Computational insights into the catalytic mechanism of is-PETase : an enzyme capable of degrading poly(ethylene) terephthalate
Date
15/12/2022Metadata
Show full item recordAbstract
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.
Citation
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
Publication
Chemistry - A European Journal
Status
Peer reviewed
ISSN
0947-6539Type
Journal article
Description
Funding: This work was supported through a studentship from BBSRC in the EastBio doctoral training programme for E. S.-P.Collections
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