ArticleNature communications2025
NAD-dependent dehydrogenases enable efficient growth of Paracoccus denitrificans on the PET monomer ethylene glycol.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 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
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.
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Who cites it
5 citing papers in PubMed.
- Ancestral hydrocarbon metabolism enables PET degradation by a natural bacterial consortium.mSystems · 2026Article
- EngineeringApplied and environmental microbiology · 2026Article
- From screening to sequencing: Investigating the monoethylene glycol (MEG) biodegradation byBiotechnology reports (Amsterdam, Netherlands) · 2026Article
- The Dark Side of Green Energy: Glycol Waste and the Microbes That Can Transform It.Molecules (Basel, Switzerland) · 2026Review
- Bridging Green Chemistry and Circular Economy: A Pathway to Sustainable Polyester Plastics Through Feedstock, Synthesis, and Waste Upcycling.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Review
Corrections and comments
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Authors and funding
10 authors.
Funding
Abstract
Ethylene glycol is a monomer of the plastic polyethylene terephthalate (PET) and an environmental pollutant of increasing concern. Although it is generally accepted that bacteria use ethylene glycol as growth substrate, not all involved enzymes are well understood. Here, we show that Paracoccus denitrificans assimilates ethylene glycol solely via NAD-dependent alcohol and aldehyde dehydrogenases. Using comparative proteomics, we identify a gene cluster that is strongly expressed in the presence of ethylene glycol. We report the functional and structural characterization of EtgB and EtgA, key enzymes encoded by this etg gene cluster. We furthermore show that the transcriptional activator EtgR controls expression of the gene cluster. Adaptive laboratory evolution on ethylene glycol results in faster growth, enabled by increased production of EtgB and EtgA. Bioinformatic analysis reveals that the etg gene cluster is widely distributed among bacteria, suggesting a common role of NAD-dependent dehydrogenases in microbial ethylene glycol assimilation.
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Registered trials
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