Difference between revisions of "Part:BBa K2982002:Design"
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| − | Modified from wild type IsPETase sequence from ' | + | Modified from wild type IsPETase sequence from 'Characterization and engineering of a plastic-degrading aromatic polyesterase', PNAs, 2018. |
===References=== | ===References=== | ||
Joo, S., Cho, I. J., Seo, H., Son, H. F., Sagong, H., Shin, T. J., . . . Kim, K. (2018). Structural insight into molecular mechanism of poly(ethylene terephthalate) degradation. Nature Communications, 9(1). doi:10.1038/s41467-018-02881-1 | Joo, S., Cho, I. J., Seo, H., Son, H. F., Sagong, H., Shin, T. J., . . . Kim, K. (2018). Structural insight into molecular mechanism of poly(ethylene terephthalate) degradation. Nature Communications, 9(1). doi:10.1038/s41467-018-02881-1 | ||
Revision as of 04:37, 7 August 2019
Coding sequence for S245I/R280L IsPETase double mutant
- 10INCOMPATIBLE WITH RFC[10]Illegal XbaI site found at 348
- 12INCOMPATIBLE WITH RFC[12]Illegal NheI site found at 304
- 21COMPATIBLE WITH RFC[21]
- 23INCOMPATIBLE WITH RFC[23]Illegal XbaI site found at 348
- 25INCOMPATIBLE WITH RFC[25]Illegal XbaI site found at 348
Illegal AgeI site found at 627 - 1000COMPATIBLE WITH RFC[1000]
Design Notes
The mutation sites locate in substrate binding site, subsite II where three MHET moieties are bound through hydrophobic interaction. In TfCut2, Isoleucine 253 residues and Leucine 288 are located at the corresponding positions of Serine 245 and Arginine 280 in subsite II of IsPETase. The resulting double mutant makes the substrate binding site, subunit II more cutinase-like and increases the hydrophobic property of the enzyme.
Source
Modified from wild type IsPETase sequence from 'Characterization and engineering of a plastic-degrading aromatic polyesterase', PNAs, 2018.
References
Joo, S., Cho, I. J., Seo, H., Son, H. F., Sagong, H., Shin, T. J., . . . Kim, K. (2018). Structural insight into molecular mechanism of poly(ethylene terephthalate) degradation. Nature Communications, 9(1). doi:10.1038/s41467-018-02881-1