ArticleNature communications2023
Structure and function of the metagenomic plastic-degrading polyester hydrolase PHL7 bound to its product.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers, 1 of them a synthesis that pooled it.
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Who cites it
27 citing papers in PubMed, 1 synthesis or guideline pooled it, 96 citations in OpenAlex.
- Atomistic-Level Insights into the Role of Mutations in the Engineering of PET Hydrolases: A Systematic Review.International journal of molecular sciences · 2025Pooled it
- Mechanistic insights into modulation of productive substrate accessibility for efficient PET depolymerization.Nature communications · 2026Article
- Computational engineering of the polyester hydrolase PHL7 for efficient poly(ethylene terephthalate) degradation in biocatalytic recycling processes.Nature communications · 2026Article
- Rethinking plastic waste: innovations in enzymatic breakdown of oil-based polyesters and bioplastics.FEBS open bio · 2026Review
- Molecular dynamics simulations of temperature-dependent PET binding in PETase, ThermoPETase, and FAST-PETase.RSC advances · 2026Article
- Reflections on bio-based PET and plastic waste management: a responsible research and innovation approach.Nature communications · 2026Review
- Dynamic shift of internal electric field accelerates enzymatic polyethylene terephthalate depolymerization.Communications chemistry · 2026Article
- Identification and characterization of R75estA, a halophilic polyester-degrading enzyme from a marine bacterium.Frontiers in microbiology · 2026Article
- Construction of microbial systems for polyethylene terephthalate degradation.Synthetic and systems biotechnology · 2025Review
- Trade-Offs between Stability and Activity of Glycosylated and Non-Glycosylated Polyester Hydrolases PHL7 and PHL7mut3.ACS ES&T engineering · 2025Article
- A third type of PETase from the marine Halopseudomonas lineage.Protein science : a publication of the Protein Society · 2025Article
- Engineering PHL7 for improved poly(ethylene terephthalate) depolymerization via rational design and directed evolution.Chem catalysis · 2025Article
- Carnivorous plants can decompose the polyesters poly(ethylene terephthalate) and poly(butylene adipate terephthalate).Scientific reports · 2025Article
- Mining Thermophile Genomes for New PETases with Exceptional Thermostabilities Using Sequence Similarity Networks.Chembiochem : a European journal of chemical biology · 2025Article
- Structural and Electronic Properties of Poly(ethylene terephthalate) (PET) from Polarizable Molecular Dynamics Simulations.Macromolecules · 2025Article
- Article
- Influence of Wobbling Tryptophan and Mutations on PET Degradation Explored by QM/MM Free Energy Calculations.Journal of chemical information and modeling · 2024Article
- Manufacturing of the highly active thermophile PETases PHL7 and PHL7mut3 using Escherichia coli.Microbial cell factories · 2024Article
- Identification of Cutinolytic Esterase from Microplastic-Associated Microbiota Using Functional Metagenomics and Its Plastic Degrading Potential.Molecular biotechnology · 2024Article
- Biodegradation: the best solution to the world problem of discarded polymers.Bioresources and bioprocessing · 2024Review
Corrections and comments
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Authors and funding
15 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The recently discovered metagenomic-derived polyester hydrolase PHL7 is able to efficiently degrade amorphous polyethylene terephthalate (PET) in post-consumer plastic waste. We present the cocrystal structure of this hydrolase with its hydrolysis product terephthalic acid and elucidate the influence of 17 single mutations on the PET-hydrolytic activity and thermal stability of PHL7. The substrate-binding mode of terephthalic acid is similar to that of the thermophilic polyester hydrolase LCC and deviates from the mesophilic IsPETase. The subsite I modifications L93F and Q95Y, derived from LCC, increased the thermal stability, while exchange of H185S, derived from IsPETase, reduced the stability of PHL7. The subsite II residue H130 is suggested to represent an adaptation for high thermal stability, whereas L210 emerged as the main contributor to the observed high PET-hydrolytic activity. Variant L210T showed significantly higher activity, achieving a degradation rate of 20 µm h
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