Difference between revisions of "Part:BBa K3468022"

 
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The PETase is an enzyme, which can hydrolyze PET and this mutation protein is changed on the basis of the PETase. This protein is changed from A80V,T113L,T116R,Q119D,S141P,N173R,A179V,Q182I,S193R,A202C,E231C and S278D which can be more stable in higher temperature compared with the wild type.
 
  
 
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===Usage and Biology===
 
===Usage and Biology===
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The PETase is an enzyme, which can hydrolyze PET and this mutation protein is changed on the basis of the PETase. This protein is changed from S to 46 at D position which can be more stable in higher temperature compared with the wild type.
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<span class='h3bb'>Sequence and Features</span>
 
<span class='h3bb'>Sequence and Features</span>
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This mutation increases the hydrogen bond near S46. The hydrogen bond is an interaction formed by N, O and H in a protein, which can stabilize the structure of the protein and improve thermal stability.
  
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We use FoldX to judge the thermal stability of S46D and Jmol to find whether there is a new salt bridge. Finally we use Pymol to find out what interaction make it become stable.
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[[File:PETase Key g.jpeg|400px|thumb|left|Fig.1 PETase-Key in docking]]
 
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===Functional Parameters===
 
===Functional Parameters===
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<partinfo>BBa_K3468002 parameters</partinfo>
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Revision as of 14:47, 27 October 2020

PETase S46D


Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    INCOMPATIBLE WITH RFC[21]
    Unknown
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]

This mutation increases the hydrogen bond near S46. The hydrogen bond is an interaction formed by N, O and H in a protein, which can stabilize the structure of the protein and improve thermal stability.

We use FoldX to judge the thermal stability of S46D and Jmol to find whether there is a new salt bridge. Finally we use Pymol to find out what interaction make it become stable.

Fig.1 PETase-Key in docking