Component

Human 2-aminoethanethiol dioxygenase / ADO

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

4 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. 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. Manipulating ADO altered G-protein-coupled calcium signals and MAP-kinase activity in the studied human cells.

    Human 2-aminoethanethiol dioxygenase / ADO → G-protein-coupled calcium and MAPK signals in human ADO experiments source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text
    experimental_model
    Human-cell functional signaling assays.
    limitations
    Not evidence of dietary calcium or cysteine requirements for this response.
    nutrient_topic
    L-Cysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Cysteine
    plain_language
    Protein turnover connected an oxygen-sensing step to signaling outputs.
    primary_references
    Conserved N-terminal cysteine dioxygenases transduce responses to hypoxia in animals and plants. · 2019 · https://pubmed.ncbi.nlm.nih.gov/31273118/ · DOI 10.1126/science.aaw0112

    L-Cysteine: sulfur allocation, redox supply and cross-nutrient mechanisms (2026-09-19) · lines 436–442

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human-cell functional signaling assays. · source_derived_draft · unverified_draft

    ## l-cysteine-ado-calcium-signals Protein turnover connected an oxygen-sensing step to signaling outputs. Manipulating ADO altered G-protein-coupled calcium signals and MAP-kinase activity in the studied human cells. Model: Human-cell functional signaling assays. Limitations: Not evidence of dietary calcium or cysteine requirements for this response. Evidence access: Primary full text Conserved N-terminal cysteine dioxygenases transduce responses to hypoxia in animals and plants. · 2019 · https://pubmed.ncbi.nlm.nih.gov/31273118/ · DOI 10.1126/science.aaw0112
    Complete structured claim and evidence

  3. Human ADO oxidized exposed N-terminal cysteine residues in RGS4/5 peptides to the corresponding sulfinic-acid state using molecular oxygen.

    Human 2-aminoethanethiol dioxygenase / ADO → Protein-incorporated N-terminal cysteine residue source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text
    experimental_model
    Human ADO biochemistry, peptide substrates and human-cell experiments.
    limitations
    This is a protein-residue reaction, not evidence that ADO is the ordinary free-cysteine catabolic enzyme.
    nutrient_topic
    L-Cysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Cysteine
    plain_language
    A cysteine already built into a protein can serve as part of an oxygen-sensitive degradation signal.
    primary_references
    Conserved N-terminal cysteine dioxygenases transduce responses to hypoxia in animals and plants. · 2019 · https://pubmed.ncbi.nlm.nih.gov/31273118/ · DOI 10.1126/science.aaw0112

    L-Cysteine: sulfur allocation, redox supply and cross-nutrient mechanisms (2026-09-19) · lines 420–426

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human ADO biochemistry, peptide substrates and human-cell experiments. · source_derived_draft · unverified_draft

    ## l-cysteine-ado-nterminal-oxidation A cysteine already built into a protein can serve as part of an oxygen-sensitive degradation signal. Human ADO oxidized exposed N-terminal cysteine residues in RGS4/5 peptides to the corresponding sulfinic-acid state using molecular oxygen. Model: Human ADO biochemistry, peptide substrates and human-cell experiments. Limitations: This is a protein-residue reaction, not evidence that ADO is the ordinary free-cysteine catabolic enzyme. Evidence access: Primary full text Conserved N-terminal cysteine dioxygenases transduce responses to hypoxia in animals and plants. · 2019 · https://pubmed.ncbi.nlm.nih.gov/31273118/ · DOI 10.1126/science.aaw0112
    Complete structured claim and evidence

  4. ADO-dependent N-terminal cysteine oxidation regulated RGS4/5 stability through the N-degron pathway in human cells.

    Human 2-aminoethanethiol dioxygenase / ADO → Human regulator of G-protein signaling 4 / RGS4 source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text
    experimental_model
    Human-cell ADO and oxygen perturbations with N-degron readouts.
    limitations
    The downstream pathway requires additional machinery; dietary cysteine effects were not tested.
    nutrient_topic
    L-Cysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Cysteine
    plain_language
    Oxidation can mark a signaling regulator for degradation rather than merely damage it.
    primary_references
    Conserved N-terminal cysteine dioxygenases transduce responses to hypoxia in animals and plants. · 2019 · https://pubmed.ncbi.nlm.nih.gov/31273118/ · DOI 10.1126/science.aaw0112

    L-Cysteine: sulfur allocation, redox supply and cross-nutrient mechanisms (2026-09-19) · lines 428–434

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human-cell ADO and oxygen perturbations with N-degron readouts. · source_derived_draft · unverified_draft

    ## l-cysteine-ado-protein-stability Oxidation can mark a signaling regulator for degradation rather than merely damage it. ADO-dependent N-terminal cysteine oxidation regulated RGS4/5 stability through the N-degron pathway in human cells. Model: Human-cell ADO and oxygen perturbations with N-degron readouts. Limitations: The downstream pathway requires additional machinery; dietary cysteine effects were not tested. Evidence access: Primary full text Conserved N-terminal cysteine dioxygenases transduce responses to hypoxia in animals and plants. · 2019 · https://pubmed.ncbi.nlm.nih.gov/31273118/ · DOI 10.1126/science.aaw0112
    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