{
  "abstract": "Among the promising microbial platforms to produce value-added products from CO₂, chemolithoautotrophic bacteria, such as Cupriavidus necator H16 (C. necator), stand out due to their ability to fix CO₂ via the Calvin-Benson-Bassham (CBB) cycle. Although C. necator has been extensively studied as a biotechnological production host, several of its biosynthetic pathways remain incompletely characterized at the biochemical level. This includes l-methionine biosynthesis, for which genome-based functional annotations of key enzymes have not been validated experimentally. In this study, we identified and characterized CnMetXS, a homoserine O-succinyltransferase involved in l-methionine biosynthesis in C. necator. Biochemical characterization demonstrated that CnMetXS catalyzes the transsuccinylation of l-homoserine to O-succinyl-l-homoserine but exhibits no transacetylase activity. Additionally, we determined the apo crystal structure of CnMetXS at 1.86 Å resolution, revealing a homodimer with a MetX-G2 active-site architecture and distinct conformations of the active-site lid region. Structural analysis and docking suggest that Arg335 stabilizes the succinylated enzyme intermediate and explains the observed succinyl-CoA specificity. Together, these results establish the function of CnMetXS and pave the way for metabolic engineering strategies to produce l-methionine in C. necator.",
  "abstract_shown": true,
  "affiliations": [
    "Department of Chemical and Pharmaceutical Biology, Groningen Research Institute of Pharmacy, University of Groningen, Groningen, The Netherlands.",
    "iAMB - Institute of Applied Microbiology, RWTH Aachen University, Aachen, Germany."
  ],
  "article_type": "research article",
  "arxiv": null,
  "author_total": 6,
  "authors": [
    {
      "affs": [
        0
      ],
      "name": "Hannah Pia Franziska Meier",
      "orcid": "0000-0001-5765-9381"
    },
    {
      "affs": [
        0
      ],
      "name": "Rick Oerlemans",
      "orcid": "0000-0001-7114-3736"
    },
    {
      "affs": [
        0
      ],
      "name": "Henrik Terholsen",
      "orcid": "0000-0001-9625-8177"
    },
    {
      "affs": [
        0
      ],
      "name": "Matthew R Groves",
      "orcid": "0000-0001-9859-5177"
    },
    {
      "affs": [
        1
      ],
      "name": "Lars Lauterbach",
      "orcid": "0000-0002-6601-6473"
    },
    {
      "affs": [
        0
      ],
      "name": "Sandy Schmidt",
      "orcid": "0000-0002-8443-8805"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/4sxb2rsvqh8sh.bib",
  "cited_by": 0,
  "doi": "10.1002/cbic.70564",
  "fulltext_url": "https://europepmc.org/articles/PMC13683966",
  "id": "4sxb2rsvqh8sh",
  "issns": [
    "1439-4227",
    "1439-7633"
  ],
  "landing_url": "https://europepmc.org/article/MED/42902934",
  "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": [
    [
      "openalex",
      "1312|Microbial Metabolic Engineering and Bioproduction"
    ]
  ],
  "openalex": "W7169757973",
  "pdf_url": "https://europepmc.org/articles/PMC13683966?pdf=render",
  "pmcid": "PMC13683966",
  "pmid": "42902934",
  "published": "2026-10-01",
  "publisher": null,
  "ris": "https://research.draconitic.com/paper/4sxb2rsvqh8sh.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:19:57Z",
      "native_id": "MED:42902934",
      "source": "europepmc",
      "url": "https://europepmc.org/article/MED/42902934"
    }
  ],
  "subjects": [
    {
      "field": "biochemistry",
      "origin": "openalex:1312|Microbial Metabolic Engineering and Bioproduction",
      "subfield": "molecular-biology"
    }
  ],
  "title": "Characterization and Crystal Structure Elucidation of the l-Homoserine O-Succinyltransferase MetXS From Cupriavidus necator H16.",
  "title_text": "Characterization and Crystal Structure Elucidation of the l-Homoserine O-Succinyltransferase MetXS From Cupriavidus necator H16.",
  "type": "peer-reviewed",
  "updated_at": "2026-10-30T12:19:57Z",
  "url": "https://research.draconitic.com/paper/4sxb2rsvqh8sh",
  "venue": "Chembiochem : a European journal of chemical biology",
  "versions": []
}