https://proteopedia.org/index.php?action=history&feed=atom&title=Choline_OxidaseCholine Oxidase - Revision history2026-09-11T13:06:21ZRevision history for this page on the wikiMediaWiki 1.43.8https://proteopedia.org/index.php?title=Choline_Oxidase&diff=3001105&oldid=prevAlexander Berchansky at 10:54, 13 February 20192019-02-13T10:54:49Z<p></p>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div><StructureSection load='2JBV' size='450' side='right' scene='37/377142/Cv/8' caption='Choline Oxidase complex with pteridin derivative and DMSO [[2jbv]]'></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><StructureSection load='2JBV' size='450' side='right' scene='37/377142/Cv/8' caption='Choline Oxidase complex with pteridin derivative and DMSO [[2jbv]]'></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>== Abstract ==</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>== Abstract ==</div></td></tr>
<tr><td class="diff-marker" data-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>'''Choline oxidase''' is the enzyme that catalyzes the reaction between choline and betaine glycine. Betaine glycine is an osmoprotectant and instrumental in helping plants and bacteria survive dry conditions. Studying the choline oxidase may help in the development of controlling populations of beneficial plants or pathogenic bacteria. The data was analyzed using the BLAST and Rasmol programs. The structure of choline oxidase from Arthrobacter globiformis (bacteria) was compared with the structure of the complimentary protein in Mus musculus (mice), carnitine acetyltransferase (Altschul et al., 2005). There are seven amino acids evolutionarily preserved within the vicinity of the flavin group (between amino acids 460 to 483 of each subunit). Of these seven, three are within 9 Å of the flavin group while the other four are farther away. These three are <scene name='37/377142/Cv/<del style="font-weight: bold; text-decoration: none;">9</del>'>threonine 463, valine 464, and histidine 466</scene> (UNK are unknown atoms or ion). They are colored olive and are connected with the ligand via white monitor lines. Evolutionary preservation of the Thr463, His 466, and Val 464 may signify an importance in aiding the function of the flavin group as it relates to the activity of the enzyme. Previous studies indicate that His466 is indeed important in the function of choline oxidase (Quaye, Lountos, Fan, Orville, & Gadda, 2008).</div></td><td class="diff-marker" data-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>'''Choline oxidase''' is the enzyme that catalyzes the reaction between choline and betaine glycine. Betaine glycine is an osmoprotectant and instrumental in helping plants and bacteria survive dry conditions. Studying the choline oxidase may help in the development of controlling populations of beneficial plants or pathogenic bacteria. The data was analyzed using the BLAST and Rasmol programs. The structure of choline oxidase from Arthrobacter globiformis (bacteria) was compared with the structure of the complimentary protein in Mus musculus (mice), carnitine acetyltransferase (Altschul et al., 2005). There are seven amino acids evolutionarily preserved within the vicinity of the flavin group (between amino acids 460 to 483 of each subunit). Of these seven, three are within 9 Å of the flavin group while the other four are farther away. These three are <scene name='37/377142/Cv/<ins style="font-weight: bold; text-decoration: none;">11</ins>'>threonine 463, valine 464, and histidine 466</scene> (UNK are unknown atoms or ion). They are colored olive and are connected with the ligand via white monitor lines. Evolutionary preservation of the Thr463, His 466, and Val 464 may signify an importance in aiding the function of the flavin group as it relates to the activity of the enzyme. Previous studies indicate that His466 is indeed important in the function of choline oxidase (Quaye, Lountos, Fan, Orville, & Gadda, 2008).</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;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker" data-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><scene name='37/377142/Cv/<del style="font-weight: bold; text-decoration: none;">10</del>'>Whole binding site</scene>.</div></td><td class="diff-marker" data-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><scene name='37/377142/Cv/<ins style="font-weight: bold; text-decoration: none;">12</ins>'>Whole binding site</scene>.</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>== Introduction ==</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>== Introduction ==</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>Choline oxidase is an enzyme which catalyses the chemical reaction choline and 2 molecules of oxygen gas into betaine glycine and two molecules of hydrogen peroxide. Recombinant choline oxidase is a convenient enzyme to introduce into transgenic plants for the synthesis of betaine glycine (Sakamoto and Murata, 2001). Plants adapt to osmotic fluctuations and temperature differences through forming an osmoprotective layer of organic compounds. Betaine Aldehyde, the intermediate of the reaction, is one such osmolyte (Rodwazowski, 1991). Choline oxidase is proposed to use a flavin prosthetic group to assist in the fore-mentioned chemical reaction. </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>Choline oxidase is an enzyme which catalyses the chemical reaction choline and 2 molecules of oxygen gas into betaine glycine and two molecules of hydrogen peroxide. Recombinant choline oxidase is a convenient enzyme to introduce into transgenic plants for the synthesis of betaine glycine (Sakamoto and Murata, 2001). Plants adapt to osmotic fluctuations and temperature differences through forming an osmoprotective layer of organic compounds. Betaine Aldehyde, the intermediate of the reaction, is one such osmolyte (Rodwazowski, 1991). Choline oxidase is proposed to use a flavin prosthetic group to assist in the fore-mentioned chemical reaction. </div></td></tr>
