Garman lab: Interconversion of lysosomal enzyme specificities: Difference between revisions

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   <text>NAGAL</text>
   <text>NAGAL</text>
  </jmolLink>
  </jmolLink>
</jmol>). The active sites differ in only two residues, and the substrates bind in almost the same way (Fig 1 panel B and C insets: compare the active site of <scene name='78/786673/Gal_active_site/5'>GAL</scene> and <scene name='78/786673/Nagal_active_site/3'>NAGAL</scene>).  
</jmol>). The active sites differ in only two residues, and the substrates bind in almost the same way (Fig 1 panel B and C insets: compare the active site of <scene name='78/786673/Gal_active_site/5'>GAL</scene> and <jmol>
<jmolLink>
  <script> model 2
  </script>
  <text>NAGAL</text>
</jmolLink>
</jmol>).  


The researchers asked the following question: Is it possible to turn one enzyme into the other (in terms of reaction catalyzed)? Their hypothesis was that a simple swap of the two amino acids in the active site that are different would accomplish an interconversion of specificities.
The researchers asked the following question: Is it possible to turn one enzyme into the other (in terms of reaction catalyzed)? Their hypothesis was that a simple swap of the two amino acids in the active site that are different would accomplish an interconversion of specificities.

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Karsten Theis