{
  "abstract": "Split transketolases (split TKs) are an underexplored class of carboligases with potential for application in biocatalysis. Here, we investigate ten split TKs and reveal substantial functional heterogeneity, with marked differences in substrate scope, activity, enantioselectivity, and robustness. The enzymes accepted diverse acceptors, aliphatic and aromatic, while retaining the canonical (S)-selectivity of full-length TKs. Pyruvate acceptance further revealed distinct catalytic behaviours, including cross-coupling and self-coupling specificity. Selected enzymes also displayed high organic solvent tolerance. Notably, pQR2829 combined high activity, strong stereocontrol, and cross-coupling specificity, whereas pQR2809 showed exceptional robustness and broad substrate acceptance. Overall, these findings establish split TKs as a diverse and promising class of carboligases for further biocatalytic development and engineering.",
  "abstract_shown": true,
  "affiliations": [
    "aDepartment of Biochemical Engineering, University College London, Bernard Katz Building, Gower Street, London, WC1E 6BT, UK.",
    "bDepartment of Chemistry, University College London, 20 Gordon Street, London, WC1H 0AJ, UK.",
    "aDepartment of Biochemical Engineering, University College London, Bernard Katz Building, Gower Street, London, WC1E 6BT, UK.bDepartment of Chemistry, University College London, 20 Gordon Street, London, WC1H 0AJ, UK.",
    "bDepartment of Chemistry, University College London, 20 Gordon Street, London, WC1H 0AJ, UK.cManufacturing Futures Laboratory, University College London, 7 Sidings Street, London, E20 2AE, UK.",
    "aDepartment of Biochemical Engineering, University College London, Bernard Katz Building, Gower Street, London, WC1E 6BT, UK.cManufacturing Futures Laboratory, University College London, 7 Sidings Street, London, E20 2AE, UK."
  ],
  "article_type": "research article",
  "arxiv": null,
  "author_total": 6,
  "authors": [
    {
      "affs": [
        0
      ],
      "name": "Alessia Tonoli",
      "orcid": "0000-0002-6032-407X"
    },
    {
      "affs": [
        1
      ],
      "name": "Silvia Anselmi",
      "orcid": "0000-0003-3087-7287"
    },
    {
      "affs": [
        2
      ],
      "name": "Yeke Ni"
    },
    {
      "affs": [
        0
      ],
      "name": "John M. Ward",
      "orcid": "0000-0002-4415-5544"
    },
    {
      "affs": [
        3
      ],
      "name": "Helen C. Hailes",
      "orcid": "0000-0001-5574-4742"
    },
    {
      "affs": [
        4
      ],
      "name": "Jack W. E. Jeffries",
      "orcid": "0000-0003-4143-2339"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/exermb3fmqd0n.bib",
  "cited_by": 0,
  "doi": "10.1039/d6cb00243a",
  "fulltext_url": "https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13663882/?tool=EBI",
  "id": "exermb3fmqd0n",
  "issns": [
    "2633-0679"
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  "landing_url": "https://europepmc.org/article/PMC/PMC13663882",
  "language": "eng",
  "licence": "CC-BY",
  "licence_label": "CC BY",
  "licence_source": "article",
  "licence_url": "https://creativecommons.org/licenses/by/4.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
      "heading",
      "Chemistry"
    ],
    [
      "lcc",
      "QD1-999"
    ],
    [
      "lcc",
      "QH301-705.5"
    ],
    [
      "openalex",
      "1312|Enzyme Catalysis and Immobilization"
    ]
  ],
  "openalex": "W7220837256",
  "pdf_url": "https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13663882/pdf/?tool=EBI",
  "pmcid": "PMC13663882",
  "pmid": "42877683",
  "published": "2026-10-01",
  "publisher": "The Royal Society of Chemistry",
  "ris": "https://research.draconitic.com/paper/exermb3fmqd0n.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:17:20Z",
      "native_id": "PMC:PMC13663882",
      "source": "europepmc",
      "url": "https://europepmc.org/article/PMC/PMC13663882"
    },
    {
      "first_seen": "2026-11-05T14:21:03Z",
      "native_id": "1db0f22b16244973b5ef828d21102f24",
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      "url": "https://doi.org/10.1039/d6cb00243a"
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    {
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      "native_id": "PMC13663882",
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      "url": "https://doi.org/10.1039/d6cb00243a"
    }
  ],
  "subjects": [
    {
      "field": "biochemistry",
      "origin": "openalex:1312|Enzyme Catalysis and Immobilization",
      "subfield": "molecular-biology"
    }
  ],
  "title": "Exploring the biocatalytic potential of wild-type split transketolases",
  "title_text": "Exploring the biocatalytic potential of wild-type split transketolases",
  "type": "peer-reviewed",
  "updated_at": "2026-11-07T12:23:32Z",
  "url": "https://research.draconitic.com/paper/exermb3fmqd0n",
  "venue": "RSC chemical biology",
  "versions": []
}