Difference between revisions of "Part:BBa K5233021:Design"
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+ | Cui Y, Chen Y, Sun J, Zhu T, Pang H, Li C, Geng WC, Wu B. Computational redesign of a hydrolase for nearly complete PET depolymerization at industrially relevant high-solids loading. Nat Commun. 2024 Feb 15;15(1):1417. doi: 10.1038/s41467-024-45662-9. PMID: 38360963; PMCID: PMC10869840. |
Revision as of 03:26, 2 October 2024
TurboPETase(malE), a designed enzyme that can be secreted into the extracellular space
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal AgeI site found at 234
Illegal AgeI site found at 590
Illegal AgeI site found at 635 - 1000COMPATIBLE WITH RFC[1000]
Design Notes
Because PET is extracellular, we need to secrete TurboPETase into the extracellular space with a signal peptide. Enhancers can enhance signal peptide effects.
Source
The TurboPETase comes from an assay called "Computational redesign of a hydrolase for nearly complete PET depolymerization at industrially relevant high-solids loading". The malE comes from maltose/maltodextrin binding periplasmic protein. The enhancer comes from an assay called "Excretory expression of IsPETase in E. coli by an enhancer of signal peptides and enhanced PET hydrolysis".
References
Cui Y, Chen Y, Sun J, Zhu T, Pang H, Li C, Geng WC, Wu B. Computational redesign of a hydrolase for nearly complete PET depolymerization at industrially relevant high-solids loading. Nat Commun. 2024 Feb 15;15(1):1417. doi: 10.1038/s41467-024-45662-9. PMID: 38360963; PMCID: PMC10869840.