Component
Metal-free molybdopterin / MPT
Metal-free molybdopterin / MPT. Species, exposure and limitations are retained in each linked claim.
3 recorded relationships. Experimental role, claim status and evidence remain attached to each record.
How nutrients influence it
Every nutrient with a recorded effect on this component, credited to the nutrient that acted rather than the chapter that recorded it. Open a nutrient to see the findings and the conditions they were measured under.
Other things that act on it
Enzymes, hormones, genes, and other components with a recorded effect. These are not nutrients, so they do not count toward the arrows above. Each finding names the chapter that recorded it.
How nutrients reach it in more than one step
Chains of two or more recorded steps that end here, grouped by the nutrient they start from. Each step is a separate finding, so a chain is a route a mechanism could take, not proof that it does.
Tracing routes…
What it does
Every recorded relationship this component is part of, grouped by its role. Plain wording comes first; the technical statement follows.
What acts on it
The gephyrin G domain produces adenylylated molybdopterin.
Experimental context and source evidence
- evidence_span
- {"source_cache": "artifacts/molybdenum-research/23163752.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "909388cf5fb7bfa5d2f8444644e20773a7a8ec6a19b4ccb8a4bda78d9ad17c5d", "start_char": 0, "end_char": 1489, "text_sha256": "909388cf5fb7bfa5d2f8444644e20773a7a8ec6a19b4ccb8a4bda78d9ad17c5d"}
- experimental_model
- Purified mammalian gephyrin domains and full multidomain protein; in-vitro Moco reconstitution
- exposure
- MPT adenylation, molybdate insertion and domain-combination assays
- limitations
- No human dietary magnesium intervention; purified domain kinetics should not be turned into supplementation efficacy.
- nutrient_topic
- Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
- organism
- Mammalian protein system
- plain_language
- Gephyrin prepares the scaffold for metal insertion.
- primary_references
- [mo-p23163752] Metal insertion into the molybdenum cofactor: product-substrate channelling demonstrates the functional origin of domain fusion in gephyrin. (2013). https://pubmed.ncbi.nlm.nih.gov/23163752/ DOI: 10.1042/bj20121078
- tissue_or_cell_type
- Purified gephyrin
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 482–493
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified mammalian gephyrin domains and full multidomain protein; in-vitro Moco reconstitution · source_derived_draft · unverified_draft
### mo-gphn-adenylation The gephyrin G domain produces adenylylated molybdopterin. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Gephyrin prepares the scaffold for metal insertion. organism: Mammalian protein system tissue_or_cell_type: Purified gephyrin experimental_model: Purified mammalian gephyrin domains and full multidomain protein; in-vitro Moco reconstitution limitations: No human dietary magnesium intervention; purified domain kinetics should not be turned into supplementation efficacy. exposure: MPT adenylation, molybdate insertion and domain-combination assays evidence_span: {"source_cache": "artifacts/molybdenum-research/23163752.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "909388cf5fb7bfa5d2f8444644e20773a7a8ec6a19b4ccb8a4bda78d9ad17c5d", "start_char": 0, "end_char": 1489, "text_sha256": "909388cf5fb7bfa5d2f8444644e20773a7a8ec6a19b4ccb8a4bda78d9ad17c5d"} [mo-p23163752] Metal insertion into the molybdenum cofactor: product-substrate channelling demonstrates the functional origin of domain fusion in gephyrin. (2013). https://pubmed.ncbi.nlm.nih.gov/23163752/ DOI: 10.1042/bj20121078
Complete structured claim and evidenceThe sulfur used to form the MPT dithiolene group is supplied from the C-terminal thiocarboxylate of the small MPT-synthase subunit.
Experimental context and source evidence
- evidence_span
- {"source_cache": "artifacts/molybdenum-research/12732628.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "154da4e4528674556bef92dfe50f098cfd9ae715c06ea01fc17d64c64b8aa319", "start_char": 0, "end_char": 1322, "text_sha256": "154da4e4528674556bef92dfe50f098cfd9ae715c06ea01fc17d64c64b8aa319"}
- experimental_model
- Purified human MPT synthase and patient-derived point mutants
- exposure
- Precursor Z/cPMP conversion assays
- limitations
- In-vitro assembly and kinetic defects; severity comparisons refer to specific patients, not a universal hierarchy.
- nutrient_topic
- Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
- organism
- Human proteins expressed in Escherichia coli
- plain_language
- MOCS2A carries a chemically attached sulfur supply.
