Component
Human flavin-containing monooxygenase 1 / FMO1
Human flavin-containing monooxygenase 1 / FMO1. 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
Recombinant human FMO1 catalyzed oxygenation of hypotaurine to taurine in vitro.
Experimental context and source evidence
- evidence_access
- Primary abstract
- experimental_model
- Human FMO1 enzyme assays.
- limitations
- This identifies an enzyme activity; it does not establish FMO1 as the only possible route in every tissue.
- nutrient_topic
- Taurine collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Taurine
- plain_language
- FMO1 completes the hypotaurine-to-taurine step.
- primary_references
- Flavin-Containing Monooxygenase 1 Catalyzes the Production of Taurine from Hypotaurine. · 2020 · https://pubmed.ncbi.nlm.nih.gov/32156684/ · DOI 10.1124/dmd.119.089995
Taurine: synthesis, transport, mitochondrial decoding and nutrient interactions (2026-09-19) · lines 73–79
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human FMO1 enzyme assays. · source_derived_draft · unverified_draft
## taurine-fmo1-oxidation FMO1 completes the hypotaurine-to-taurine step. Recombinant human FMO1 catalyzed oxygenation of hypotaurine to taurine in vitro. Model: Human FMO1 enzyme assays. Limitations: This identifies an enzyme activity; it does not establish FMO1 as the only possible route in every tissue. Evidence access: Primary abstract Flavin-Containing Monooxygenase 1 Catalyzes the Production of Taurine from Hypotaurine. · 2020 · https://pubmed.ncbi.nlm.nih.gov/32156684/ · DOI 10.1124/dmd.119.089995
Complete structured claim and evidenceFMO1 also oxidized TMA in the comparison, with FMO3 showing about tenfold higher specific activity.
Experimental context and source evidence
- evidence_span
- {"source_cache": "artifacts/choline-research/23312283.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e7c2641ac478a43513c49a68d2ba21e40aa909b32269e91d106072a9028febae", "start_char": 0, "end_char": 1052, "text_sha256": "e7c2641ac478a43513c49a68d2ba21e40aa909b32269e91d106072a9028febae"}
- experimental_model
- Recombinant FMO comparison, mouse manipulation and human expression analyses
- exposure
- FMO1/FMO3 enzyme assays; mouse Fmo3 overexpression and silencing
- limitations
- Enzyme activity, circulating TMAO and clinical disease are different endpoints. Sex regulation is not assigned universally across species.
- nutrient_topic
- Choline research collection; topical membership is not evidence of a direct dietary effect. · Choline
- organism
- Human recombinant FMO1 assay
- plain_language
- The related enzymes differed quantitatively in this preparation.
- primary_references
- [choline-p23312283] Trimethylamine-N-oxide, a metabolite associated with atherosclerosis, exhibits complex genetic and dietary regulation. (2013). https://pubmed.ncbi.nlm.nih.gov/23312283/ DOI: 10.1016/j.cmet.2012.12.011
- tissue_or_cell_type
- Hepatic TMA oxidation
Choline: metabolism, signaling and nutrient connections (2026-09-17) · lines 1127–1138
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant FMO comparison, mouse manipulation and human expression analyses · source_derived_draft · unverified_draft
### choline-fmo1-tmao FMO1 also oxidized TMA in the comparison, with FMO3 showing about tenfold higher specific activity. Condition category: normal nutrient_topic: Choline research collection; topical membership is not evidence of a direct dietary effect. plain_language: The related enzymes differed quantitatively in this preparation. organism: Human recombinant FMO1 assay tissue_or_cell_type: Hepatic TMA oxidation experimental_model: Recombinant FMO comparison, mouse manipulation and human expression analyses limitations: Enzyme activity, circulating TMAO and clinical disease are different endpoints. Sex regulation is not assigned universally across species. exposure: FMO1/FMO3 enzyme assays; mouse Fmo3 overexpression and silencing evidence_span: {"source_cache": "artifacts/choline-research/23312283.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e7c2641ac478a43513c49a68d2ba21e40aa909b32269e91d106072a9028febae", "start_char": 0, "end_char": 1052, "text_sha256": "e7c2641ac478a43513c49a68d2ba21e40aa909b32269e91d106072a9028febae"} [choline-p23312283] Trimethylamine-N-oxide, a metabolite associated with atherosclerosis, exhibits complex genetic and dietary regulation. (2013). https://pubmed.ncbi.nlm.nih.gov/23312283/ DOI: 10.1016/j.cmet.2012.12.011
Complete structured claim and evidence
What acts on it
Human FMO1 converted hypotaurine to taurine with either NADPH or NADH as the reducing cofactor in the reported assays.
Experimental context and source evidence
- evidence_access
- Primary abstract
- experimental_model
- Recombinant human FMO1 biochemistry.
- limitations
- NAD(P)H availability, FMO1 abundance and substrate availability are separate variables; no niacin repletion effect was tested.
- nutrient_topic
- Taurine collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Taurine
- plain_language
- Niacin-derived electron carriers support this synthetic reaction.
- primary_references
- Flavin-Containing Monooxygenase 1 Catalyzes the Production of Taurine from Hypotaurine. · 2020 · https://pubmed.ncbi.nlm.nih.gov/32156684/ · DOI 10.1124/dmd.119.089995
Taurine: synthesis, transport, mitochondrial decoding and nutrient interactions (2026-09-19) · lines 81–87
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Recombinant human FMO1 biochemistry. · source_derived_draft · unverified_draft
## taurine-fmo1-reducing-cofactors Niacin-derived electron carriers support this synthetic reaction. Human FMO1 converted hypotaurine to taurine with either NADPH or NADH as the reducing cofactor in the reported assays. Model: Recombinant human FMO1 biochemistry. Limitations: NAD(P)H availability, FMO1 abundance and substrate availability are separate variables; no niacin repletion effect was tested. Evidence access: Primary abstract Flavin-Containing Monooxygenase 1 Catalyzes the Production of Taurine from Hypotaurine. · 2020 · https://pubmed.ncbi.nlm.nih.gov/32156684/ · DOI 10.1124/dmd.119.089995
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.