Part:BBa_K2382005

Thioredoxin-FGD fusion protein

Sequence and Features

Assembly Compatibility:

• 10
  COMPATIBLE WITH RFC[10]
• 12
  INCOMPATIBLE WITH RFC[12]

  Illegal NotI site found at 1068
  
• 21
  INCOMPATIBLE WITH RFC[21]

  Illegal BglII site found at 1117
  Illegal BamHI site found at 405
  Illegal XhoI site found at 411
  Illegal XhoI site found at 1383
  
• 23
  COMPATIBLE WITH RFC[23]
• 25
  INCOMPATIBLE WITH RFC[25]

  Illegal NgoMIV site found at 777
  Illegal NgoMIV site found at 975
  Illegal AgeI site found at 741
  
• 1000
  COMPATIBLE WITH RFC[1000]

Usage and Biology

By ligating these two different parts as a fusion protein, it is supposed to raise the solubility of our protein, F420-dependent glucose-6- phosphate dehydrogenase (FGD).

This is a fusion protein made out of Thioredoxin and FGD. Those two proteins have different functions. Thioredoxin can help the protein folding correctly, and have the fusion protein produced in soluble form that are biologically active. FGD could help the electrons transferring from G6P(Glucose 6-phosphate) to the F420(It is a flavin derivative which plays a role like a coenzyme that could help the redox reactions in Methanogens such as Actinobacteria, especially in bacterial lineages.) Finally, the F420 would be reduced to F420H2, attaching two hydrogens and electrons on it. This fusion protein will help us transferring electrons and reduce aflatoxin via MSMEG5998.

References

Carsten Berndt, Christopher Horst Lillig, Arne Holmgren, Thioredoxins and glutaredoxins as facilitators of protein folding, In Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, Volume 1783, Issue 4, 2008, Pages 641-650, ISSN 0167-4889, https://doi.org/10.1016/j.bbamcr.2008.02.003. (http://www.sciencedirect.com/science/article/pii/S0167488908000700)