</cite>. It has been proposed that in PL7 ALY-1 from ''Corynebacterium'' sp. Q117+Y195 interact near the reaction site of alginate to maintain proper orientation of the substrate, R72 interacts with alginate <del class="diffchange diffchange-inline">due </del>to <del class="diffchange diffchange-inline">the formation of salt bridges with </del>the carboxyl groups at <del class="diffchange diffchange-inline">the </del>C5 and H119 <del class="diffchange diffchange-inline">acts as </del>a <del class="diffchange diffchange-inline">base to deprotonate </del><cite>Osawa2015</cite>. However, there can also be additional charged residues at the active site, which promote substrate recognition and binding <cite>Thomas2013</cite>. Such residues can be found in the N-terminal R*ELREML and VIIGQIH regions. Both highly conserved regions are mainly characterized by hydrophobic amino acids (especially aromatic amino acids) such as leucine, tryptophan and methionine as well as residues with planar polar side chains (especially amino acids with charged side chains) such as arginine, glutamic acid, glutamine (Figure 2). These residues have been suggested to be substrate-binding molecules <cite>Wong2000</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>Several structural and biochemical analyses of wild type and mutated PL7s revealed five residues forming the active site: arginine (R), glutamine (Q), histidine (H), <ins class="diffchange diffchange-inline">2x </ins>tyrosine (Y) <cite>Preston2000 Yamasaki200 Yamasaki2005</cite>, which are present in three highly conserved regions: R*ELR*ML, VIIGQ(I/V)H, YFKAG*Y*Q respectively (Figure 1) <cite>Wong2000</cite>. It has been proposed that in PL7 ALY-1 from ''Corynebacterium'' sp. Q117+Y195 interact near the reaction site of alginate to maintain proper orientation of the substrate, R72 <ins class="diffchange diffchange-inline"> </ins>interacts with alginate <ins class="diffchange diffchange-inline">as a base </ins>to <ins class="diffchange diffchange-inline">deprotonate </ins>the carboxyl groups at C5 and H119 <ins class="diffchange diffchange-inline">forming </ins>a <ins class="diffchange diffchange-inline">salt bridge between substrate and enzyme</ins><cite>Osawa2015</cite>. However, there can also be additional charged residues at the active site, which promote substrate recognition and binding <cite>Thomas2013</cite>. Such residues can be found in the N-terminal R*ELREML and VIIGQIH regions. Both highly conserved regions are mainly characterized by hydrophobic amino acids (especially aromatic amino acids) such as leucine, tryptophan and methionine as well as residues with planar polar side chains (especially amino acids with charged side chains) such as arginine, glutamic acid, glutamine (Figure 2). These residues have been suggested to be substrate-binding molecules <cite>Wong2000</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>== 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="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>[[Image:PL7SF_Thomasetal2013.JPG|thumb|400px|'''Figure 2. Subfamilies of PL7s''' <cite>Thomas2013</cite>. Unrooted tree with bootstrap values after maximum likelihood analysis. Number refer to Uniprot accession numbers. Red dots indicate enzymes from ''Z. galactanivorans''. Pink triangles indicate enzymes characterized biochemically. Blue squares indicate that the structure of the protein has been solved.]]</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>[[Image:PL7SF_Thomasetal2013.JPG|thumb|400px|'''Figure 2. Subfamilies of PL7s''' <cite>Thomas2013</cite>. Unrooted tree with bootstrap values after maximum likelihood analysis. Number refer to Uniprot accession numbers. Red dots indicate enzymes from ''Z. galactanivorans''. Pink triangles indicate enzymes characterized biochemically. Blue squares indicate that the structure of the protein has been solved.]]</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>Polysaccharide lyase family 7 (PL7) contains five subfamilies (SF) based on their sequence similarities <cite>Lombard2010</cite>, plus a so far uncharacterized sixth subfamily, which consist only of marine representatives of the Flavobacteriaceae (Figure 2) <cite>Thomas2013</cite>. The substrate specificity depends on the source of alginate, i.e. derived from brown seaweed or mucoid bacteria ''Pseudomonas'' spp. and ''Azotobacter vinelandii'', as well as geographical and seasonal parameters. Alginate is a heteropolysaccharide, consisting of β-D-mannuronate (M) and α-L-guluronate (G). These monosaccharides can occur in homogenous and heterogenous blocks. In addition, bacterial alginate is often acetylated at the C2 and / or C3 of mannuronate, thereby shielding the substrate from degradation. Hence, PL7s can be mannuronate ([{{EClink}}4.2.2.3 EC 4.2.2.3]), guluronate ([{{EClink}}4.2.2.11 EC 4.2.2.11]) or mixed link (EC 4.2.2.