ArticleProtein science : a publication of the Protein Society2025
A third type of PETase from the marine Halopseudomonas lineage.
Article 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 8 papers.
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
8 citing papers in PubMed.
- Biodegradation of components from an oxidized polyethylene by aApplied and environmental microbiology · 2026Article
- Why Do PETases Struggle with Crystalline PET? Catalytic Ensemble Sampling Reveals Molecular Bottlenecks.The journal of physical chemistry letters · 2026Article
- Lignocellulose-mediated selection of potential halophilic PET-degrading enzymes from mangrove soil.Nature communications · 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
- Protein engineering: status report.Protein engineering, design & selection : PEDS · 2026Review
- Identification and characterization of R75estA, a halophilic polyester-degrading enzyme from a marine bacterium.Frontiers in microbiology · 2026Article
- A third type of PETase from the marine Halopseudomonas lineage.Protein science : a publication of the Protein Society · 2025Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors.
Funding
Abstract
The enzymatic degradation of polyethylene terephthalate (PET) offers a sustainable solution for PET recycling. Over the past two decades, more than 100 PETases have been characterized, primarily exhibiting similar sequences and structures. Here, we report PET-degrading α/β hydrolases, including HaloPETase1 from the marine Halopseudomonas lineage, thereby extending the narrow sequence space by novel features at the active site. The crystal structure of HaloPETase1 was determined to a resolution of 1.16 Å, revealing a unique active site architecture and a lack of the canonical π-stacking clamp found in PETases so far. Further, variations in active site composition and loop structures were observed. Additionally, we found five more enzymes from the same lineage, two of which have a high similarity to type IIa bacterial PETases, while the other three resemble HaloPETase1. All these enzymes exhibited high salt tolerance ranging from 2.5 to 5 M NaCl, leading to higher total product releases upon PET degradation at 40 or 50°C. Based on these findings, we propose an extension of the existing PETase classification system to include type III PETases.
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.