Evidence map›Paper›PMID 39921299›Full record

ArticleAdvanced science (Weinheim, Baden-Wurttemberg, Germany)2025

Structure-Guided Engineering of a Versatile Urethanase Improves Its Polyurethane Depolymerization Activity.

Zhishuai Li, Xu Han, Lin Cong, Parinita Singh, Pedro Paiva, Yannick Branson, Wenshuo Li, Yangyang Chen, Da'san M M Jaradat, Frank Lennartz and 10 more

Abstract read
In one paragraph

Article in Advanced science (Weinheim, Baden-Wurttemberg, Germany), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from 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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

13 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Insights into the Catalytic Activity of a Metagenome-Derived Urethanase.Journal of the American Chemical Society · 2025
    Article
  6. Article
  7. Article
  8. An Update: Enzymatic Synthesis for Industrial Applications.Angewandte Chemie (International ed. in English) · 2025
    Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

20 authors.

Zhishuai LiKey Laboratory of Engineering Biology for Low-carbon Manufacturing, National Engineering Research Center for Industrial Enzymes, National Technology Innovation Center of Synthetic Biology, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, 32 West Seventh Avenue, Tianjin Airport Economic Area, Tianjin, 300308, China.
Xu HanKey Laboratory of Engineering Biology for Low-carbon Manufacturing, National Engineering Research Center for Industrial Enzymes, National Technology Innovation Center of Synthetic Biology, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, 32 West Seventh Avenue, Tianjin Airport Economic Area, Tianjin, 300308, China.
Lin CongKey Laboratory of Engineering Biology for Low-carbon Manufacturing, National Engineering Research Center for Industrial Enzymes, National Technology Innovation Center of Synthetic Biology, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, 32 West Seventh Avenue, Tianjin Airport Economic Area, Tianjin, 300308, China.
Parinita SinghHelmholtz-Zentrum Berlin für Materialien und Energie, Albert-Einstein-Str. 15, D-12489, Berlin, Germany.
Pedro PaivaLAQV@REQUIMTE, Departamento de Química e Bioquímica, Faculdade de Ciências da Universidade do Porto, Rua do Campo Alegre, Porto, 4169-007, Portugal.ORCID https://orcid.org/0000-0002-7003-6055
Yannick BransonDepartment of Biotechnology and Enzyme Catalysis, Institute of Biochemistry, University of Greifswald, Felix-Hausdorff-Str. 4, 17487, Greifswald, Germany.ORCID https://orcid.org/0000-0002-0282-7090
Wenshuo LiKey Laboratory of Engineering Biology for Low-carbon Manufacturing, National Engineering Research Center for Industrial Enzymes, National Technology Innovation Center of Synthetic Biology, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, 32 West Seventh Avenue, Tianjin Airport Economic Area, Tianjin, 300308, China.
Yangyang ChenKey Laboratory of Engineering Biology for Low-carbon Manufacturing, National Engineering Research Center for Industrial Enzymes, National Technology Innovation Center of Synthetic Biology, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, 32 West Seventh Avenue, Tianjin Airport Economic Area, Tianjin, 300308, China.
Da'san M M JaradatHelmholtz-Zentrum Berlin für Materialien und Energie, Albert-Einstein-Str. 15, D-12489, Berlin, Germany.
Frank LennartzHelmholtz-Zentrum Berlin für Materialien und Energie, Albert-Einstein-Str. 15, D-12489, Berlin, Germany.
Thomas BayerDepartment of Biotechnology and Enzyme Catalysis, Institute of Biochemistry, University of Greifswald, Felix-Hausdorff-Str. 4, 17487, Greifswald, Germany.ORCID https://orcid.org/0000-0002-0656-3280
Louis SchmidtDepartment of Pharmaceutical and Medicinal Chemistry, Institute of Pharmacy, University of Greifswald, Friedrich-Ludwig-Jahn-Str. 17, 17489, Greifswald, Germany.
Ulrike GarschaDepartment of Pharmaceutical and Medicinal Chemistry, Institute of Pharmacy, University of Greifswald, Friedrich-Ludwig-Jahn-Str. 17, 17489, Greifswald, Germany.
Song YouSchool of Life Sciences and Biopharmaceutical Sciences, Shenyang Pharmaceutical University, 103 Wenhua Road, Shenhe District, Shenyang, Liaoning, 110016, China.
Pedro Alexandrino FernandesLAQV@REQUIMTE, Departamento de Química e Bioquímica, Faculdade de Ciências da Universidade do Porto, Rua do Campo Alegre, Porto, 4169-007, Portugal.ORCID https://orcid.org/0000-0003-2748-4722
Maria João RamosLAQV@REQUIMTE, Departamento de Química e Bioquímica, Faculdade de Ciências da Universidade do Porto, Rua do Campo Alegre, Porto, 4169-007, Portugal.ORCID https://orcid.org/0000-0002-7554-8324
Uwe T BornscheuerDepartment of Biotechnology and Enzyme Catalysis, Institute of Biochemistry, University of Greifswald, Felix-Hausdorff-Str. 4, 17487, Greifswald, Germany.ORCID https://orcid.org/0000-0003-0685-2696
Gert WeberHelmholtz-Zentrum Berlin für Materialien und Energie, Albert-Einstein-Str. 15, D-12489, Berlin, Germany.ORCID https://orcid.org/0000-0003-3624-1060
Ren WeiDepartment of Biotechnology and Enzyme Catalysis, Institute of Biochemistry, University of Greifswald, Felix-Hausdorff-Str. 4, 17487, Greifswald, Germany.ORCID https://orcid.org/0000-0003-3876-1350
Weidong LiuKey Laboratory of Engineering Biology for Low-carbon Manufacturing, National Engineering Research Center for Industrial Enzymes, National Technology Innovation Center of Synthetic Biology, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, 32 West Seventh Avenue, Tianjin Airport Economic Area, Tianjin, 300308, China.