</table>Alexander Berchanskyhttps://proteopedia.org/index.php?title=Choline_Oxidase&diff=2734771&oldid=prevMichal Harel at 08:19, 3 April 20172017-04-03T08:19:15Z<p></p>
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 08:19, 3 April 2017</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>Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}</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>Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}</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;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker" data-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>[[2jbv<del style="font-weight: bold; text-decoration: none;">]], [[5abc</del>]] – AgChOx – ''Arthrobacter globiformis''<br /></div></td><td class="diff-marker" data-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>[[2jbv]] – AgChOx – ''Arthrobacter globiformis''<br /></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>[[3nne]], [[3ljp]] – AgChOx (mutant)<br /></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>[[3nne]], [[3ljp]] – AgChOx (mutant)<br /></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>[[4mjw]] – AgChOx + trimethylglycine<br /></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>[[4mjw]] – AgChOx + trimethylglycine<br /></div></td></tr>
</table>Michal Harelhttps://proteopedia.org/index.php?title=Choline_Oxidase&diff=2734770&oldid=prevMichal Harel at 08:18, 3 April 20172017-04-03T08:18:17Z<p></p>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker" data-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>[[2jbv]] – AgChOx – ''Arthrobacter globiformis''<br /></div></td><td class="diff-marker" data-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>[[2jbv<ins style="font-weight: bold; text-decoration: none;">]], [[5abc</ins>]] – AgChOx – ''Arthrobacter globiformis''<br /></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>[[3nne]], [[3ljp]] – AgChOx (mutant)<br /></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>[[3nne]], [[3ljp]] – AgChOx (mutant)<br /></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>[[4mjw]] – AgChOx + trimethylglycine<br /></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>[[4mjw]] – AgChOx + trimethylglycine<br /></div></td></tr>
</table>Michal Harelhttps://proteopedia.org/index.php?title=Choline_Oxidase&diff=2520562&oldid=prevAlexander Berchansky at 14:49, 19 January 20162016-01-19T14:49:55Z<p></p>
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 14:49, 19 January 2016</td>
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<tr><td class="diff-marker" data-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><StructureSection load='2JBV' size='<del style="font-weight: bold; text-decoration: none;">350</del>' side='right' scene='37/377142/Cv/<del style="font-weight: bold; text-decoration: none;">1</del>' caption='Choline Oxidase complex with pteridin derivative and DMSO [[2jbv]]'></div></td><td class="diff-marker" data-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><StructureSection load='2JBV' size='<ins style="font-weight: bold; text-decoration: none;">450</ins>' side='right' scene='37/377142/Cv/<ins style="font-weight: bold; text-decoration: none;">8</ins>' caption='Choline Oxidase complex with pteridin derivative and DMSO [[2jbv]]'></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>== Abstract ==</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>== Abstract ==</div></td></tr>
<tr><td class="diff-marker" data-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>'''Choline oxidase''' is the enzyme that catalyzes the reaction between choline and betaine glycine. Betaine glycine is an osmoprotectant and instrumental in helping plants and bacteria survive dry conditions. Studying the choline oxidase may help in the development of controlling populations of beneficial plants or pathogenic bacteria. The data was analyzed using the BLAST and Rasmol programs. The structure of choline oxidase from Arthrobacter globiformis (bacteria) was compared with the structure of the complimentary protein in Mus musculus (mice), carnitine acetyltransferase (Altschul et al., 2005). There are seven amino acids evolutionarily preserved within the vicinity of the flavin group (between amino acids 460 to 483 of each subunit). Of these seven, three are within 9 Å of the flavin group while the other four are farther away. These three are threonine 463, valine 464, and histidine 466. They are colored <del style="font-weight: bold; text-decoration: none;">blue </del>and are connected with the ligand via white monitor