SynthesisProtein science : a publication of the Protein Society2025
The diversity of PET degrading enzymes: A systematic review of sequence, structure, and function.
Synthesis in Protein science : a publication of the Protein Society, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers, 1 of them a synthesis that pooled it.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
6 citing papers in PubMed, 1 synthesis or guideline pooled it.
- The diversity of PET degrading enzymes: A systematic review of sequence, structure, and function.Protein science : a publication of the Protein Society · 2025Pooled it
- Isosteric Engineering of Enzymes: Overcoming Activity-Stability Trade-Offs by Site-Selective CH → N Substitutions.Angewandte Chemie (International ed. in English) · 2026Article
- Experimental, Genomic, and Structural Evidence Supporting Putative PET-Hydrolases in Thermophilic Bacteria Isolated From Hot Springs in Cajamarca, Peru.MicrobiologyOpen · 2026Article
- Structure-Guided Extremophile Genome Mining Expands the PETase Landscape and Reveals PET-Hydrolysing True Lipase Lineages.Microbial biotechnology · 2026Article
- Discovering PETases: An Interlink Between Engineering Enzymes and Microbiomes.Environmental microbiology · 2026Review
- Through the holes: the biotechnological potential of actinoporins (and other PFPs).Biophysical reviews · 2026Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
Abstract
Polyethylene terephthalate (PET) is one of the most significant plastic pollutants. Unlike other plastic polymers, PET can be degraded by PET-hydrolytic enzymes (PETases). Over the past two decades, numerous publications have reported the discovery, characterization, and engineering of PETases. This review thoroughly examines the sequence, structure, and functional diversity of naturally occurring PETases. To achieve this, we compiled data from 48 publications into a single table. The resulting dataset enabled us to contextualize previously reported features and shed light on the sequence-structure-function relationships of PETases. Finally, we review selected engineering campaigns and suggest future directions for the enzymatic recycling of PET under mesophilic and thermophilic conditions, aiming to understand the gaps to tackle the PET pollution crisis.
Indexed as
Identifiers
What OpenQuestion holds
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.