Thioredoxin with polylinker
Sequence and Features
- 10COMPATIBLE WITH RFC
- 12COMPATIBLE WITH RFC
- 21Illegal BamHI site found at 367
Illegal XhoI site found at 373
- 23COMPATIBLE WITH RFC
- 25COMPATIBLE WITH RFC
- 1000COMPATIBLE WITH RFC
Usage and Biology
This part previously functioned as a DNA recombination and repair protein in E. coli.
Thioredoxin can facilitate protein folding. And this par has its potential of being used in a fusion protein design.
It is also found that Thioredoxin is capable of increasing enzyme activity of our protein, MSMEG5998(BBa_K2382001). We designed a polylinker that has multiple restriction cutting sites at the end of this part for future iGEM teams who want to make their protein more effective.
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)
Edward R. LaVallie1, Elizabeth A. DiBlasio1, Sharlotte Kovacic1, Kathleen L. Grant1, Paul F. Schendel1 & John M. McCoy1. A Thioredoxin Gene Fusion Expression System That Circumvents Inclusion Body Formation in the E. coli Cytoplasm. Nature Biotechnology 11, 187 - 193 (1993) doi:10.1038/nbt0293-187
Escherichia coli str. K-12 substr. MG1655 https://www.ncbi.nlm.nih.gov/nuccore/NC_000913.3
|function||enzyme joint in reductionoxidation reaction|