lines<del style="font-weight: bold; text-decoration: none;">. The other four conserved residues are colored cyan, but are too far to really interact with the flavin group (colored cpk). Beta sheets are colored yellow to showcase the secondary structure of the entire subunit</del>. Evolutionary preservation of the Thr463, </div></td><td class="diff-marker" data-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>'''Choline oxidase''' is the enzyme that catalyzes the reaction between choline and betaine glycine. Betaine glycine is an osmoprotectant and instrumental in helping plants and bacteria survive dry conditions. Studying the choline oxidase may help in the development of controlling populations of beneficial plants or pathogenic bacteria. The data was analyzed using the BLAST and Rasmol programs. The structure of choline oxidase from Arthrobacter globiformis (bacteria) was compared with the structure of the complimentary protein in Mus musculus (mice), carnitine acetyltransferase (Altschul et al., 2005). There are seven amino acids evolutionarily preserved within the vicinity of the flavin group (between amino acids 460 to 483 of each subunit). Of these seven, three are within 9 Å of the flavin group while the other four are farther away. These three are <ins style="font-weight: bold; text-decoration: none;"><scene name='37/377142/Cv/9'></ins>threonine 463, valine 464, and histidine 466<ins style="font-weight: bold; text-decoration: none;"></scene> (UNK are unknown atoms or ion)</ins>. They are colored <ins style="font-weight: bold; text-decoration: none;">olive </ins>and are connected with the ligand via white monitor lines. Evolutionary preservation of the Thr463, His 466, and Val 464 may signify an importance in aiding the function of the flavin group as it relates to the activity of the enzyme. Previous studies indicate that His466 is indeed important in the function of choline oxidase (Quaye, Lountos, Fan, Orville, & Gadda, 2008).</div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div><del style="font-weight: bold; text-decoration: none;"><scene name='User:Mohammad_Rao/Sandbox1_Choline_Oxidase/Choline_oxidase-_2_residues/1'></del>His 466, and Val 464<del style="font-weight: bold; text-decoration: none;"></scene> </del>may signify an importance in aiding the function of the flavin group as it relates to the activity of the enzyme. Previous studies indicate that His466 is indeed important in the function of choline oxidase (Quaye, Lountos, Fan, Orville, & Gadda, 2008).</div></td><td colspan="2" class="diff-side-added"></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;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker" data-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><scene name='37/377142/Cv/<del style="font-weight: bold; text-decoration: none;">7</del>'><del style="font-weight: bold; text-decoration: none;">Binding </del>site</scene>.</div></td><td class="diff-marker" data-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><scene name='37/377142/Cv/<ins style="font-weight: bold; text-decoration: none;">10</ins>'><ins style="font-weight: bold; text-decoration: none;">Whole binding </ins>site</scene>.</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>== Introduction ==</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>== Introduction ==</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>Choline oxidase is an enzyme which catalyses the chemical reaction choline and 2 molecules of oxygen gas into betaine glycine and two molecules of hydrogen peroxide. Recombinant choline oxidase is a convenient enzyme to introduce into transgenic plants for the synthesis of betaine glycine (Sakamoto and Murata, 2001). Plants adapt to osmotic fluctuations and temperature differences through forming an osmoprotective layer of organic compounds. Betaine Aldehyde, the intermediate of the reaction, is one such osmolyte (Rodwazowski, 1991). Choline oxidase is proposed to use a flavin prosthetic group to assist in the fore-mentioned chemical reaction. </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>Choline oxidase is an enzyme which catalyses the chemical reaction choline and 2 molecules of oxygen gas into betaine glycine and two molecules of hydrogen peroxide. Recombinant choline oxidase is a convenient enzyme to introduce into transgenic plants for the synthesis of betaine glycine (Sakamoto and Murata, 2001). Plants adapt to osmotic fluctuations and temperature differences through forming an osmoprotective layer of organic compounds. Betaine Aldehyde, the intermediate of the reaction, is one such osmolyte (Rodwazowski, 1991). Choline oxidase is proposed to use a flavin prosthetic group to assist in the fore-mentioned chemical reaction. </div></td></tr>
</table>Alexander Berchanskyhttps://proteopedia.org/index.php?title=Choline_Oxidase&diff=2520557&oldid=prevAlexander Berchansky at 14:30, 19 January 20162016-01-19T14:30:27Z<p></p>
<table style="background-color: #fff; color: #202122;" data-mw="interface">
