Component

Hypotaurine

Context-specific entity; species, compartment and exposure are stated on each claim.

8 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 acts on it

  1. RNA-mediated reduction of endogenous human ADO in HepG2/C3A cells decreased hypotaurine production from cysteamine.

    Human 2-aminoethanethiol dioxygenase / ADO → Hypotaurine source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human liver-derived cultured cells.
    limitations
    Cysteamine can arise through CoA breakdown; this experiment does not show that B5 supplementation raises taurine.
    nutrient_topic
    Taurine collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Taurine
    plain_language
    Human-cell gene silencing supports the cysteamine pathway.
    primary_references
    Discovery and characterization of a second mammalian thiol dioxygenase, cysteamine dioxygenase. · 2007 · https://pubmed.ncbi.nlm.nih.gov/17581819/ · DOI 10.1074/jbc.M703089200

    Taurine: synthesis, transport, mitochondrial decoding and nutrient interactions (2026-09-19) · lines 65–71

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human liver-derived cultured cells. · source_derived_draft · unverified_draft

    ## taurine-ado-human-knockdown Human-cell gene silencing supports the cysteamine pathway. RNA-mediated reduction of endogenous human ADO in HepG2/C3A cells decreased hypotaurine production from cysteamine. Model: Human liver-derived cultured cells. Limitations: Cysteamine can arise through CoA breakdown; this experiment does not show that B5 supplementation raises taurine. Evidence access: Primary abstract Discovery and characterization of a second mammalian thiol dioxygenase, cysteamine dioxygenase. · 2007 · https://pubmed.ncbi.nlm.nih.gov/17581819/ · DOI 10.1074/jbc.M703089200
    Complete structured claim and evidence

  2. Recombinant mouse Ado oxidized cysteamine to hypotaurine but did not oxidize cysteine in the tested assay.

    Mouse cysteamine dioxygenase / Ado → Hypotaurine source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Purified recombinant murine protein.
    limitations
    Do not assign the mouse enzyme kinetics directly to human ADO.
    nutrient_topic
    Taurine collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Taurine
    plain_language
    A separate enzyme provides a route from cysteamine.
    primary_references
    Discovery and characterization of a second mammalian thiol dioxygenase, cysteamine dioxygenase. · 2007 · https://pubmed.ncbi.nlm.nih.gov/17581819/ · DOI 10.1074/jbc.M703089200

    Taurine: synthesis, transport, mitochondrial decoding and nutrient interactions (2026-09-19) · lines 57–63

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Purified recombinant murine protein. · source_derived_draft · unverified_draft

    ## taurine-ado-mouse-enzyme A separate enzyme provides a route from cysteamine. Recombinant mouse Ado oxidized cysteamine to hypotaurine but did not oxidize cysteine in the tested assay. Model: Purified recombinant murine protein. Limitations: Do not assign the mouse enzyme kinetics directly to human ADO. Evidence access: Primary abstract Discovery and characterization of a second mammalian thiol dioxygenase, cysteamine dioxygenase. · 2007 · https://pubmed.ncbi.nlm.nih.gov/17581819/ · DOI 10.1074/jbc.M703089200
    Complete structured claim and evidence

  3. Purified human CSAD decarboxylated L-cysteine sulfinic acid to hypotaurine in PLP-containing enzyme assays.

    Human cysteine sulfinic acid decarboxylase / CSAD → Hypotaurine source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text, introduction and enzyme-assay results
    experimental_model
    Recombinant human enzyme; substrate kinetics and circular-dichroism assays.
    limitations
    Hypotaurine still needs oxidation to become taurine; this is not a human supplementation experiment.
    nutrient_topic
    Taurine collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Taurine
    plain_language
    Vitamin B6-dependent CSAD performs a step between cysteine and taurine.
    primary_references
    A Novel, Easy Assay Method for Human Cysteine Sulfinic Acid Decarboxylase. · 2021 · https://pubmed.ncbi.nlm.nih.gov/34068845/ · DOI 10.3390/life11050438

    Taurine: synthesis, transport, mitochondrial decoding and nutrient interactions (2026-09-19) · lines 33–39

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Recombinant human enzyme; substrate kinetics and circular-dichroism assays. · source_derived_draft · unverified_draft

    ## taurine-csad-cysteinesulfinate Vitamin B6-dependent CSAD performs a step between cysteine and taurine. Purified human CSAD decarboxylated L-cysteine sulfinic acid to hypotaurine in PLP-containing enzyme assays. Model: Recombinant human enzyme; substrate kinetics and circular-dichroism assays. Limitations: Hypotaurine still needs oxidation to become taurine; this is not a human supplementation experiment. Evidence access: Primary full text, introduction and enzyme-assay results A Novel, Easy Assay Method for Human Cysteine Sulfinic Acid Decarboxylase. · 2021 · https://pubmed.ncbi.nlm.nih.gov/34068845/ · DOI 10.3390/life11050438
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. The purified human CSAD characterized in this study was a PLP-dependent enzyme, linking its decarboxylation chemistry to the active cofactor form of vitamin B6.

