{
  "abstract": "Fluorinases have high potential for industrial biofluorination, but any applications have been precluded by low catalytic efficiency and resistance to active site engineering. In this work, we employed PRIZM, a computational workflow utilizing an existing low-N data set and zero-shot models for in silico prediction of activity-enhancing mutations at distal sites. The combination of these predictions with expert opinion led to the identification of 21 fluorinase mutants with enhanced relative activities, while 3 variants showed increased melting temperatures. A mutation in the hexameric interface, K237R, resulted in the largest stability gain, a more than 3.2-fold improvement in catalytic efficiency at 57 °C, and an 8-fold increase in relative activity at 62 °C. These results highlight the potential of distal fluorinase engineering for improving properties required to realize its industrial applications.",
  "abstract_shown": true,
  "affiliations": [
    "The Novo Nordisk Foundation Center for Biosustainability, Technical University of Denmark, Søltofts Plads 220, 2200 Kongens Lyngby, Denmark",
    "Loschmidt Laboratories, Department of Experimental Biology and RECETOX, Faculty of Science, Masaryk University, Kamenice 5, 625 00 Brno, Czech Republic",
    "International Clinical Research Center, St. Anne’s University Hospital, Pekařská 664/53, 602 00 Brno, Czech Republic"
  ],
  "article_type": "research article",
  "arxiv": null,
  "author_total": 6,
  "authors": [
    {
      "affs": [
        0
      ],
      "name": "David Harding-Larsen",
      "orcid": "0009-0001-7800-2669"
    },
    {
      "affs": [
        0
      ],
      "name": "Brianna M. Lax",
      "orcid": "0000-0002-9727-7529"
    },
    {
      "affs": [
        0
      ],
      "name": "Christopher Kurt Weingarten",
      "orcid": "0009-0004-1246-0415"
    },
    {
      "affs": [
        0
      ],
      "name": "Aboubakar Sako"
    },
    {
      "affs": [
        1,
        2
      ],
      "name": "Stanislav Mazurenko",
      "orcid": "0000-0003-3659-4819"
    },
    {
      "affs": [
        0
      ],
      "name": "Ditte Hededam Welner",
      "orcid": "0000-0001-9297-4133"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/9zb9vg7pyy758.bib",
  "cited_by": 0,
  "doi": "10.1021/cbe.6c00028",
  "fulltext_url": "https://pmc.ncbi.nlm.nih.gov/articles/PMC13697940/",
  "id": "9zb9vg7pyy758",
  "issns": [
    "2836-967X"
  ],
  "landing_url": "https://doi.org/10.1021/cbe.6c00028",
  "language": "en",
  "licence": "CC-BY-4.0",
  "licence_label": "CC BY 4.0",
  "licence_source": "article",
  "licence_url": "https://creativecommons.org/licenses/by/4.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
      "heading",
      "Article"
    ],
    [
      "openalex",
      "1312|Enzyme Catalysis and Immobilization"
    ]
  ],
  "openalex": "W7172522540",
  "pdf_url": "https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13697940/pdf/?tool=EBI",
  "pmcid": "PMC13697940",
  "pmid": "42936490",
  "published": "2026-08-05",
  "publisher": "American Chemical Society",
  "ris": "https://research.draconitic.com/paper/9zb9vg7pyy758.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:18:54Z",
      "native_id": "PMC13697940",
      "source": "pmc",
      "url": "https://doi.org/10.1021/cbe.6c00028"
    },
    {
      "first_seen": "2026-10-30T12:21:25Z",
      "native_id": "PMC:PMC13697940",
      "source": "europepmc",
      "url": "https://europepmc.org/article/PMC/PMC13697940"
    }
  ],
  "subjects": [
    {
      "field": "biochemistry",
      "origin": "openalex:1312|Enzyme Catalysis and Immobilization",
      "subfield": "molecular-biology"
    }
  ],
  "title": "Data-Efficient Distal Engineering of Fluorinase Using Zero-Shot Models",
  "title_text": "Data-Efficient Distal Engineering of Fluorinase Using Zero-Shot Models",
  "type": "peer-reviewed",
  "updated_at": "2026-10-30T12:34:53Z",
  "url": "https://research.draconitic.com/paper/9zb9vg7pyy758",
  "venue": "Chem & Bio Engineering",
  "versions": []
}