{
  "source": "ORD Dataset Wishlist",
  "snapshot_date": "2026-09-25",
  "ord_wishlist_status_at_snapshot": "Available",
  "ord_wishlist_card": "https://github.com/orgs/open-reaction-database/projects/11?pane=issue&itemId=127173320",
  "ord_data_issue": null,
  "title": "High-Throughput 19F NMR Chiral Analysis for Screening and Directed Evolution of Imine Reductases",
  "doi": "10.1021/acscentsci.5c00498",
  "journal": "ACS Central Sci",
  "publication_date": "2025-06-02",
  "authors": [
    "Shucheng Song",
    "Chenyang Wang",
    "Wenjing Bao",
    "Zhenchuang Xu",
    "Jian Wu",
    "Liang Lin",
    "Yanchuan Zhao"
  ],
  "article_open_access": {
    "status": "diamond",
    "license": "cc-by"
  },
  "dataset_size_estimate": 300,
  "experiment_type": "HTE biocatalytic",
  "ord_priority": "Medium",
  "ord_difficulty": "Hard",
  "source_data_kind": "si_pdf_tables",
  "smiles_in_source": "no",
  "needs_author_contact": false,
  "data_locations": [
    {
      "url": "https://pmc.ncbi.nlm.nih.gov/articles/PMC12291108/",
      "what": "PMC open-access copy of the article",
      "license": "CC-BY (per Europe PMC)"
    },
    {
      "url": "https://www.ebi.ac.uk/europepmc/webservices/rest/PMC12291108/supplementaryFiles",
      "what": "Europe PMC supplementary bundle (zip, 6.8 MB) containing oc5c00498_si_001.pdf (6.3 MB, 50 pp). Text-extractable tables: S1 (1a yields/ee across the IRED panel), S2 (2a), S3 (directed evolution mutants of IRED-195), S4 (4a), S5-S9 (validation/conditions/whole-cell/preparative), S10 primers, S11 NCBI sequence IDs for 134 IREDs. Reaction conditions given under tables.",
      "license": "CC-BY (distributed with CC-BY article; SI license not separately stated)"
    },
    {
      "url": "https://doi.org/10.1021/acscentsci.5c00498",
      "what": "ACS version of record (not fetched; ACS pages block bots)",
      "license": "CC-BY (article)"
    }
  ],
  "notes": "This paper screens imine reductases (IREDs) for reductive amination by high-throughput 19F NMR chiral analysis, with directed evolution of IRED-195. There are about 300 reactions. The article is CC-BY and in PMC (PMC12291108). The SI PDF, available from the Europe PMC supplementary-files bundle, is text-extractable. Tables S1-S4 give, per enzyme or mutant, the 19F NMR integrals for the (R)/(S) products and the internal standard, plus yield (%) and ee (%). Tables S5-S9 cover conditions, analytical validation and preparative runs. Reaction conditions are printed under each table. For example, cell-free extract, substrate, amine, NADP+, GDH/glucose recycling, KPi buffer, DMSO, 30 °C, 12 h. Table S11 maps IRED-n labels to NCBI protein accessions, and mutants are given as point mutations of IRED-195. Substrate, amine and product structures appear only as scheme images, so SMILES must be drawn for this small set. Enzymes need an agreed ORD representation, such as a NAME plus a CUSTOM identifier holding the NCBI accession, or an AMINO_ACID_SEQUENCE fetched from NCBI. Record 'N.D.' entries as no product detected, and represent '>99' as a bounded value.",
  "verification_caveats": "Biocatalysis: enzymes are identified by accession or mutation, not SMILES. Cell-free extract and whole-cell catalysts are ill-defined inputs. Cofactor recycling systems add inputs. Outcomes include ee and stereochemistry, and some values are 'N.D.' or '>99'. Several substrates/products mean several templates across tables S1-S4. Yields are computed from integrals versus an internal standard, which is an NMR yield, not an isolated yield."
}