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 14:30, 19 January 2016</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l4">Line 4:</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><scene name='User:Mohammad_Rao/Sandbox1_Choline_Oxidase/Choline_oxidase-_2_residues/1'>His 466, and Val 464</scene> may signify an importance in aiding the function of the flavin group as it relates to the activity of the enzyme. Previous studies indicate that His466 is indeed important in the function of choline oxidase (Quaye, Lountos, Fan, Orville, & Gadda, 2008).</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><scene name='User:Mohammad_Rao/Sandbox1_Choline_Oxidase/Choline_oxidase-_2_residues/1'>His 466, and Val 464</scene> may signify an importance in aiding the function of the flavin group as it relates to the activity of the enzyme. Previous studies indicate that His466 is indeed important in the function of choline oxidase (Quaye, Lountos, Fan, Orville, & Gadda, 2008).</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;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td colspan="2" class="diff-side-deleted"></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;"><scene name='37/377142/Cv/7'>Binding site</scene>.</ins></div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Introduction ==</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>== Introduction ==</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>Choline oxidase is an enzyme which catalyses the chemical reaction choline and 2 molecules of oxygen gas into betaine glycine and two molecules of hydrogen peroxide. Recombinant choline oxidase is a convenient enzyme to introduce into transgenic plants for the synthesis of betaine glycine (Sakamoto and Murata, 2001). Plants adapt to osmotic fluctuations and temperature differences through forming an osmoprotective layer of organic compounds. Betaine Aldehyde, the intermediate of the reaction, is one such osmolyte (Rodwazowski, 1991). Choline oxidase is proposed to use a flavin prosthetic group to assist in the fore-mentioned chemical reaction. </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>Choline oxidase is an enzyme which catalyses the chemical reaction choline and 2 molecules of oxygen gas into betaine glycine and two molecules of hydrogen peroxide. Recombinant choline oxidase is a convenient enzyme to introduce into transgenic plants for the synthesis of betaine glycine (Sakamoto and Murata, 2001). Plants adapt to osmotic fluctuations and temperature differences through forming an osmoprotective layer of organic compounds. Betaine Aldehyde, the intermediate of the reaction, is one such osmolyte (Rodwazowski, 1991). Choline oxidase is proposed to use a flavin prosthetic group to assist in the fore-mentioned chemical reaction. </div></td></tr>
</table>Alexander Berchanskyhttps://proteopedia.org/index.php?title=Choline_Oxidase&diff=2520556&oldid=prevAlexander Berchansky at 10:42, 19 January 20162016-01-19T10:42:30Z<p></p>
<table style="background-color: #fff; color: #202122;" data-mw="interface">
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<col class="diff-content" />
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">← Older revision</td>
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 10:42, 19 January 2016</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l1">Line 1:</td>
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<tr><td class="diff-marker" data-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><StructureSection load='2JBV' size='350' side='right' scene='' caption='Choline Oxidase <del style="font-weight: bold; text-decoration: none;">dimer </del>complex with pteridin derivative and DMSO [[2jbv]]'></div></td><td class="diff-marker" data-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><StructureSection load='2JBV' size='350' side='right' scene='<ins style="font-weight: bold; text-decoration: none;">37/377142/Cv/1</ins>' caption='Choline Oxidase complex with pteridin derivative and DMSO [[2jbv]]'></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>== Abstract ==</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>== Abstract ==</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>'''Choline oxidase''' is the enzyme that catalyzes the reaction between choline and betaine glycine. Betaine glycine is an osmoprotectant and instrumental in helping plants and bacteria survive dry conditions. Studying the choline oxidase may help in the development of controlling populations of beneficial plants or pathogenic bacteria. The data was analyzed using the BLAST and Rasmol programs. The structure of choline oxidase from Arthrobacter globiformis (bacteria) was compared with the structure of the complimentary protein in Mus musculus (mice), carnitine acetyltransferase (Altschul et al., 2005). There are seven amino acids evolutionarily preserved within the vicinity of the flavin group (between amino acids 460 to 483 of each subunit). Of these seven, three are within 9 Å of the flavin group while the other four are farther away. These three are threonine 463, valine 464, and histidine 466. They are colored blue and are connected with the ligand via white monitor lines. The other four conserved residues are colored cyan, but are too far to really interact with the flavin group (colored cpk). Beta sheets are colored yellow to showcase the secondary structure of the entire subunit. Evolutionary preservation of the Thr463, </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>'''Choline oxidase''' is the enzyme that catalyzes the reaction between