Component
Rat dimethylglycine dehydrogenase / Dmgdh
Rat dimethylglycine dehydrogenase / Dmgdh. 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 it acts on
Rat DMGDH catalyzes oxidative demethylation of dimethylglycine to sarcosine.
Experimental context and source evidence
- evidence_span
- {"source_cache": "artifacts/choline-research/24858690.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e00bbb8f1c2c805e9d7261c286bace5758abd277bc95b3e0a830bd9cdb82a34f", "start_char": 0, "end_char": 1506, "text_sha256": "e00bbb8f1c2c805e9d7261c286bace5758abd277bc95b3e0a830bd9cdb82a34f"}
- experimental_model
- Rat DMGDH crystallography and enzyme characterization
- exposure
- Dimethylglycine turnover and THF-bound structures
- limitations
- Species and assay context retained. The proposed intramolecular transfer route is not represented as a directly observed moving intermediate.
- nutrient_topic
- Choline research collection; topical membership is not evidence of a direct dietary effect. · Choline
- organism
- Rat recombinant enzyme
- plain_language
- After betaine donates one methyl group, another enzyme handles the remaining dimethylglycine.
- primary_references
- [choline-p24858690] Folate in demethylation: the crystal structure of the rat dimethylglycine dehydrogenase complexed with tetrahydrofolate. (2014). https://pubmed.ncbi.nlm.nih.gov/24858690/ DOI: 10.1016/j.bbrc.2014.05.064
- tissue_or_cell_type
- Mitochondrial-enzyme preparation
Choline: metabolism, signaling and nutrient connections (2026-09-17) · lines 659–670
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Rat DMGDH crystallography and enzyme characterization · source_derived_draft · unverified_draft
### choline-dmgdh-sarcosine Rat DMGDH catalyzes oxidative demethylation of dimethylglycine to sarcosine. Condition category: normal nutrient_topic: Choline research collection; topical membership is not evidence of a direct dietary effect. plain_language: After betaine donates one methyl group, another enzyme handles the remaining dimethylglycine. organism: Rat recombinant enzyme tissue_or_cell_type: Mitochondrial-enzyme preparation experimental_model: Rat DMGDH crystallography and enzyme characterization limitations: Species and assay context retained. The proposed intramolecular transfer route is not represented as a directly observed moving intermediate. exposure: Dimethylglycine turnover and THF-bound structures evidence_span: {"source_cache": "artifacts/choline-research/24858690.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e00bbb8f1c2c805e9d7261c286bace5758abd277bc95b3e0a830bd9cdb82a34f", "start_char": 0, "end_char": 1506, "text_sha256": "e00bbb8f1c2c805e9d7261c286bace5758abd277bc95b3e0a830bd9cdb82a34f"} [choline-p24858690] Folate in demethylation: the crystal structure of the rat dimethylglycine dehydrogenase complexed with tetrahydrofolate. (2014). https://pubmed.ncbi.nlm.nih.gov/24858690/ DOI: 10.1016/j.bbrc.2014.05.064
Complete structured claim and evidenceRat DMGDH structures located THF in a domain separated from the FAD-containing active center and connected by an internal channel.
Experimental context and source evidence
- evidence_span
- {"source_cache": "artifacts/choline-research/24858690.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e00bbb8f1c2c805e9d7261c286bace5758abd277bc95b3e0a830bd9cdb82a34f", "start_char": 0, "end_char": 1506, "text_sha256": "e00bbb8f1c2c805e9d7261c286bace5758abd277bc95b3e0a830bd9cdb82a34f"}
- experimental_model
- Rat DMGDH crystallography and enzyme characterization
- exposure
- Dimethylglycine turnover and THF-bound structures
- limitations
- Species and assay context retained. The proposed intramolecular transfer route is not represented as a directly observed moving intermediate.
- nutrient_topic
- Choline research collection; topical membership is not evidence of a direct dietary effect. · Choline
- organism
- Rat recombinant enzyme
- plain_language
- Folate and a riboflavin-derived cofactor occupy distinct sites in the same enzyme.
