Difference between revisions of "Team:CCU Taiwan/Parts"

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            <p class="first" id="ca1">Background</p> 
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                 <p class="first" id="ca1">&emsp;&emsp; “Liggreen” is composed of monolignols, and we have produced three enzymes to catalyze the polymerization. Laccase 1 from Pinus taeda can catalyze monolignols dehydrogenation, which leads to free radical addition of dehydrogenated monolignols. However, after the monolignols become dimers or oligomers, it will be hard for those dimers or oligomers to bind to the active site of laccase 1 and stop the dehydrogenation reaction of monolignols.<br><br>
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                 <p class="description" id="ca1">&emsp;&emsp; “Liggreen” is composed of monolignols, and we have produced three enzymes to catalyze the polymerization. Laccase 1 from Pinus taeda can catalyze monolignols dehydrogenation, which leads to free radical addition of dehydrogenated monolignols. However, after the monolignols become dimers or oligomers, it will be hard for those dimers or oligomers to bind to the active site of laccase 1 and stop the dehydrogenation reaction of monolignols.<br><br>
 
&emsp;&emsp; In this case, we choose the others enzymes, peroxidase 16 and peroxidase 18. Those are isoenzymes from Picea abies, which are able to bind to oligomers and directly polymerize.<br><br>
 
&emsp;&emsp; In this case, we choose the others enzymes, peroxidase 16 and peroxidase 18. Those are isoenzymes from Picea abies, which are able to bind to oligomers and directly polymerize.<br><br>
 
&emsp;&emsp; All the enzymes above can function in the same pH value and buffer, which  is critical to our design for co-reaction in production line.
 
&emsp;&emsp; All the enzymes above can function in the same pH value and buffer, which  is critical to our design for co-reaction in production line.
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            <p class="first" id="ca2">Basic Parts</p>  
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<groupparts>iGEM18 CCU_Taiwan</groupparts>
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<table class="table" border="1.5" style="width:60vw;">
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  <tr style="background:#92cd7e">
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</div>
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    <th>Part Name</th>
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    <th>Part type</th>
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    <th>Description</th>
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    <th>Lenght</th>
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  </tr>
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  <tr>
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    <td><a href="http://parts.igem.org/wiki/index.php?title=Part:BBa_K2809001">BBa_K2809001</a></td>
 +
    <td>Ribosome binding site</td>
 +
    <td>Kozak sequence (Pichia pastoris)</td>
 +
    <td>7</td>
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  </tr>
 +
  <tr>
 +
    <td><a href="http://parts.igem.org/wiki/index.php?title=Part:BBa_K2809002">BBa_K2809002</a></td>
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    <td>Tag</td>
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    <td>Prepro-alpha-factor (codon modified for Pichia pastoris)</td>
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    <td>267</td>
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  </tr>
 +
    <tr>
 +
    <td><a href="http://parts.igem.org/wiki/index.php?title=Part:BBa_K2809010">BBa_K2809010</a></td>
 +
    <td>Protein_Domain</td>
 +
    <td>Mature Lac 1(laccase)</td>
 +
    <td>1719</td>
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  </tr>
 +
    <tr>
 +
    <td><a href="http://parts.igem.org/wiki/index.php?title=Part:BBa_K2809020">BBa_K2809020</a></td>
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    <td>Protein_Domain</td>
 +
    <td>Mature Px18(peroxidase)</td>
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    <td>954</td>
 +
  </tr>
 +
    <tr>
 +
    <td><a href="http://parts.igem.org/wiki/index.php?title=Part:BBa_K2809030">BBa_K2809030</a></td>
 +
    <td>Protein_Domain</td>
 +
    <td>Mature Px16(peroxidase)</td>
 +
    <td>972</td>
 +
  </tr>
 +
</table>
  
 +
            <p class="first" id="ca3">Composite Parts</p>
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<table class="table" border="1.5" style="width:60vw;">
 +
  <tr style="background:#92cd7e">
 +
    <th>Part Name</th>
 +
    <th>Part type</th>
 +
    <th>Description</th>
 +
    <th>Lenght</th>
 +
  </tr>
 +
  <tr>
 +
    <td><a href="http://parts.igem.org/wiki/index.php?title=Part:BBa_K2809011">BBa_K2809011</a></td>
 +
    <td rowspan="3">Composite</td>
 +
    <td>Laccase 1</td>
 +
    <td>1993</td>
 +
  </tr>
 +
  <tr>
 +
    <td><a href="http://parts.igem.org/wiki/index.php?title=Part:BBa_K2809021">BBa_K2809021</a></td>
 +
    <td>Peroxidase 18</td>
 +
    <td>1228</td>
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  </tr>
 +
  <tr>
 +
    <td><a href="http://parts.igem.org/wiki/index.php?title=Part:BBa_K2809031">BBa_K2809031</a></td>
 +
    <td>Peroxidase 16</td>
 +
    <td>1246</td>
 +
  </tr>
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</table>
  
  
 
</html>
 
</html>

Revision as of 18:14, 16 October 2018

Parts


Background

   “Liggreen” is composed of monolignols, and we have produced three enzymes to catalyze the polymerization. Laccase 1 from Pinus taeda can catalyze monolignols dehydrogenation, which leads to free radical addition of dehydrogenated monolignols. However, after the monolignols become dimers or oligomers, it will be hard for those dimers or oligomers to bind to the active site of laccase 1 and stop the dehydrogenation reaction of monolignols.

   In this case, we choose the others enzymes, peroxidase 16 and peroxidase 18. Those are isoenzymes from Picea abies, which are able to bind to oligomers and directly polymerize.

   All the enzymes above can function in the same pH value and buffer, which is critical to our design for co-reaction in production line.




Basic Parts

Part Name Part type Description Lenght
BBa_K2809001 Ribosome binding site Kozak sequence (Pichia pastoris) 7
BBa_K2809002 Tag Prepro-alpha-factor (codon modified for Pichia pastoris) 267
BBa_K2809010 Protein_Domain Mature Lac 1(laccase) 1719
BBa_K2809020 Protein_Domain Mature Px18(peroxidase) 954
BBa_K2809030 Protein_Domain Mature Px16(peroxidase) 972

Composite Parts

Part Name Part type Description Lenght
BBa_K2809011 Composite Laccase 1 1993
BBa_K2809021 Peroxidase 18 1228
BBa_K2809031 Peroxidase 16 1246