Team:INSA-Lyon/Project/Stage3/Results

From 2010.igem.org

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<p>The data we compiled showed a very high-level of similarity between the FAS I. They all contain conserved domains:</p>
<p>The data we compiled showed a very high-level of similarity between the FAS I. They all contain conserved domains:</p>
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<ol id="list_extra">
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<li>β Ketoacyl-ACP Synthase (2.3.1.41), </li>
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<li>β Ketoacyl-ACP Synthase (2.3.1.41), </li><br>
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<li>Malonyl/Acetyl transferase (2.3.1.38/39), </li>
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<li>Malonyl/Acetyl transferase (2.3.1.38/39), </li><br>
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<li>3 Hydroxyacyl-ACP Dehydrase (4.2.1.61), </li>
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<li>3 Hydroxyacyl-ACP Dehydrase (4.2.1.61), </li><br>
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<li>Enoyl Reductase (1.3.1.10), </li>
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<li>Enoyl Reductase (1.3.1.10), </li><br>
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<li>β Ketoacyl-ACP Reductase ( 1.1.1.100), </li>
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<li>β Ketoacyl-ACP Reductase ( 1.1.1.100), </li><br>
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<li>Thioesterase (3.1.2). </li></ol><br>
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<li>Thioesterase (3.1.2). </li><br>
<div style="text-align:center;">
<div style="text-align:center;">

Revision as of 18:57, 23 October 2010




Stage 3 : Results


The data we compiled showed a very high-level of similarity between the FAS I. They all contain conserved domains:


  • β Ketoacyl-ACP Synthase (2.3.1.41),

  • Malonyl/Acetyl transferase (2.3.1.38/39),

  • 3 Hydroxyacyl-ACP Dehydrase (4.2.1.61),

  • Enoyl Reductase (1.3.1.10),

  • β Ketoacyl-ACP Reductase ( 1.1.1.100),

  • Thioesterase (3.1.2).