| Part Name |
Past Name |
Part Function |
| BBa_K2910000 |
PETase-W159H-S258F with C-Terminal Hexahistidine Tag |
PETase mutant that contains two mutations that result in the nonsynonymous amino acid substitutions W159H and S238F relative to the wildtype sequence. Point mutations enhance catalytic activity of the enzyme by narrowing the active site, which makes PETase more "cutinase-like" according to X-ray crystallography structure analysis. |
| BBa_K2910001 |
LamB::PETase with C-Terminal Hexahistidine Tag |
Fusion between the LamB maltoporin signal sequence and wildtype PETase, which is reported to stimulate extracellular secretion of PETase for poly(ethylene terephthalate) degradation through the sec-dependent pathway of E. coli K-12. |
| BBa_K2910002 |
IsPETase-ML Mut 1 with C-terminal Hexahistidine Tag |
PETase, optimized for E. coli, which degrades poly(ethylene terephthala te. Using a Machine Learning Algorithm to optimize hydrophobicity content, the thermostability of the protein is predicted to be improved. |
| BBa_K2910003/a> |
IsPETase-T88F-I208Y-S238F-S245Y-R280A with C-terminal Hexahistidine Tag (Working Name: Dimi1) |
PETase with several mutations predicted to increase its catalytic activity. The bulky arginine residue at 280 has been mutated to an alanine to reduce steric clash with PET. The other mutations are predicted to increase interaction between isPETase and aromatic moieties of PET. |
| BBa_K2910004 |
IsPETase-T88I-I208F-S238F-S245F-R280T with C-terminal Hexahistidine Tag (Working Name: Dimi2) |
PETase with several mutations predicted to increase its catalytic activity. The bulky arginine residue at 280 has been mutated to threonine, to reduce steric clash with PET and to contribute a hydrogen-bonding interaction with ester oxygen in the PET chain. Mutations at sites 208, 238, and 245 are predicted to increase interaction between isPETase and aromatic moieties of PET. T88 was mutated to isoleucine to better interact with a nonpolar PET moiety. |
| BBa_K2910005 |
IsPETase-T88F-I208F-S238F-S245F-R280T with C-terminal Hexahistidine Tag (Working Name: Dimi3) |
PETase with several mutations predicted to increase its catalytic activity. The bulky arginine residue at 280 has been mutated to threonine, to reduce steric clash with PET and to contribute a hydrogen-bonding interaction with ester oxygen in the PET chain. The other mutations are predicted to increase interaction between isPETase and aromatic moieties of PET. |
| BBa_K2910006 |
IsPETase-T88I-I208Y-S238F-N241T-S245Y-R280T with C-terminal Hexahistidine Tag (Working Name: Dimi4) |
PETase with several mutations predicted to increase its catalytic activity. The bulky arginine residue at 280 has been mutated to threonine, to reduce steric clash with PET and to contribute a hydrogen-bonding interaction with ester oxygen in the PET chain. Mutations at sites 208, 238, and 245 are predicted to increase interaction between isPETase and aromatic moieties of PET. T88 was mutated to isoleucine to better interact with a nonpolar PET moiety. N241 was mutated to threonine, to better-position a hydrogen-bonding interaction with ester oxygen in the PET chain. |