choline and betaine glycine. Betaine glycine is an osmoprotectant and instrumental in helping plants and bacteria survive dry conditions. Studying the choline oxidase may help in the development of controlling populations of beneficial plants or pathogenic bacteria. The data was analyzed using the BLAST and Rasmol programs. The structure of choline oxidase from Arthrobacter globiformis (bacteria) was compared with the structure of the complimentary protein in Mus musculus (mice), carnitine acetyltransferase (Altschul et al., 2005). There are seven amino acids evolutionarily preserved within the vicinity of the flavin group (between amino acids 460 to 483 of each subunit). Of these seven, three are within 9 Å of the flavin group while the other four are farther away. These three are threonine 463, valine 464, and histidine 466. They are colored blue and are connected with the ligand via white monitor lines. The other four conserved residues are colored cyan, but are too far to really interact with the flavin group (colored cpk). Beta sheets are colored yellow to showcase the secondary structure of the entire subunit. Evolutionary preservation of the Thr463, </div></td></tr>
</table>Alexander Berchanskyhttps://proteopedia.org/index.php?title=Choline_Oxidase&diff=2520555&oldid=prevAlexander Berchansky at 10:35, 19 January 20162016-01-19T10:35:47Z<p></p>
<table style="background-color: #fff; color: #202122;" data-mw="interface">
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">← Older revision</td>
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 10:35, 19 January 2016</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l1">Line 1:</td>
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<tr><td colspan="2" class="diff-side-deleted"></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;"><StructureSection load='2JBV' size='350' side='right' scene='' caption='Choline Oxidase dimer complex with pteridin derivative and DMSO [[2jbv]]'></ins></div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Abstract ==</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>== Abstract ==</div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div><del style="font-weight: bold; text-decoration: none;"><applet load='2JBV' size='350' frame='true' align='right' caption='Choline Oxidase dimer complex with pteridin derivative and DMSO [[2jbv]]' /></del></div></td><td colspan="2" class="diff-side-added"></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>'''Choline oxidase''' is the enzyme that catalyzes the reaction between choline and betaine glycine. Betaine glycine is an osmoprotectant and instrumental in helping plants and bacteria survive dry conditions. Studying the choline oxidase may help in the development of controlling populations of beneficial plants or pathogenic bacteria. The data was analyzed using the BLAST and Rasmol programs. The structure of choline oxidase from Arthrobacter globiformis (bacteria) was compared with the structure of the complimentary protein in Mus musculus (mice), carnitine acetyltransferase (Altschul et al., 2005). There are seven amino acids evolutionarily preserved within the vicinity of the flavin group (between amino acids 460 to 483 of each subunit). Of these seven, three are within 9 Å of the flavin group while the other four are farther away. These three are threonine 463, valine 464, and histidine 466. They are colored blue and are connected with the ligand via white monitor lines. The other four conserved residues are colored cyan, but are too far to really interact with the flavin group (colored cpk). Beta sheets are colored yellow to showcase the secondary structure of the entire subunit. Evolutionary preservation of the Thr463, </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>'''Choline oxidase''' is the enzyme that catalyzes the reaction between choline and betaine glycine. Betaine glycine is an osmoprotectant and instrumental in helping plants and bacteria survive dry conditions. Studying the choline oxidase may help in the development of controlling populations of beneficial plants or pathogenic bacteria. The data was analyzed using the BLAST and Rasmol programs. The structure of choline oxidase from Arthrobacter globiformis (bacteria) was compared with the structure of the complimentary protein in Mus musculus (mice), carnitine acetyltransferase (Altschul et al., 2005). There are seven amino acids evolutionarily preserved within the vicinity of the flavin group (between amino acids 460 to 483 of each subunit). Of these seven, three are within 9 Å of the flavin group while the other four are farther away. These three are threonine 463, valine 464, and histidine 466. They are colored blue and are connected with the ligand via white monitor lines. The other four conserved residues are colored cyan, but are too far to really interact with the flavin group (colored cpk). Beta sheets are colored yellow to showcase the secondary structure of the entire subunit. Evolutionary preservation of the Thr463, </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><scene name='User:Mohammad_Rao/Sandbox1_Choline_Oxidase/Choline_oxidase-_2_residues/1'>His 466, and Val 464</scene> may signify an importance in aiding the function of the flavin group as it relates to the activity of the enzyme. Previous studies indicate that His466 is indeed important in the function of choline oxidase (Quaye, Lountos, Fan, Orville, & Gadda, 2008).</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><scene name='User:Mohammad_Rao/Sandbox1_Choline_Oxidase/Choline_oxidase-_2_residues/1'>His 466, and Val 464</scene> may signify an importance in aiding the function of the flavin group as it relates to the activity of the enzyme. Previous studies indicate that His466 is indeed important in the function of choline oxidase (Quaye, Lountos, Fan, Orville, & Gadda, 2008).</div></td></tr>
