Component

Human flavin-containing monooxygenase 3

Human flavin-containing monooxygenase 3. Species, exposure and limitations are retained in each linked claim.

2 recorded relationships. Experimental role, claim status and evidence remain attached to each record.

Read recorded mechanisms Open recursive mind map

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.

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.

Recorded relationships

What it acts on

  1. FMO3 played a major role in olanzapine N-oxide formation.

    Human flavin-containing monooxygenase 3 → Olanzapine N-oxide source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/dim-research/26329789.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1f2f35be434034ef4788653d084a6b184b1b5a109d445591c4fd0fc94b36e543", "start_char": 0, "end_char": 1657, "text_sha256": "1f2f35be434034ef4788653d084a6b184b1b5a109d445591c4fd0fc94b36e543"}
    experimental_model
    Human liver microsomes and recombinant enzyme phenotyping
    exposure
    Metabolite-specific assays including albumin effects
    limitations
    In-vitro relative contributions; no DIM coadministration. Multiple routes limit prediction from CYP1A2 alone.
    nutrient_topic
    Diindolylmethane (DIM) research collection; topical membership is not evidence of a direct dietary effect. · 3,3'-Diindolylmethane / DIM
    organism
    Human CYP, FMO and UGT enzymes
    plain_language
    This independently identified route also contributes to olanzapine handling.
    primary_references
    [dim-p26329789] In Vitro Characterization of the Human Liver Microsomal Kinetics and Reaction Phenotyping of Olanzapine Metabolism. (2015). https://pubmed.ncbi.nlm.nih.gov/26329789/ DOI: 10.1124/dmd.115.064790
    tissue_or_cell_type
    Olanzapine oxidation and conjugation

    Diindolylmethane (DIM): formation, receptor signaling, metabolism and drug interactions (2026-09-17) · lines 727–738

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human liver microsomes and recombinant enzyme phenotyping · source_derived_draft · unverified_draft

    ### dim-olanzapine-fmo FMO3 played a major role in olanzapine N-oxide formation. Condition category: normal nutrient_topic: Diindolylmethane (DIM) research collection; topical membership is not evidence of a direct dietary effect. plain_language: This independently identified route also contributes to olanzapine handling. organism: Human CYP, FMO and UGT enzymes tissue_or_cell_type: Olanzapine oxidation and conjugation experimental_model: Human liver microsomes and recombinant enzyme phenotyping limitations: In-vitro relative contributions; no DIM coadministration. Multiple routes limit prediction from CYP1A2 alone. exposure: Metabolite-specific assays including albumin effects evidence_span: {"source_cache": "artifacts/dim-research/26329789.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1f2f35be434034ef4788653d084a6b184b1b5a109d445591c4fd0fc94b36e543", "start_char": 0, "end_char": 1657, "text_sha256": "1f2f35be434034ef4788653d084a6b184b1b5a109d445591c4fd0fc94b36e543"} [dim-p26329789] In Vitro Characterization of the Human Liver Microsomal Kinetics and Reaction Phenotyping of Olanzapine Metabolism. (2015). https://pubmed.ncbi.nlm.nih.gov/26329789/ DOI: 10.1124/dmd.115.064790
    Complete structured claim and evidence

  2. The enzyme comparison demonstrated FMO3-mediated oxidation of TMA to TMAO.

    Human flavin-containing monooxygenase 3 → Trimethylamine / TMA source_derived_draftungraded
    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 FMO3 assay
    plain_language
    The liver-side enzyme processes a product generated by microbial metabolism.
    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 1114–1125

    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-fmo3-tmao The enzyme comparison demonstrated FMO3-mediated oxidation of TMA to TMAO. Condition category: normal nutrient_topic: Choline research collection; topical membership is not evidence of a direct dietary effect. plain_language: The liver-side enzyme processes a product generated by microbial metabolism. organism: Human recombinant FMO3 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

In the sources

Preserved passages that mention this component, quoted exactly. Open one to read it in context.

    This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.

    Evidence, AI assistance and curation standards