Computational insights into the catalytic mechanism of is-PETase : an enzyme capable of degrading poly(ethylene) terephthalate
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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.
Shrimpton-Phoenix , E , Mitchell , J B O & Buehl , M 2022 , ' Computational insights into the catalytic mechanism of is -PETase : an enzyme capable of degrading poly(ethylene) terephthalate ' , Chemistry - A European Journal , vol. 28 , no. 70 , e202201728 . https://doi.org/10.1002/chem.202201728
Chemistry - A European Journal
Copyright © 2022 The Authors. Chemistry - A European Journal published by Wiley-VCH GmbH. This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
DescriptionFunding: This work was supported through a studentship from BBSRC in the EastBio doctoral training programme for E. S.-P.
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