Difference between revisions of "Part:BBa K3468039"

 
 
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<span class='h3bb'>Sequence and Features</span>
 
<span class='h3bb'>Sequence and Features</span>
 
<partinfo>BBa_K3468039 SequenceAndFeatures</partinfo>
 
<partinfo>BBa_K3468039 SequenceAndFeatures</partinfo>
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Adding hydrogen bonds stabilized α3 helix and α3-β5loop
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screening, which formed hydrogen bonds with 135-ALA and 136-SER. after mutating it into ARG, it formed hydrogen bonds with 151-THR, which stabilized α3 helix and α3-β5loop, which was beneficial to improve the thermal stability of PETase.
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[[File:G139R.png|400px|thumb|left|Fig.1 G139R in PyMOL]]
  
 
<!-- Uncomment this to enable Functional Parameter display  
 
<!-- Uncomment this to enable Functional Parameter display  

Latest revision as of 13:24, 27 October 2020


PETase G139R

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 G to R at 139 position which can be more stable in higher temperature compared with the wild type.

Sequence and Features


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

Adding hydrogen bonds stabilized α3 helix and α3-β5loop screening, which formed hydrogen bonds with 135-ALA and 136-SER. after mutating it into ARG, it formed hydrogen bonds with 151-THR, which stabilized α3 helix and α3-β5loop, which was beneficial to improve the thermal stability of PETase.

Fig.1 G139R in PyMOL