Difference between revisions of "Part:BBa K4147006:Design"
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===References=== | ===References=== | ||
+ | [1] Shouldice, S. R., Heras, B., Jarrott, R., Sharma, P., Scanlon, M. J., & Martin, J. L. (2010). Characterization of the DsbA Oxidative Folding Catalyst from Pseudomonas aeruginosa Reveals a Highly Oxidizing Protein that Binds Small Molecules. Antioxidants & Redox Signaling, 12(8), 921–931. doi:10.1089/ars.2009.2736 | ||
+ | [2] Zhang, W., Lu, J., Zhang, S., Liu, L., Pang, X., & Lv, J. (2018). Development an effective system to expression recombinant protein in E. coli via comparison and optimization of signal peptides: Expression of Pseudomonas fluorescens BJ-10 thermostable lipase as case study. Microbial Cell Factories, 17(1). doi:10.1186/s12934-018-0894-y |
Revision as of 10:39, 8 October 2022
Disulfide interchange protein DsbA from Pseudomonas aeruginosa
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal NgoMIV site found at 219
Illegal NgoMIV site found at 403 - 1000COMPATIBLE WITH RFC[1000]
Design Notes
Although signal peptides have been successfully used for this purpose, their presence does not always ensure the efficient secretion of protein into the periplasmic space and the formation of soluble, functional proteins that are correctly folded [2].
Source
The CDS comes from the GenBank accession number (NC_002516.2).
References
[1] Shouldice, S. R., Heras, B., Jarrott, R., Sharma, P., Scanlon, M. J., & Martin, J. L. (2010). Characterization of the DsbA Oxidative Folding Catalyst from Pseudomonas aeruginosa Reveals a Highly Oxidizing Protein that Binds Small Molecules. Antioxidants & Redox Signaling, 12(8), 921–931. doi:10.1089/ars.2009.2736 [2] Zhang, W., Lu, J., Zhang, S., Liu, L., Pang, X., & Lv, J. (2018). Development an effective system to expression recombinant protein in E. coli via comparison and optimization of signal peptides: Expression of Pseudomonas fluorescens BJ-10 thermostable lipase as case study. Microbial Cell Factories, 17(1). doi:10.1186/s12934-018-0894-y