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<td colspan="2" class="diff-lineno">Line 19:</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>== Discussion ==</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>== Discussion ==</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>Threonine 463, valine 464, and histidine 466 are evolutionarily preserved from bacteria to mice in an enzyme that changed drastically. We found that the Histidine 466 is 4.09 Å from the flavin group, that valine 464 is 5.07 Å away, and that threonine 463 is 7.67 Å away. Each of these three residues should therefore be of some importance to the stability of the flavin group, seeing as they were evolutionarily critical. It is evident that His466 acts as a base in the active site of choline oxidase (Chen and Murata, 2002). However, the functions of Thr463 and Val464 are unknown. Therefore, further research would be necessary to determine the functions of all of the amino acids lining the active site. Mutational studies will also help a great deal in our understanding of the enzyme to see what effect mutating any combination of these three amino acids would have on the enzymatic activity of choline oxidase. Knowing the functions of the amino acids in the active site will enable us to devise genetically modified choline oxidase enzymes. Were any recombinant enzymes found to be functionally better, then they could be introduced to a population of plants to genetically induce potential resistance to drought. On the other hand, recombinant choline oxidase enzymes that were catalytically slower could be studied for their effect on reducing, if not completely suppressing, the growth of pathogenic bacterial colonies. </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>Threonine 463, valine 464, and histidine 466 are evolutionarily preserved from bacteria to mice in an enzyme that changed drastically. We found that the Histidine 466 is 4.09 Å from the flavin group, that valine 464 is 5.07 Å away, and that threonine 463 is 7.67 Å away. Each of these three residues should therefore be of some importance to the stability of the flavin group, seeing as they were evolutionarily critical. It is evident that His466 acts as a base in the active site of choline oxidase (Chen and Murata, 2002). However, the functions of Thr463 and Val464 are unknown. Therefore, further research would be necessary to determine the functions of all of the amino acids lining the active site. Mutational studies will also help a great deal in our understanding of the enzyme to see what effect mutating any combination of these three amino acids would have on the enzymatic activity of choline oxidase. Knowing the functions of the amino acids in the active site will enable us to devise genetically modified choline oxidase enzymes. Were any recombinant enzymes found to be functionally better, then they could be introduced to a population of plants to genetically induce potential resistance to drought. On the other hand, recombinant choline oxidase enzymes that were catalytically slower could be studied for their effect on reducing, if not completely suppressing, the growth of pathogenic bacterial colonies. </div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div> </div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;"></StructureSection></ins></div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>==3D structure of Choline oxidase==</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>==3D structure of Choline oxidase==</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;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
</table>Alexander Berchanskyhttps://proteopedia.org/index.php?title=Choline_Oxidase&diff=2508125&oldid=prevMichal Harel at 08:43, 8 December 20152015-12-08T08:43:11Z<p></p>
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 08:43, 8 December 2015</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>== Abstract ==</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>== Abstract ==</div></td></tr>
<tr><td class="diff-marker" data-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><applet load='2JBV' size='<del style="font-weight: bold; text-decoration: none;">400</del>' frame='true' align='right' caption='Choline Oxidase dimer complex with pteridin derivative and DMSO [[2jbv]]' /></div></td><td class="diff-marker" data-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><applet load='2JBV' size='<ins style="font-weight: bold; text-decoration: none;">350</ins>' frame='true' align='right' caption='Choline Oxidase dimer complex with pteridin derivative and DMSO [[2jbv]]' /></div></td></tr>