-) specific lyases. Despite the preference for M- or G-enriched blocks, most PL7 also have a low to moderate activity <del class="diffchange diffchange-inline">for </del>the other building block <cite>Thomas2013 Badur2015 Sim2017</cite>. PolyG specific PL7 have been found in the SF3 and SF5 <cite>Thomas2013</cite> with QIH in the second highly conserved region, while polyM specific PL7s are characterized by QVH <cite>Zhu2015 Deng2014</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>Polysaccharide lyase family 7 (PL7) contains five subfamilies (SF) based on their sequence similarities <cite>Lombard2010</cite>, plus a so far uncharacterized sixth subfamily, which consist only of marine representatives of the Flavobacteriaceae (Figure 2) <cite>Thomas2013</cite>. The substrate specificity depends on the source of alginate, i.e. derived from brown seaweed or mucoid bacteria ''Pseudomonas'' spp. and ''Azotobacter vinelandii'', as well as geographical and seasonal parameters. Alginate is a heteropolysaccharide, consisting of β-D-mannuronate (M) and α-L-guluronate (G). These monosaccharides can occur in homogenous and heterogenous blocks. In addition, bacterial alginate is often acetylated at the C2 and / or C3 of mannuronate, thereby shielding the substrate from degradation. Hence, PL7s can be mannuronate ([{{EClink}}4.2.2.3 EC 4.2.2.3]), guluronate ([{{EClink}}4.2.2.11 EC 4.2.2.11]) or mixed link (EC 4.2.2.-) specific lyases. Despite the preference for M- or G-enriched blocks, most PL7 also have a low to moderate activity <ins class="diffchange diffchange-inline">at </ins>the other building block <cite>Thomas2013 Badur2015 Sim2017</cite>. PolyG specific PL7 have been found in the SF3 and SF5 <cite>Thomas2013</cite> with QIH in the second highly conserved region, while polyM specific PL7s are characterized by QVH <cite>Zhu2015 Deng2014</cite>.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Three-dimensional structures ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Three-dimensional structures ==</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>[[Image:EndovsexoPL7_Thomas_et_al_2013.jpg|thumb|400px|'''Figure 3. 3D Structure of endo- and exo-active PL7s''' <cite>Thomas2013</cite>. (A,B) endo AlyA1 and (C, D) exo AlyA5 from ''Zobellia galaactinovorans'' DsijT shown as cartoon (A,C) and surface structure (B,D) with superimposed tetrasaccharide from [{{PDBlink}}2ZAA PDB ID 2ZAA]. The image was conducted in PyMOL <cite>DeLano2002</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>[[Image:EndovsexoPL7_Thomas_et_al_2013.jpg|thumb|400px|'''Figure 3. 3D Structure of endo- and exo-active PL7s''' <cite>Thomas2013</cite>. (A,B) endo AlyA1 and (C, D) exo AlyA5 from ''Zobellia galaactinovorans'' DsijT shown as cartoon (A,C) and surface structure (B,D) with superimposed tetrasaccharide from [{{PDBlink}}2ZAA PDB ID 2ZAA]. The image was conducted in PyMOL <cite>DeLano2002</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>PL7 displays a jelly roll fold, which is also found in [[PL14]] as well as in glycoside hydrolases of family [[GH16]]. ''Zobellia galactanivorans'' DsijT possess, among others, two <del class="diffchange diffchange-inline">PL7 </del>with different modes of activity <cite>Thomas2013</cite>. AlyA1 is an endo-acting PL7 belonging to SF3 with a wide open cleft harboring the active site (Figure 3A, B), whereas AlyA5 belongs to SF5 and is exo-active <del class="diffchange diffchange-inline">which </del>active site <del class="diffchange diffchange-inline">is </del>closed by three loops forming a small pocket (Figure 3C, D). The highly conserved 9-amino-acid-block YFKAGVY*Q (where * is a variable residue) at the C-terminus of PL7s (Figure 2) has also been found for an extracellular pectate lyase (PL1, PDB: 1AIR) in ''E. chrysanthemi''. Alginate and pectate/pectin lyases share the β-elimination mechanism, the recognition of substrates of a similar