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This part is a part of the <a href="https://2019.igem.org/Team:Humboldt_Berlin/Part_Collection">Chlamy-HUB-Collection</a>. The PETase is an enzyme that was discovered in the bacterium <i>Ideonella sakaiensis</i> and catalyzes the hydrolysis of PET to MHET (Yoshida et al. 2016). This enzyme has caught the attention of many research groups around the world for its potential to be used for biotechnological applications regarding PET degradation.  
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This part is a part of the <a href="https://2019.igem.org/Team:Humboldt_Berlin/Part_Collection">Chlamy-HUB-Collection</a>. The PETase is an enzyme that was discovered in the bacterium <i>Ideonella sakaiensis</i> and catalyzes the hydrolysis of PET to MHET (Yoshida et al. 2016). This enzyme has caught the attention of many research groups around the world for its potential to be used for biotechnological applications regarding PET degradation. Austin et al. (2018) engineered this enzyme to improve its capacity to degrade PET.
 
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Yoshida, S., Hiraga, K., Takehana, T., Taniguchi, I., Yamaji, H., Maeda, Y., ... & Oda, K. (2016). A bacterium that degrades and assimilates poly (ethylene terephthalate). Science, 351(6278), 1196-1199.
 
Yoshida, S., Hiraga, K., Takehana, T., Taniguchi, I., Yamaji, H., Maeda, Y., ... & Oda, K. (2016). A bacterium that degrades and assimilates poly (ethylene terephthalate). Science, 351(6278), 1196-1199.
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Austin, H. P., Allen, M. D., Donohoe, B. S., Rorrer, N. A., Kearns, F. L., Silveira, R. L., . . . Beckham, G. T. (2018). Characterization and engineering of a plastic-degrading aromatic polyesterase. Proceedings of the National Academy of Sciences, 115(19), E4350.
 
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Latest revision as of 21:21, 21 October 2019


PETase CDS; Enzyme that catalyzes the first degradation step of PET B3-B3

This part is a part of the Chlamy-HUB-Collection. The PETase is an enzyme that was discovered in the bacterium Ideonella sakaiensis and catalyzes the hydrolysis of PET to MHET (Yoshida et al. 2016). This enzyme has caught the attention of many research groups around the world for its potential to be used for biotechnological applications regarding PET degradation. Austin et al. (2018) engineered this enzyme to improve its capacity to degrade PET.

This part was designed to be used with the MoClo standard and has B3-B3 overhangs.

Sequence and Features


Assembly Compatibility:
  • 10
    INCOMPATIBLE WITH RFC[10]
    Illegal PstI site found at 879
  • 12
    INCOMPATIBLE WITH RFC[12]
    Illegal NheI site found at 418
    Illegal PstI site found at 879
  • 21
    INCOMPATIBLE WITH RFC[21]
    Illegal XhoI site found at 142
  • 23
    INCOMPATIBLE WITH RFC[23]
    Illegal PstI site found at 879
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal PstI site found at 879
  • 1000
    COMPATIBLE WITH RFC[1000]



Characterization

Plate_L0-PETase_B3-B3_E.coli
Fig.1 - Successful transformation of L0-PETase_B3-B3 into E. coli.


References

  1. Yoshida, S., Hiraga, K., Takehana, T., Taniguchi, I., Yamaji, H., Maeda, Y., ... & Oda, K. (2016). A bacterium that degrades and assimilates poly (ethylene terephthalate). Science, 351(6278), 1196-1199.
  2. Austin, H. P., Allen, M. D., Donohoe, B. S., Rorrer, N. A., Kearns, F. L., Silveira, R. L., . . . Beckham, G. T. (2018). Characterization and engineering of a plastic-degrading aromatic polyesterase. Proceedings of the National Academy of Sciences, 115(19), E4350.