ArticleJACS Au2024
From Bulk to Binding: Decoding the Entry of PET into Hydrolase Binding Pockets.
Article in JACS Au, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 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.
The trial behind it
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Who cites it
16 citing papers in PubMed.
- Application of the YebF secretion pathway inRSC chemical biology · 2026Article
- Challenges and opportunities in the enzymatic recycling of nylons.Nature chemical biology · 2026Review
- Mechanistic insights into modulation of productive substrate accessibility for efficient PET depolymerization.Nature communications · 2026Article
- Article
- Advances in quantum dot-based fluorescent biosensors for enzyme detection: mechanistic insights and applications in disease.Mikrochimica acta · 2026Review
- Computational engineering of the polyester hydrolase PHL7 for efficient poly(ethylene terephthalate) degradation in biocatalytic recycling processes.Nature communications · 2026Article
- Why Do PETases Struggle with Crystalline PET? Catalytic Ensemble Sampling Reveals Molecular Bottlenecks.The journal of physical chemistry letters · 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
- Protein engineering: status report.Protein engineering, design & selection : PEDS · 2026Review
- Machine Learning-Guided Identification of PET Hydrolases from Natural Diversity.ACS catalysis · 2025Article
- Engineering PHL7 for improved poly(ethylene terephthalate) depolymerization via rational design and directed evolution.Chem catalysis · 2025Article
- Harnessing protein language model for structure-based discovery of highly efficient and robust PET hydrolases.Nature communications · 2025Article
- Standardization guidelines and future trends for PET hydrolase research.Nature communications · 2025Review
- Article
- 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
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Plastic-degrading enzymes facilitate the biocatalytic recycling of poly(ethylene terephthalate) (PET), a significant synthetic polymer, and substantial progress has been made in utilizing PET hydrolases for industrial applications. To fully exploit the potential of these enzymes, a deeper mechanistic understanding followed by targeted protein engineering is essential. Through advanced molecular dynamics simulations and free energy analysis methods, we elucidated the complete pathway from the initial binding of two PET hydrolases-the thermophilic leaf-branch compost cutinase (LCC) and polyester hydrolase 1 (PES-H1)-to an amorphous PET substrate, ultimately leading to a PET chain entering the active site in a hydrolyzable conformation. Our findings indicate that initial PET binding is nonspecific and driven by polar and hydrophobic interactions. We demonstrate that the subsequent entry of PET into the active site can occur via one of three key pathways, identifying barriers related to both PET-PET and PET-enzyme interactions, as well as specific residues highlighted through
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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.