structure, Ca<sup>2+</sup>-binding site and primary sequence similarity, indicating that they probably possess a similar core structural fold probably important to maintain a stable 3D-confirmation <cite>Wong2000</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>PL7 displays a jelly roll fold, which is also found in [[PL14]] as well as in glycoside hydrolases of family [[GH16]]. ''Zobellia galactanivorans'' DsijT possess, among others, two <ins class="diffchange diffchange-inline">PL7s </ins>with different modes of activity <cite>Thomas2013</cite>. AlyA1 is an endo-acting PL7 belonging to SF3 with a wide open cleft harboring the active site (Figure 3A, B), whereas AlyA5 belongs to SF5 and is exo-active <ins class="diffchange diffchange-inline">with an </ins>active site closed by three loops forming a small pocket (Figure 3C, D). The highly conserved 9-amino-acid-block YFKAGVY*Q (where * is a variable residue) at the C-terminus of PL7s (Figure 2) has also been found for an extracellular pectate lyase (PL1, PDB: 1AIR) in ''E. chrysanthemi''. Alginate and pectate/pectin lyases share the β-elimination mechanism, the recognition of substrates of a similar structure, <ins class="diffchange diffchange-inline">a </ins>Ca<sup>2+</sup>-binding site and primary sequence similarity, indicating that they probably possess a similar core structural fold probably important to maintain a stable 3D-confirmation <cite>Wong2000</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>Several alginate lyases have been reported to be multimodular enzymes with putative non-catalytic, [[Carbohydrate_Binding_Module_Families|carbohydrate-binding modules (CBMs)]]. The first biochemically characterized CBM of an endo PL7 was <del class="diffchange diffchange-inline">a </del>N-terminal [[CBM13]] from ''Agarivorans'' sp. L11, which increased <del class="diffchange diffchange-inline">its </del>substrate binding and therefore catalytic efficiency, influenced substrate specificity, the product profile and thermo stability <cite>Li2015</cite>. Opposite observations regarding catalytic efficiency and substrate specificity were made for an endo PL7 from ''Vibrio splendidus'' OU02 DNA with an N-terminal [[CBM32]] linked by a unique alpha-helix linker. The CBM and linker were proposed to serve as a "pivot point" somehow just pushing the product profile towards trisaccharides <cite>Lyu2018</cite>. The PL7 from ''Persicobacter'' sp. CCB-QB2 consists of three domains - <del class="diffchange diffchange-inline">a </del>N-terminal [[CBM16]] with unknown function, a [[CBM32]] and the C-terminal PL7 <cite>Sim2017</cite>. Overall the role of [[CBM]]s from different families as part of PL7s still remains unclear. Another common structural feature found in PLs <del class="diffchange diffchange-inline">are </del>flexible loops facing above the active site <cite>Xu2018</cite>, which have been demonstrated to influence substrate recognition, binding <cite>Thomas2013 Ogura2008</cite> and potentially specificity <cite>Qin2018</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>Several alginate lyases have been reported to be multimodular enzymes with putative non-catalytic, [[Carbohydrate_Binding_Module_Families|carbohydrate-binding modules (CBMs)]]. The first biochemically characterized CBM of an endo PL7 was <ins class="diffchange diffchange-inline">an </ins>N-terminal [[CBM13]] from ''Agarivorans'' sp. L11, which increased <ins class="diffchange diffchange-inline">the </ins>substrate binding and therefore catalytic efficiency, influenced substrate specificity, the product profile and thermo stability <ins class="diffchange diffchange-inline">of the lyase </ins><cite>Li2015</cite>. Opposite observations regarding catalytic efficiency and substrate specificity were made for an endo PL7 from ''Vibrio splendidus'' OU02 DNA with an N-terminal [[CBM32]] linked by a unique alpha-helix linker. The CBM and linker were proposed to serve as a "pivot point" somehow just pushing the product profile towards trisaccharides <cite>Lyu2018</cite>. The PL7 from ''Persicobacter'' sp. CCB-QB2 consists of three domains - <ins class="diffchange diffchange-inline">an </ins>N-terminal [[CBM16]] with unknown function, a [[CBM32]] and the C-terminal PL7 <cite>Sim2017</cite>. Overall the role of [[CBM]]s from different families as part of PL7s still remains unclear. Another common structural feature found in PLs <ins class="diffchange