Part:BBa_K2382005
Thioredoxin-FGD fusion protein
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12INCOMPATIBLE WITH RFC[12]Illegal NotI site found at 1068
- 21INCOMPATIBLE 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 - 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal NgoMIV site found at 777
Illegal NgoMIV site found at 975
Illegal AgeI site found at 741 - 1000COMPATIBLE 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. Both of them have different function. Thioredoxin can help the protein folding correctly, and produce the fusion proteins in soluble form that are biologically active. FGD could help the electron transferred from G6P(Glucose 6-phosphate) to the F420(It is a flavin derivative, and it plays like a coenzyme that could help the redox reactions in methanogens ,many Actinobacteria, especially in bacterial lineages.) Finally, the F420 would be reduced to F420H2,attaching two hydrogens and electron on it. This fusion protein will help us to convert electrons to reduce the compound via MSMEG5998.
Characterization of the Thioredoxin-FGD fusion protein
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)
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