<tr><td class="diff-marker" data-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>'''Choline oxidase''' is the enzyme that catalyzes the reaction between choline and betaine glycine. Betaine glycine is an osmoprotectant and instrumental in helping plants and bacteria survive dry conditions. Studying the choline oxidase may help in the development of controlling populations of beneficial plants or pathogenic bacteria. The data was analyzed using the BLAST and Rasmol programs. The structure of choline oxidase from Arthrobacter globiformis (bacteria) was compared with the structure of the complimentary protein in Mus musculus (mice), carnitine acetyltransferase (Altschul et al., 2005). There are seven amino acids evolutionarily preserved within the vicinity of the flavin group (between amino acids 460 to 483 of each subunit). Of these seven, three are within 9 Å of the flavin group while the other four are farther away. These three are threonine 463, valine 464, and <del style="font-weight: bold; text-decoration: none;">histadine </del>466. They are colored blue and are connected with the ligand via white monitor lines. The other four conserved residues are colored cyan, but are too far to really interact with the flavin group (colored cpk). Beta sheets are colored yellow to showcase the secondary structure of the entire subunit. Evolutionary preservation of the Thr463, </div></td><td class="diff-marker" data-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>'''Choline oxidase''' is the enzyme that catalyzes the reaction between choline and betaine glycine. Betaine glycine is an osmoprotectant and instrumental in helping plants and bacteria survive dry conditions. Studying the choline oxidase may help in the development of controlling populations of beneficial plants or pathogenic bacteria. The data was analyzed using the BLAST and Rasmol programs. The structure of choline oxidase from Arthrobacter globiformis (bacteria) was compared with the structure of the complimentary protein in Mus musculus (mice), carnitine acetyltransferase (Altschul et al., 2005). There are seven amino acids evolutionarily preserved within the vicinity of the flavin group (between amino acids 460 to 483 of each subunit). Of these seven, three are within 9 Å of the flavin group while the other four are farther away. These three are threonine 463, valine 464, and <ins style="font-weight: bold; text-decoration: none;">histidine </ins>466. They are colored blue and are connected with the ligand via white monitor lines. The other four conserved residues are colored cyan, but are too far to really interact with the flavin group (colored cpk). Beta sheets are colored yellow to showcase the secondary structure of the entire subunit. Evolutionary preservation of the Thr463, </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><scene name='User:Mohammad_Rao/Sandbox1_Choline_Oxidase/Choline_oxidase-_2_residues/1'>His 466, and Val 464</scene> may signify an importance in aiding the function of the flavin group as it relates to the activity of the enzyme. Previous studies indicate that His466 is indeed important in the function of choline oxidase (Quaye, Lountos, Fan, Orville, & Gadda, 2008).</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><scene name='User:Mohammad_Rao/Sandbox1_Choline_Oxidase/Choline_oxidase-_2_residues/1'>His 466, and Val 464</scene> may signify an importance in aiding the function of the flavin group as it relates to the activity of the enzyme. Previous studies indicate that His466 is indeed important in the function of choline oxidase (Quaye, Lountos, Fan, Orville, & Gadda, 2008).</div></td></tr>
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</table>Michal Harelhttps://proteopedia.org/index.php?title=Choline_Oxidase&diff=1898928&oldid=prevMichal Harel at 10:01, 20 February 20142014-02-20T10:01:21Z<p></p>
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 10:01, 20 February 2014</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>[[2jbv]] – AgChOx – ''Arthrobacter globiformis''<br /></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>[[2jbv]] – AgChOx – ''Arthrobacter globiformis''<br /></div></td></tr>
<tr><td class="diff-marker" data-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>[[3nne]], [[3ljp]] – AgChOx (mutant)</div></td><td class="diff-marker" data-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>[[3nne]], [[3ljp]] – AgChOx (mutant)<ins style="font-weight: bold; text-decoration: none;"><br /></ins></div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div> </div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;">[[4mjw]] – AgChOx + trimethylglycine<br /></ins></div></td></tr>
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</table>Michal Harelhttps://proteopedia.org/index.php?title=Choline_Oxidase&diff=1735093&oldid=prevMichal Harel at 11:04, 7 March 20132013-03-07T11:04:50Z<p></p>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>==3D structure of Choline oxidase==</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>==3D structure of Choline oxidase==</div></td></tr>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></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>[[2jbv]] – AgChOx – ''Arthrobacter globiformis''<br /></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>[[2jbv]] – AgChOx – ''Arthrobacter globiformis''<br /></div></td></tr>
</table>Michal Harel