{
  "abstract": "L-Methionine deprivation for cancer treatment requires pyridoxal 5′-phosphate (PLP)-dependent L-methionine γlyases (MGL) with sustained activity in plasma. We investigated the MGL from the alkaliphilic thermophile Thermobrachium celere (TcMGL), which was compared to that from Pseudomonas putida (PpMGL) as a reference. Catalysis was limited to L-methionine, L-homocysteine, and L-cysteine, with highest catalytic efficiency towards Lmethionine. Binding of apo-TcMGL to PLP results from an endothermic entropy-driven process, contrasting with apo-PpMGL that binds to cofactor following an exothermic enthalpy-driven reaction, as demonstrated with isothermal titration calorimetry. The tetrameric crystal structure of TcMGL revealed a mobile domain adopting open and closed conformations, regulating access of substrate and PLP to the active site. TcMGL exhibited great stability in human plasma in vitro. Half-life of the active enzyme increased from 9.2 h to 66.7 h with increasing PLP concentration, in much greater magnitude than that of PpMGL. Two-way ANOVA demonstrated a highly significant effect on half-lives of enzyme type and PLP concentration. The enzyme eliminated L-methionine from human plasma and exerted potent cytotoxicity against human carcinoma cells in vitro. TcMGL favourable characteristics make it a suitable candidate for treatment of cancer.",
  "abstract_shown": true,
  "affiliations": [],
  "article_type": null,
  "arxiv": null,
  "author_total": 10,
  "authors": [
    {
      "name": "Nathan Ferchaud"
    },
    {
      "name": "David Kopečný"
    },
    {
      "name": "Miroslav Peřina"
    },
    {
      "name": "Angélique Boyer"
    },
    {
      "name": "Sihem Hentati"
    },
    {
      "name": "Clément Pontoizeau"
    },
    {
      "name": "Christophe Desterke"
    },
    {
      "name": "Vladimir Kryštof"
    },
    {
      "name": "David Machover"
    },
    {
      "name": "Pierre Briozzo"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/5ptzcf40212gj.bib",
  "cited_by": 1,
  "doi": "10.1016/j.ijbiomac.2025.147876",
  "fulltext_url": null,
  "id": "5ptzcf40212gj",
  "issns": [
    "0141-8130"
  ],
  "landing_url": "https://agroparistech.hal.science/hal-05636257v1",
  "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": [
    [
      "hal",
      "0.sdv"
    ],
    [
      "openalex",
      "1305|Cancer Research and Treatments"
    ]
  ],
  "openalex": "W4414578781",
  "pdf_url": "https://agroparistech.hal.science/hal-05636257/document",
  "pmcid": null,
  "pmid": "41005402",
  "published": "2026-09-01",
  "publisher": "Elsevier",
  "ris": "https://research.draconitic.com/paper/5ptzcf40212gj.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:17:24Z",
      "native_id": "hal-05636257",
      "source": "hal",
      "url": "https://agroparistech.hal.science/hal-05636257v1"
    }
  ],
  "subjects": [
    {
      "field": "biology",
      "origin": "openalex:1305|Cancer Research and Treatments",
      "subfield": "systems-synthetic"
    }
  ],
  "title": "The methioninase from the alkalithermophile Thermobrachium celere possesses suitable properties for treatment of cancer",
  "title_text": "The methioninase from the alkalithermophile Thermobrachium celere possesses suitable properties for treatment of cancer",
  "type": "peer-reviewed",
  "updated_at": "2026-10-30T12:17:24Z",
  "url": "https://research.draconitic.com/paper/5ptzcf40212gj",
  "venue": "International Journal of Biological Macromolecules",
  "versions": []
}