    PLP → Human cysteine sulfinic acid decarboxylase / CSAD source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text, enzyme characterization
    experimental_model
    Human recombinant CSAD biochemical characterization.
    limitations
    Cofactor dependence does not establish that extra B6 increases taurine in a replete person.
    nutrient_topic
    Taurine collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Taurine
    plain_language
    CSAD needs the active B6 cofactor, not just its cysteine-derived substrate.
    primary_references
    A Novel, Easy Assay Method for Human Cysteine Sulfinic Acid Decarboxylase. · 2021 · https://pubmed.ncbi.nlm.nih.gov/34068845/ · DOI 10.3390/life11050438

    Taurine: synthesis, transport, mitochondrial decoding and nutrient interactions (2026-09-19) · lines 41–47

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human recombinant CSAD biochemical characterization. · source_derived_draft · unverified_draft

    ## taurine-csad-plp CSAD needs the active B6 cofactor, not just its cysteine-derived substrate. The purified human CSAD characterized in this study was a PLP-dependent enzyme, linking its decarboxylation chemistry to the active cofactor form of vitamin B6. Model: Human recombinant CSAD biochemical characterization. Limitations: Cofactor dependence does not establish that extra B6 increases taurine in a replete person. Evidence access: Primary full text, enzyme characterization A Novel, Easy Assay Method for Human Cysteine Sulfinic Acid Decarboxylase. · 2021 · https://pubmed.ncbi.nlm.nih.gov/34068845/ · DOI 10.3390/life11050438
    Complete structured claim and evidence

  2. Fmo1-null mice accumulated urinary hypotaurine and had less urinary taurine than wild-type mice.

    Mouse flavin-containing monooxygenase 1 / Fmo1 → Urinary hypotaurine and taurine in Fmo1-null mice source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary abstract
    experimental_model
    Mouse knockout; urinary proton NMR metabolomics.
    limitations
    Urine metabolites do not directly measure every tissue pool or prove human dietary deficiency.
    nutrient_topic
    Taurine collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Taurine
    plain_language
    Disabling the final enzyme changed the precursor/product pattern.
    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
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Taurine: synthesis, transport, mitochondrial decoding and nutrient interactions (2026-09-19) · lines 89–95

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Mouse knockout; urinary proton NMR metabolomics. · source_derived_draft · unverified_draft

    ## taurine-fmo1-deletion Disabling the final enzyme changed the precursor/product pattern. Fmo1-null mice accumulated urinary hypotaurine and had less urinary taurine than wild-type mice. Model: Mouse knockout; urinary proton NMR metabolomics. Limitations: Urine metabolites do not directly measure every tissue pool or prove human dietary deficiency. 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

  3. Recombinant human FMO1 catalyzed oxygenation of hypotaurine to taurine in vitro.

    Human flavin-containing monooxygenase 1 / FMO1 → Taurine source_derived_draftungraded
    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 evidence

  4. Human FMO1 converted hypotaurine to taurine with either NADPH or NADH as the reducing cofactor in the reported assays.

    NADPH → Human flavin-containing monooxygenase 1 / FMO1 source_derived_draftungraded
    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

  5. Liver-specific Cdo1 deletion increased extrahepatic CDO abundance and hypotaurine; mice maintained taurine, glutathione and sulfate despite a taurine-free diet.

    Mouse cysteine dioxygenase / Cdo1 → Extrahepatic compensation for hepatic Cdo1 loss in mice source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Conditional mouse liver knockout; kidney, adipose and pancreatic measurements.
    limitations
    This tissue-restricted deletion differs from complete pathway loss and from human deficiency.
    nutrient_topic
    Taurine collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Taurine
    plain_language
    Other tissues compensated when liver synthesis was impaired.
    primary_references
    Extrahepatic tissues compensate for loss of hepatic taurine synthesis in mice with liver-specific knockout of cysteine dioxygenase. · 2012 · https://pubmed.ncbi.nlm.nih.gov/22414809/ · DOI 10.1152/ajpendo.00589.2011

    Taurine: synthesis, transport, mitochondrial decoding and nutrient interactions (2026-09-19) · lines 97–103

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Conditional mouse liver knockout; kidney, adipose and pancreatic measurements. · source_derived_draft · unverified_draft

    ## taurine-hepatic-compensation Other tissues compensated when liver synthesis was impaired. Liver-specific Cdo1 deletion increased extrahepatic CDO abundance and hypotaurine; mice maintained taurine, glutathione and sulfate despite a taurine-free diet. Model: Conditional mouse liver knockout; kidney, adipose and pancreatic measurements. Limitations: This tissue-restricted deletion differs from complete pathway loss and from human deficiency. Evidence access: Primary abstract Extrahepatic tissues compensate for loss of hepatic taurine synthesis in mice with liver-specific knockout of cysteine dioxygenase. · 2012 · https://pubmed.ncbi.nlm.nih.gov/22414809/ · DOI 10.1152/ajpendo.00589.2011
    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