diffchange-inline">is a number of </ins>flexible loops facing above the active site <cite>Xu2018</cite>, which have been demonstrated to influence substrate recognition, binding <cite>Thomas2013 Ogura2008</cite> and potentially specificity <cite>Qin2018</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>== Gene transfer of Alys among different habitats ==</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>== Gene transfer of Alys among different habitats ==</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>Alginate degrading organisms often possess specified gene clusters for glycan utilization which contain, among other proteins such as transporters, several endo- and exo-acting Alys of different families. These gene clusters are called polysaccharide utilization loci (PULs) for Bacteriodetes <cite>Bjursell2016</cite> or alginolytic operons in case a SusCD pair transporter is missing or replaced by a different transporter system. It has been shown that these gene clusters can be transferred horizontally from one organism to another and thereby even cross different environmental habitats <cite>Hehemann2010 Mathieu2018</cite>. The first alginate utilization system (AUS) was found in ''Zobellia galactinovorans'' which contains two clusters harboring five out of seven Alys (3x PL7). Those operons originated from an ancestral marine Flavobacterium and were independently transferred to marine Proteobacteria and Japanese gut Bacteriodetes by lateral gene transfer (LGT) <cite>Thomas2012</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>Alginate degrading organisms often possess specified gene clusters for glycan utilization which contain, among other proteins such as transporters, several endo- and exo-acting Alys of different families. These gene clusters are called polysaccharide utilization loci (PULs) for Bacteriodetes <cite>Bjursell2016</cite> or alginolytic operons in case a SusCD pair transporter is missing or replaced by a different transporter system. It has been shown that these gene clusters can be transferred horizontally from one organism to another and thereby even cross different environmental habitats <cite>Hehemann2010 Mathieu2018</cite>. The first alginate utilization system (AUS) was found in ''Zobellia galactinovorans'' which contains two clusters harboring five out of seven Alys (3x PL7). Those operons originated from an ancestral marine Flavobacterium and were independently transferred to marine Proteobacteria and Japanese gut Bacteriodetes by lateral gene transfer (LGT) <cite>Thomas2012</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="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>A more detailed studied on horizontal gene transfer of PL7 between marine, ecophysiological different Vibrionaceae isolates revealed rapid adaptation of closely related but speciated bacterial populations, resulting <del class="diffchange diffchange-inline">into </del>a fine scale of resource partitioning. The exchange of PL7 between marine microbes drove the evolution of polysaccharide degrading pathways, which might have led to three ecotypes – the pioneers, which degrade the polymer into oligomers, the <del class="diffchange diffchange-inline">harvester </del>(intermediate of the other two types) and the <del class="diffchange diffchange-inline">scavenger</del>, which can only utilize very small <del class="diffchange diffchange-inline">oligos </del>created by the pioneers <cite>Hehemann2016</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>A more detailed studied on horizontal gene transfer of PL7 between marine, ecophysiological different Vibrionaceae isolates revealed rapid adaptation of closely related but speciated bacterial populations, resulting <ins class="diffchange diffchange-inline">in </ins>a fine scale of resource partitioning. The exchange of PL7 between marine microbes drove the evolution of polysaccharide degrading pathways, which might have led to three ecotypes – the pioneers, which degrade the polymer into oligomers, the <ins class="diffchange diffchange-inline">harvesters </ins>(intermediate of the other two types) and the <ins class="diffchange diffchange-inline">scavengers</ins>, which can only utilize very small <ins class="diffchange diffchange-inline">oligosaccharides </ins>created by the pioneers <cite>Hehemann2016</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>Nadine Gerlach