Part:BBa_K3039020
PETase Reconstructed Ancestor 4
The enzymes PETase and MHETase were first discovered in Ideonella sakaiensis in 2016 by a group of researchers in Japan. These enzymes were found to degrade polyethylene terephthalate (PET) into its monomers, terephthalic acid (TPA) and ethylene glycol (EG). PETase degrades PET into Mono-(2-hydroxyethyl)terephthalic acid (MHET), Bis(2-Hydroxyethyl) terephthalate (BHET) and TPA, the main product being MHET. MHET is further degraded by MHETase into TPA and EG. We are aiming to use mutants of these enzymes to degrade the microfibres that are coming off clothing during washing cycles. The enzymes would be secreted into a filter that captures the microfibres. This is the sequence of one of the four reconstructed ancestors of PETase with a His tag attached to it. The sequence has been obtained through the method of ancestral reconstruction. The His tag has been used in order to more easily identify the enzyme.
Sequence and Features
- 10INCOMPATIBLE WITH RFC[10]Illegal PstI site found at 433
- 12INCOMPATIBLE WITH RFC[12]Illegal PstI site found at 433
- 21COMPATIBLE WITH RFC[21]
- 23INCOMPATIBLE WITH RFC[23]Illegal PstI site found at 433
- 25INCOMPATIBLE WITH RFC[25]Illegal PstI site found at 433
- 1000COMPATIBLE WITH RFC[1000]
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