Funding

European High-Performance Computing Joint Undertaking EHPC-REG-2023R03-163FCT/MCTES LA/P/0008/2020FCT/MCTES UIDB/50006/2020FCT/MCTES UIDP/50006/2020Horizon 2020 Framework Programme 870294Horizon 2020 Framework Programme 953214Investment and Networking Fund of the Helmholtz Association KA2-HSC-10Investment and Networking Fund of the Helmholtz Association KA-HSC-13National Key Research and Development Program of China 2023YFC3905000National Natural Science Foundation of China 32371530Novo Nordisk Fonden NNF22OC0072891Strategic Priority Research Program of the Chinese Academy of Science XDC0120400Tianjin Synthetic Biotechnology Innovation Capacity Improvement Project TSBICIP-IJCP-003Tianjin Synthetic Biotechnology Innovation Capacity Improvement Project TSBICIP-PTJJ-008Tianjin Synthetic Biotechnology Innovation Capacity Improvement Project TSBICIP-PTJJ-014
6 · The paper itself

Abstract

Polyurethane (PUR), the fifth most prevalent synthetic polymer, substantially contributes to the global plastic waste problem. Biotechnology-based recycling methods have recently emerged as innovative solutions to plastic waste disposal and sparked interest among scientific communities and industrial stakeholders in discovering and designing highly active plastic-degrading enzymes. Here, the ligand-free crystal structure of UMG-SP2, a metagenome-derived urethanase with depolymerization activities, at 2.59 Å resolution, as well as its (co-)structures bound to a suicide hydrolase inhibitor and a short-chain carbamate substrate at 2.16 and 2.40 Å resolutions, respectively, is reported. Structural analysis and molecular dynamics simulations reveal that the flexible loop L3 consisting of residues 219-226 is crucial for regulating the hydrolytic activity of UMG-SP2. The semi-rational redesign of UMG-SP2 reveals superior variants, A141G and Q399A, exhibiting over 30.7- and 7.4-fold increased activities on polyester-PUR and a methylene diamine derivative of PUR, respectively, compared to the wild-type enzyme. These findings advance the understanding of the structure-function relationship of PUR-hydrolyzing enzymes, which hold great promise for developing effective industrial PUR recycling processes and mitigating the environmental footprint of plastic waste.

Indexed as

PolyurethanesMolecular Dynamics SimulationPolymerizationProtein EngineeringPolyurethanescrystal structuresenzyme engineeringmolecular dynamics simulationsplastic degradationpolyurethaneurethanase

Identifiers

PMID39921299
PMCPMC11967865

What OpenQuestion holds

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Registered trials

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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.