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

doi:10.1002/chem.202201728

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

Research output: Contribution to journal › Article › peer-review

6 Citations (Scopus)

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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 language	English
Article number	e202201728
Number of pages	7
Journal	Chemistry - A European Journal
Volume	28
Issue number	70
Early online date	25 Oct 2022
DOIs	https://doi.org/10.1002/chem.202201728
Publication status	Published - 15 Dec 2022

Keywords

Enzyme
Catalysis
QM/MM
Green chemistry
Plastics

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10.1002/chem.202201728Licence: CC BY

Shrimpton-Phoenix_2022_CEJ_Computational-insights_CC
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.
Final published version, 1.3 MBLicence: CC BY

Computational Insights into the Catalytic Mechanism of Is-PETase: An Enzyme Capable of degrading poly(ethylene) terephthalate (dataset)
Shrimpton-Phoenix, E. (Creator), Mitchell, J. B. O. (Creator) & Buehl, M. (Creator), University of St Andrews, 27 Oct 2022
DOI: 10.17630/486acc90-3be5-43c2-aa08-17c02096bb85
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title = "Computational insights into the catalytic mechanism of is-PETase: an enzyme capable of degrading poly(ethylene) terephthalate",

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.",

keywords = "Enzyme, Catalysis, QM/MM, Green chemistry, Plastics",

author = "Eugene Shrimpton-Phoenix and Mitchell, {John B. O.} and Michael Buehl",

note = "Funding: This work was supported through a studentship from BBSRC in the EastBio doctoral training programme for E. S.-P.",

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T1 - Computational insights into the catalytic mechanism of is-PETase

T2 - an enzyme capable of degrading poly(ethylene) terephthalate

AU - Shrimpton-Phoenix, Eugene

AU - Mitchell, John B. O.

AU - Buehl, Michael

N1 - Funding: This work was supported through a studentship from BBSRC in the EastBio doctoral training programme for E. S.-P.

PY - 2022/12/15

Y1 - 2022/12/15

N2 - 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.

AB - 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.

KW - Enzyme

KW - Catalysis

KW - QM/MM

KW - Green chemistry

KW - Plastics

U2 - 10.1002/chem.202201728

DO - 10.1002/chem.202201728

M3 - Article

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VL - 28

JO - Chemistry - A European Journal

JF - Chemistry - A European Journal

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ER -

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

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Computational Insights into the Catalytic Mechanism of Is-PETase: An Enzyme Capable of degrading poly(ethylene) terephthalate (dataset)

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