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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<span class='h3bb'>Sequence and Features</span>
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<partinfo>BBa_K4147006 SequenceAndFeatures</partinfo>
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===REFERENCES===
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[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

Revision as of 10:38, 8 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.

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