ArticleChemistry (Weinheim an der Bergstrasse, Germany)2022
Computational Insights into the Catalytic Mechanism of Is-PETase: An Enzyme Capable of Degrading Poly(ethylene) Terephthalate.
Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
9 citing papers in PubMed, 18 citations in OpenAlex.
- Advances in amidases and urethanases as depolymerization biocatalysts.Nature chemical biology · 2026Review
- Molecular dynamics simulations of temperature-dependent PET binding in PETase, ThermoPETase, and FAST-PETase.RSC advances · 2026Article
- The Action of Plastic Degrading Enzyme Is Accelerated Mainly Due to an Increase in Thermal Stability Rather Than by an Inherent Catalytic Effect.Journal of the American Chemical Society · 2025Article
- Influence of Wobbling Tryptophan and Mutations on PET Degradation Explored by QM/MM Free Energy Calculations.Journal of chemical information and modeling · 2024Article
- Exploring the Reaction Mechanism of Polyethylene Terephthalate Biodegradation through QM/MM Approach.The journal of physical chemistry. B · 2024Article
- The reaction mechanism of the Ideonella sakaiensis PETase enzyme.Communications chemistry · 2024Article
- Insights into the Enhancement of the Poly(ethylene terephthalate) Degradation by FAST-PETase from Computational Modeling.Journal of the American Chemical Society · 2023Article
- Trends inComputational and structural biotechnology journal · 2023Review
- Computational Insights into the Catalytic Mechanism of Is-PETase: An Enzyme Capable of Degrading Poly(ethylene) Terephthalate.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
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
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.