Component

3-prime-Phosphoadenosine-5-prime-phosphosulfate / PAPS

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

5 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

Where it participates (unsigned role)

  1. Recombinant human SULT1A1*2 converted indoxyl to indoxyl sulfate using PAPS; apparent indoxyl Km was 5.6 ± 1.8 micromolar.

    Human sulfotransferase 1A1 / SULT1A1 → Indoxyl sulfate source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human recombinant allozyme and liver cytosol kinetic comparison.
    limitations
    Sulfation does not necessarily make a retained metabolite harmless; no inference that sulfur intake controls clinical toxicity.
    nutrient_topic
    Tryptophan collection; molecular form, preparation, species, exposure and manipulation remain explicit. · L-Tryptophan
    plain_language
    A human sulfation enzyme adds a sulfur-containing group to the metabolite.
    primary_references
    Sulfation of indoxyl by human and rat aryl (phenol) sulfotransferases to form indoxyl sulfate. · 2002 · https://pubmed.ncbi.nlm.nih.gov/12064372/ · DOI 10.1007/BF03190428

    Tryptophan: transport, protein synthesis, neuroactive metabolites, NAD and microbial pathways (2026-09-19) · lines 594–600

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human recombinant allozyme and liver cytosol kinetic comparison. · source_derived_draft · unverified_draft

    ## tryptophan-indoxyl-sulfation A human sulfation enzyme adds a sulfur-containing group to the metabolite. Recombinant human SULT1A1*2 converted indoxyl to indoxyl sulfate using PAPS; apparent indoxyl Km was 5.6 ± 1.8 micromolar. Model: Human recombinant allozyme and liver cytosol kinetic comparison. Limitations: Sulfation does not necessarily make a retained metabolite harmless; no inference that sulfur intake controls clinical toxicity. Evidence access: Primary abstract Sulfation of indoxyl by human and rat aryl (phenol) sulfotransferases to form indoxyl sulfate. · 2002 · https://pubmed.ncbi.nlm.nih.gov/12064372/ · DOI 10.1007/BF03190428
    Complete structured claim and evidence

  2. After 30 mg/kg intravenous fisetin in rats, plasma AUC ratios for free fisetin, glucuronides and sulfates were approximately 1:6:21.

    Fisetin → Fisetin sulfates, unresolved positional pool source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Male Sprague-Dawley rats; phase-II analytical pools.
    limitations
    No particular human SULT or UGT isoform is established by this result.
    nutrient_topic
    Fisetin collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Fisetin
    plain_language
    Most measured circulating material was conjugated.
    primary_references
    Pharmacokinetics and Biliary Excretion of Fisetin in Rats. · 2018 · https://pubmed.ncbi.nlm.nih.gov/29862816/ · DOI 10.1021/acs.jafc.8b00917

    Fisetin: metabolism, cell-state responses and cross-nutrient mechanisms (2026-09-19) · lines 56–62

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Male Sprague-Dawley rats; phase-II analytical pools. · source_derived_draft · unverified_draft

    ## fisetin-rat-conjugate-dominance Most measured circulating material was conjugated. After 30 mg/kg intravenous fisetin in rats, plasma AUC ratios for free fisetin, glucuronides and sulfates were approximately 1:6:21. Model: Male Sprague-Dawley rats; phase-II analytical pools. Limitations: No particular human SULT or UGT isoform is established by this result. Evidence access: Primary abstract Pharmacokinetics and Biliary Excretion of Fisetin in Rats. · 2018 · https://pubmed.ncbi.nlm.nih.gov/29862816/ · DOI 10.1021/acs.jafc.8b00917
    Complete structured claim and evidence

  3. Cloned rat RnPIP hydrolyzed PAP and Ins(1,4)P2 in magnesium-dependent reactions.

    Rat bisphosphate nucleotidase 1 / RnPIP → 3-prime-Phosphoadenosine-5-prime-phosphate / PAP source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Cloned rat enzyme; biochemical substrate assays.
    limitations
    The paper proposes consequences for sulfotransferases/RNA processing; those downstream effects were not all tested.
    nutrient_topic
    Lithium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Lithium
    plain_language
    Clearing a sulfur-pathway by-product uses another metal-dependent enzyme.
    primary_references
    A novel mammalian lithium-sensitive enzyme with a dual enzymatic activity, 3'-phosphoadenosine 5'-phosphate phosphatase and inositol-polyphosphate 1-phosphatase. · 1999 · https://pubmed.ncbi.nlm.nih.gov/10347153/ · DOI 10.1074/jbc.274.23.16034

