Difference between revisions of "Part:BBa K3349011"

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<partinfo>BBa_K3349011 short</partinfo>
 
<partinfo>BBa_K3349011 short</partinfo>
  
The PelC Pectin Lyase is originally from Paenabacillus amylolyticus . This particular pectin lyase is more specific to methylated pectin or homogalacturonan substrates rather than polygalacturonic acid [1]. This protein also works with both PelB(BBa_K3349001) and Pnl(BBa_K3349001) in this organism to effectively break down pectin. PelC has an optimal activity at 55°C and a pH of 10. The Km in in terms of 80% methylated substrates is 0.41 +/-0.06mg/ml. Calcium is a cofactor for this protein and is therefore necessary within the buffer conditions [1].
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The PelC Pectin Lyase is originally from <i>Paenabacillus amylolyticus</i>. This particular pectin lyase is more specific to methylated pectin or homogalacturonan substrates rather than polygalacturonic acid [1]. This protein also works with both PelB (BBa_K3349001) and Pnl (BBa_K3349001) in this organism to effectively break down pectin. PelC has an optimal activity at 55°C and a pH of 10. The Km in in terms of 80% methylated substrates is 0.41 +/-0.06mg/ml. Calcium is a cofactor for this protein and is therefore necessary within the buffer conditions [1].
  
A GFP reporter was added onto the C-terminus. As well a C-terminal his tag was added to the GFp for nickel affinity purification.  
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A GFP reporter was added onto the C-terminus. As well a C-terminal his tag was added to the GFP for nickel affinity purification.  
  
 
<!-- Add more about the biology of this part here
 
<!-- Add more about the biology of this part here

Revision as of 15:24, 7 October 2020


Pectin Lyase PelC-GFP

The PelC Pectin Lyase is originally from Paenabacillus amylolyticus. This particular pectin lyase is more specific to methylated pectin or homogalacturonan substrates rather than polygalacturonic acid [1]. This protein also works with both PelB (BBa_K3349001) and Pnl (BBa_K3349001) in this organism to effectively break down pectin. PelC has an optimal activity at 55°C and a pH of 10. The Km in in terms of 80% methylated substrates is 0.41 +/-0.06mg/ml. Calcium is a cofactor for this protein and is therefore necessary within the buffer conditions [1].

A GFP reporter was added onto the C-terminus. As well a C-terminal his tag was added to the GFP for nickel affinity purification.

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
    INCOMPATIBLE WITH RFC[25]
    Illegal AgeI site found at 901
  • 1000
    INCOMPATIBLE WITH RFC[1000]
    Illegal BsaI.rc site found at 287