ArticleJournal of the American Chemical Society2023
Insights into the Enhancement of the Poly(ethylene terephthalate) Degradation by FAST-PETase from Computational Modeling.
Article in Journal of the American Chemical Society, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers, 1 of them a synthesis that pooled it.
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Who cites it
24 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Atomistic-Level Insights into the Role of Mutations in the Engineering of PET Hydrolases: A Systematic Review.International journal of molecular sciences · 2025Pooled it
- Structural analysis of Sphingobium yanoikuyae P4 carboxylesterase reveals conformational and catalytic determinants for PET biodegradation.World journal of microbiology & biotechnology · 2026Article
- Isosteric Engineering of Enzymes: Overcoming Activity-Stability Trade-Offs by Site-Selective CH → N Substitutions.Angewandte Chemie (International ed. in English) · 2026Article
- Plastics and Bioplastics End of Life: A Biocatalytic Perspective.Microbial biotechnology · 2026Article
- Structure-Guided Extremophile Genome Mining Expands the PETase Landscape and Reveals PET-Hydrolysing True Lipase Lineages.Microbial biotechnology · 2026Article
- Emerging Frontiers in CRISPR-Based Strategies for the Detection and Degradation of Microplastics.Life (Basel, Switzerland) · 2026Review
- Integrative frameworks for plastic biodegradation in insect-microbiome systems: mechanistic insights, emerging multi-omics and enzyme engineering perspectives.Biodegradation · 2026Review
- Inactivation of PETase at Interfaces Inhibits PET Plastic Depolymerization.ACS sustainable chemistry & engineering · 2026Article
- Why Do PETases Struggle with Crystalline PET? Catalytic Ensemble Sampling Reveals Molecular Bottlenecks.The journal of physical chemistry letters · 2026Article
- Catalytic Triad-Inspired Nanozyme Catalysts for Ester Hydrolysis in Organic Solvent Mixtures.ACS catalysis · 2026Article
- Molecular dynamics simulations of temperature-dependent PET binding in PETase, ThermoPETase, and FAST-PETase.RSC advances · 2026Article
- Dynamic shift of internal electric field accelerates enzymatic polyethylene terephthalate depolymerization.Communications chemistry · 2026Article
- The effect of ionic strength on PETase enzymes: An experimental and computational study.Protein science : a publication of the Protein Society · 2026Article
- Degradation of polyethylene terephthalate by microorganisms and their enzymes: A review of experimental and in silico research.World journal of microbiology & biotechnology · 2025Review
- Comparison of Polyethylene Terephthalate (PET) Degrading Cutinases from Bacteria and Fungi: Structural Characterization and Molecular Docking Analysis.Applied biochemistry and biotechnology · 2025Article
- 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
- Aliphatic Polyester Recognition and Reactivity at the Active Cleft of a Fungal Cutinase.Journal of chemical information and modeling · 2025Article
- Computational analysis reveals temperature-induced stabilization of FAST-PETase.Computational and structural biotechnology journal · 2025Article
- Unraveling the Interplay between Stability and Flexibility in the Design of Polyethylene Terephthalate (PET) Hydrolases.Journal of chemical information and modeling · 2024Article
- Influence of Wobbling Tryptophan and Mutations on PET Degradation Explored by QM/MM Free Energy Calculations.Journal of chemical information and modeling · 2024Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Polyethylene terephthalate (PET) is the most abundant polyester plastic, widely used in textiles and packaging, but, unfortunately, it is also one of the most discarded plastics after one use. In the last years, the enzymatic biodegradation of PET has sparked great interest owing to the discovery and subsequent mutation of PETase-like enzymes, able to depolymerize PET. FAST-PETase is one of the best enzymes hitherto proposed to efficiently degrade PET, although the origin of its efficiency is not completely clear. To understand the molecular origin of its enhanced catalytic activity, we have carried out a thorough computational study of PET degradation by the FAST-PETase action by employing classical and hybrid (QM/MM) molecular dynamics (MD) simulations. Our findings show that the rate-limiting reaction step for FAST-PETase corresponds to the acylation stage with an estimated free energy barrier of 12.1 kcal mol
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Registered trials
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