    Lithium: metal-sensitive enzymes, transport and cross-nutrient mechanisms (2026-09-19) · lines 112–118

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Cloned rat enzyme; biochemical substrate assays. · source_derived_draft · unverified_draft

    ## lithium-bpnt1-substrate Clearing a sulfur-pathway by-product uses another metal-dependent enzyme. Cloned rat RnPIP hydrolyzed PAP and Ins(1,4)P2 in magnesium-dependent reactions. Model: Cloned rat enzyme; biochemical substrate assays. Limitations: The paper proposes consequences for sulfotransferases/RNA processing; those downstream effects were not all tested. Evidence access: Primary abstract A novel mammalian lithium-sensitive enzyme with a dual enzymatic activity, 3'-phosphoadenosine 5'-phosphate phosphatase and inositol-polyphosphate 1-phosphatase. · 1999 · https://pubmed.ncbi.nlm.nih.gov/10347153/ · DOI 10.1074/jbc.274.23.16034
    Complete structured claim and evidence

  4. Wild-type Bpnt2 restored GAG sulfation in knockout fibroblasts; catalytic-dead D108A did not.

    Mouse Golgi bisphosphate nucleotidase 2 / Bpnt2 → Mouse fibroblast glycosaminoglycan sulfation source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary full text
    experimental_model
    Mouse embryonic fibroblast pellets; complementation and sulfation assays.
    limitations
    Sulfation depends on compartment and substrate; not a universal human sulfur requirement.
    nutrient_topic
    Lithium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Lithium
    plain_language
    The enzyme must work, not merely be present.
    primary_references
    Sulfation of glycosaminoglycans depends on the catalytic activity of lithium-inhibited phosphatase BPNT2 in vitro. · 2021 · https://pubmed.ncbi.nlm.nih.gov/34634304/ · DOI 10.1016/j.jbc.2021.101293
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Lithium: metal-sensitive enzymes, transport and cross-nutrient mechanisms (2026-09-19) · lines 152–158

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Mouse embryonic fibroblast pellets; complementation and sulfation assays. · source_derived_draft · unverified_draft

    ## lithium-bpnt2-catalysis The enzyme must work, not merely be present. Wild-type Bpnt2 restored GAG sulfation in knockout fibroblasts; catalytic-dead D108A did not. Model: Mouse embryonic fibroblast pellets; complementation and sulfation assays. Limitations: Sulfation depends on compartment and substrate; not a universal human sulfur requirement. Evidence access: Primary full text Sulfation of glycosaminoglycans depends on the catalytic activity of lithium-inhibited phosphatase BPNT2 in vitro. · 2021 · https://pubmed.ncbi.nlm.nih.gov/34634304/ · DOI 10.1016/j.jbc.2021.101293
    Complete structured claim and evidence

  5. LiCl reduced intracellular and secreted GAG sulfation in wild-type mouse fibroblasts, with no further reduction after Bpnt2 knockout.

    Lithium ion (Li+) → Mouse fibroblast glycosaminoglycan sulfation source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text
    experimental_model
    Mouse embryonic fibroblasts; 10 mM LiCl versus matched NaCl.
    limitations
    High experimental exposure; knockout occlusion supports a pathway but does not prove clinical cartilage damage.
    nutrient_topic
    Lithium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Lithium
    plain_language
    The lithium response depended on this Golgi enzyme.
    primary_references
    Sulfation of glycosaminoglycans depends on the catalytic activity of lithium-inhibited phosphatase BPNT2 in vitro. · 2021 · https://pubmed.ncbi.nlm.nih.gov/34634304/ · DOI 10.1016/j.jbc.2021.101293

    Lithium: metal-sensitive enzymes, transport and cross-nutrient mechanisms (2026-09-19) · lines 160–166

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Mouse embryonic fibroblasts; 10 mM LiCl versus matched NaCl. · source_derived_draft · unverified_draft

    ## lithium-bpnt2-lithium-gag The lithium response depended on this Golgi enzyme. LiCl reduced intracellular and secreted GAG sulfation in wild-type mouse fibroblasts, with no further reduction after Bpnt2 knockout. Model: Mouse embryonic fibroblasts; 10 mM LiCl versus matched NaCl. Limitations: High experimental exposure; knockout occlusion supports a pathway but does not prove clinical cartilage damage. Evidence access: Primary full text Sulfation of glycosaminoglycans depends on the catalytic activity of lithium-inhibited phosphatase BPNT2 in vitro. · 2021 · https://pubmed.ncbi.nlm.nih.gov/34634304/ · DOI 10.1016/j.jbc.2021.101293
    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