Computational insights into the catalytic mechanism of is-PETase: an enzyme capable of degrading poly(ethylene) terephthalate

Eugene Shrimpton-Phoenix, John B. O. Mitchell*, Michael Buehl*

*Corresponding author for this work

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Abstract

Is-PETase has become an enzyme of significant interest due to its ability to catalyse the degradation of polyethylene terephthalate (PET) at mesophilic temperatures. We performed hybrid quantum mechanics and molecular mechanics (QM/MM) at the DSD-PBEP86-D3/ma-def2-TZVP/CHARMM27//rev-PBE-D3/dev2-SVP/CHARMM level to calculate the energy profile for the degradation of a suitable PET model by this enzyme. Very low overall barriers are computed for serine protease-type hydrolysis steps (as low as 34.1 kJ mol-1). Spontaneous deprotonation of the final product, terephthalic acid, with a high computed driving force indicates that product release could be rate limiting.
Original languageEnglish
Article numbere202201728
Number of pages7
JournalChemistry - A European Journal
Volume28
Issue number70
Early online date25 Oct 2022
DOIs
Publication statusPublished - 15 Dec 2022

Keywords

  • Enzyme
  • Catalysis
  • QM/MM
  • Green chemistry
  • Plastics

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