- primary_references
- [choline-p24858690] Folate in demethylation: the crystal structure of the rat dimethylglycine dehydrogenase complexed with tetrahydrofolate. (2014). https://pubmed.ncbi.nlm.nih.gov/24858690/ DOI: 10.1016/j.bbrc.2014.05.064
- tissue_or_cell_type
- Mitochondrial-enzyme preparation
Choline: metabolism, signaling and nutrient connections (2026-09-17) · lines 672–683
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Rat DMGDH crystallography and enzyme characterization · source_derived_draft · unverified_draft
### choline-dmgdh-thf Rat DMGDH structures located THF in a domain separated from the FAD-containing active center and connected by an internal channel. Condition category: normal nutrient_topic: Choline research collection; topical membership is not evidence of a direct dietary effect. plain_language: Folate and a riboflavin-derived cofactor occupy distinct sites in the same enzyme. organism: Rat recombinant enzyme tissue_or_cell_type: Mitochondrial-enzyme preparation experimental_model: Rat DMGDH crystallography and enzyme characterization limitations: Species and assay context retained. The proposed intramolecular transfer route is not represented as a directly observed moving intermediate. exposure: Dimethylglycine turnover and THF-bound structures evidence_span: {"source_cache": "artifacts/choline-research/24858690.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e00bbb8f1c2c805e9d7261c286bace5758abd277bc95b3e0a830bd9cdb82a34f", "start_char": 0, "end_char": 1506, "text_sha256": "e00bbb8f1c2c805e9d7261c286bace5758abd277bc95b3e0a830bd9cdb82a34f"} [choline-p24858690] Folate in demethylation: the crystal structure of the rat dimethylglycine dehydrogenase complexed with tetrahydrofolate. (2014). https://pubmed.ncbi.nlm.nih.gov/24858690/ DOI: 10.1016/j.bbrc.2014.05.064
Complete structured claim and evidence
Where it participates (unsigned role)
In the THF-coupled DMGDH pathway, a removed one-carbon unit is captured as 5,10-methylenetetrahydrofolate rather than released as free formaldehyde.
Experimental context and source evidence
- evidence_span
- {"source_cache": "artifacts/choline-research/24858690.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e00bbb8f1c2c805e9d7261c286bace5758abd277bc95b3e0a830bd9cdb82a34f", "start_char": 0, "end_char": 1506, "text_sha256": "e00bbb8f1c2c805e9d7261c286bace5758abd277bc95b3e0a830bd9cdb82a34f"}
- experimental_model
- Rat DMGDH crystallography and enzyme characterization
- exposure
- Dimethylglycine turnover and THF-bound structures
- limitations
- Pathway chemistry interpreted with rat enzyme structures; not proof that dietary folate rescue restores every human choline-dependent function.
- nutrient_topic
- Choline research collection; topical membership is not evidence of a direct dietary effect. · Choline
- organism
- Rat recombinant enzyme
- plain_language
- Choline-derived methyl metabolism feeds the folate pool.
- primary_references
- [choline-p24858690] Folate in demethylation: the crystal structure of the rat dimethylglycine dehydrogenase complexed with tetrahydrofolate. (2014). https://pubmed.ncbi.nlm.nih.gov/24858690/ DOI: 10.1016/j.bbrc.2014.05.064
- tissue_or_cell_type
- Mitochondrial-enzyme preparation
Choline: metabolism, signaling and nutrient connections (2026-09-17) · lines 685–696
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Rat DMGDH crystallography and enzyme characterization · source_derived_draft · unverified_draft
### choline-dmgdh-one-carbon In the THF-coupled DMGDH pathway, a removed one-carbon unit is captured as 5,10-methylenetetrahydrofolate rather than released as free formaldehyde. Condition category: normal nutrient_topic: Choline research collection; topical membership is not evidence of a direct dietary effect. plain_language: Choline-derived methyl metabolism feeds the folate pool. organism: Rat recombinant enzyme tissue_or_cell_type: Mitochondrial-enzyme preparation experimental_model: Rat DMGDH crystallography and enzyme characterization limitations: Pathway chemistry interpreted with rat enzyme structures; not proof that dietary folate rescue restores every human choline-dependent function. exposure: Dimethylglycine turnover and THF-bound structures evidence_span: {"source_cache": "artifacts/choline-research/24858690.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e00bbb8f1c2c805e9d7261c286bace5758abd277bc95b3e0a830bd9cdb82a34f", "start_char": 0, "end_char": 1506, "text_sha256": "e00bbb8f1c2c805e9d7261c286bace5758abd277bc95b3e0a830bd9cdb82a34f"} [choline-p24858690] Folate in demethylation: the crystal structure of the rat dimethylglycine dehydrogenase complexed with tetrahydrofolate. (2014). https://pubmed.ncbi.nlm.nih.gov/24858690/ DOI: 10.1016/j.bbrc.2014.05.064
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.