Difference between revisions of "Part:BBa K4147006"
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<partinfo>BBa_K4147006 short</partinfo>
 
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The DsbA enzyme from <i>P. aeruginosa</i> is one of the most oxidizing proteins yet characterized [1]. This protein introduces disulfide bonds into proteins secreted to the periplasm.  
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The DsbA enzyme from <i>P. aeruginosa</i> is one of the most oxidizing proteins yet characterized [1]. This protein introduces disulfide bonds into proteins secreted to the periplasm. It was later optimized for <i>E. coli </i> strains.
  
 
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Revision as of 02:38, 9 October 2022


Disulfide interchange protein DsbA from Pseudomonas aeruginosa

The DsbA enzyme from P. aeruginosa is one of the most oxidizing proteins yet characterized [1]. This protein introduces disulfide bonds into proteins secreted to the periplasm. It was later optimized for E. coli strains.

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 NgoMIV site found at 219
    Illegal NgoMIV site found at 403
  • 1000
    COMPATIBLE WITH RFC[1000]


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