Types | DnaRegion
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Roles | Composite
engineered_region
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Sequences | BBa_K1885123_sequence (Version 1)
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Description
PETase is a novel enzyme for the degradation of polyethylene terephthalate (PET) plastic. It was discovered in Ideonella sakaiensis, a bacteria species found by screening PET-exposed microbe communities in Japan. It functions as the first step in the degradation of PET; PETase catalyzes the hydrolysis of PET into terephthalate and ethylene glycol monomers. The N-terminal osmY protein and its signal peptide fused to PETase, with serine-glycine peptide repeats intervening, serves to secrete the PETase out of the cell so that it can act on PET in the cell's local environment. The Anderson promoter with a relative strength of 0.33 that precedes the fusion protein serves to constitutively express the fusion PETase, enhancing the degradation of environmental PET by the presence of more fusion PETase by constitutive expression. This part offers a more efficient initial step for teams interested in the bioremediation of PET, because the first step involved in PET bioremediation is hydrolysis into products that can then be utilized by a cell. Teams can then metabolically engineer bacteria of interest to metabolize ethylene glycol and terephthalate, but initially, these monomers must be produced by hydrolysis. Thus, PET bioremediation depends on the production of metabolizable monomers, and this part offers more efficient production of such monomers.
Notes
We added the glycine-serine linker because we considered the c-terminal osmY domains and n-terminal PETase domains interfering with one another's folding.
Source
The osmY and PETase sequences were drawn from genome sequences of escherichia coli and ideonella sakanesis, respectively.