- primary_references
- [mo-p12732628] Mechanistic studies of human molybdopterin synthase reaction and characterization of mutants identified in group B patients of molybdenum cofactor deficiency. (2003). https://pubmed.ncbi.nlm.nih.gov/12732628/ DOI: 10.1074/jbc.m303092200
- tissue_or_cell_type
- Reconstituted MOCS2A/MOCS2B tetramers
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 404–415
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified human MPT synthase and patient-derived point mutants · source_derived_draft · unverified_draft
### mo-mocs2a-sulfur The sulfur used to form the MPT dithiolene group is supplied from the C-terminal thiocarboxylate of the small MPT-synthase subunit. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: MOCS2A carries a chemically attached sulfur supply. organism: Human proteins expressed in Escherichia coli tissue_or_cell_type: Reconstituted MOCS2A/MOCS2B tetramers experimental_model: Purified human MPT synthase and patient-derived point mutants limitations: In-vitro assembly and kinetic defects; severity comparisons refer to specific patients, not a universal hierarchy. exposure: Precursor Z/cPMP conversion assays evidence_span: {"source_cache": "artifacts/molybdenum-research/12732628.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "154da4e4528674556bef92dfe50f098cfd9ae715c06ea01fc17d64c64b8aa319", "start_char": 0, "end_char": 1322, "text_sha256": "154da4e4528674556bef92dfe50f098cfd9ae715c06ea01fc17d64c64b8aa319"} [mo-p12732628] Mechanistic studies of human molybdopterin synthase reaction and characterization of mutants identified in group B patients of molybdenum cofactor deficiency. (2003). https://pubmed.ncbi.nlm.nih.gov/12732628/ DOI: 10.1074/jbc.m303092200
Complete structured claim and evidence
Where it participates (unsigned role)
Human MOCS2A and MOCS2B assemble as active MPT synthase and convert cPMP to molybdopterin.
Experimental context and source evidence
- evidence_span
- {"source_cache": "artifacts/molybdenum-research/12732628.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "154da4e4528674556bef92dfe50f098cfd9ae715c06ea01fc17d64c64b8aa319", "start_char": 0, "end_char": 1322, "text_sha256": "154da4e4528674556bef92dfe50f098cfd9ae715c06ea01fc17d64c64b8aa319"}
- experimental_model
- Purified human MPT synthase and patient-derived point mutants
- exposure
- Precursor Z/cPMP conversion assays
- limitations
- In-vitro assembly and kinetic defects; severity comparisons refer to specific patients, not a universal hierarchy.
- nutrient_topic
- Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
- organism
- Human proteins expressed in Escherichia coli
- plain_language
- Two sulfur atoms create the part of the scaffold that will hold molybdenum.
- primary_references
- [mo-p12732628] Mechanistic studies of human molybdopterin synthase reaction and characterization of mutants identified in group B patients of molybdenum cofactor deficiency. (2003). https://pubmed.ncbi.nlm.nih.gov/12732628/ DOI: 10.1074/jbc.m303092200
- tissue_or_cell_type
- Reconstituted MOCS2A/MOCS2B tetramers
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 391–402
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified human MPT synthase and patient-derived point mutants · source_derived_draft · unverified_draft
### mo-mpt-synthase Human MOCS2A and MOCS2B assemble as active MPT synthase and convert cPMP to molybdopterin. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Two sulfur atoms create the part of the scaffold that will hold molybdenum. organism: Human proteins expressed in Escherichia coli tissue_or_cell_type: Reconstituted MOCS2A/MOCS2B tetramers experimental_model: Purified human MPT synthase and patient-derived point mutants limitations: In-vitro assembly and kinetic defects; severity comparisons refer to specific patients, not a universal hierarchy. exposure: Precursor Z/cPMP conversion assays evidence_span: {"source_cache": "artifacts/molybdenum-research/12732628.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "154da4e4528674556bef92dfe50f098cfd9ae715c06ea01fc17d64c64b8aa319", "start_char": 0, "end_char": 1322, "text_sha256": "154da4e4528674556bef92dfe50f098cfd9ae715c06ea01fc17d64c64b8aa319"} [mo-p12732628] Mechanistic studies of human molybdopterin synthase reaction and characterization of mutants identified in group B patients of molybdenum cofactor deficiency. (2003). https://pubmed.ncbi.nlm.nih.gov/12732628/ DOI: 10.1074/jbc.m303092200
Complete structured claim and evidence
The events it takes part in
A mechanism often involves more than two components. These are the full events, with every participant and its role.
Situations it appears in
Low-supply and faulty-machinery situations recorded in the chapters where this component plays a part.
In the sources
Preserved passages that mention this component, quoted exactly. Open one to read it in context.
Open hypotheses
Proposed ideas that involve this component. They are labeled as hypotheses and do not change any recorded statement.
This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.