Component

5′-Methylthioadenosine

Study-scoped entity; inspect species, exposure and experimental limitations 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 it acts on

  1. Biochemical methyltransferase profiling identified MTA as a potent selective PRMT5 inhibitor; MTAP-deleted cells had reduced PRMT5 methylation activity.

    5′-Methylthioadenosine → Human protein arginine methyltransferase 5 / PRMT5 source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human cancer-cell and purified-enzyme study.
    limitations
    Selectivity applies to the tested panel and conditions; not all methyltransferases.
    nutrient_topic
    L-Methionine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Methionine
    plain_language
    A recycling product can inhibit another methylation enzyme.
    primary_references
    MTAP Deletions in Cancer Create Vulnerability to Targeting of the MAT2A/PRMT5/RIOK1 Axis. · 2016 · https://pubmed.ncbi.nlm.nih.gov/27068473/ · DOI 10.1016/j.celrep.2016.03.043

    L-Methionine: transport, methylation, sulfur metabolism and cross-nutrient mechanisms (2026-09-19) · lines 292–298

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human cancer-cell and purified-enzyme study. · source_derived_draft · unverified_draft

    ## methionine-mta-prmt5 A recycling product can inhibit another methylation enzyme. Biochemical methyltransferase profiling identified MTA as a potent selective PRMT5 inhibitor; MTAP-deleted cells had reduced PRMT5 methylation activity. Model: Human cancer-cell and purified-enzyme study. Limitations: Selectivity applies to the tested panel and conditions; not all methyltransferases. Evidence access: Primary abstract MTAP Deletions in Cancer Create Vulnerability to Targeting of the MAT2A/PRMT5/RIOK1 Axis. · 2016 · https://pubmed.ncbi.nlm.nih.gov/27068473/ · DOI 10.1016/j.celrep.2016.03.043
    Complete structured claim and evidence

  2. The product-bound SMS structure supplied a mechanistic explanation for inhibition by methylthioadenosine.

    5′-Methylthioadenosine → Human spermine synthase / SMS source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human SMS structural and biochemical study.
    limitations
    Product inhibition is not a measured dietary-arginine effect.
    nutrient_topic
    L-Arginine collection; tissue, species, dose and formulation distinctions retained. · L-Arginine
    plain_language
    A reaction product can slow its own production pathway.
    primary_references
    Crystal structure of human spermine synthase: implications of substrate binding and catalytic mechanism. · 2008 · https://pubmed.ncbi.nlm.nih.gov/18367445/ · DOI 10.1074/jbc.m710323200

    L-Arginine: transport, metabolic branches, nutrient interactions, availability and discovery questions (2026-09-18) · lines 166–172

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

    ## arg-sms-inhibition A reaction product can slow its own production pathway. The product-bound SMS structure supplied a mechanistic explanation for inhibition by methylthioadenosine. Model: Human SMS structural and biochemical study. Limitations: Product inhibition is not a measured dietary-arginine effect. Evidence access: Primary abstract Crystal structure of human spermine synthase: implications of substrate binding and catalytic mechanism. · 2008 · https://pubmed.ncbi.nlm.nih.gov/18367445/ · DOI 10.1074/jbc.m710323200
    Complete structured claim and evidence

What acts on it

  1. MTAP loss caused methylthioadenosine accumulation in the study cancer-cell systems, identifying salvage failure as a change in the intracellular metabolite environment.

    Human methylthioadenosine phosphorylase / MTAP → 5′-Methylthioadenosine source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary abstract
    experimental_model
    Human cancer-cell shRNA/metabolomics and biochemical profiling.
    limitations
    Extracellular stromal clearance and in-vivo exposure can differ from isolated culture.
    nutrient_topic
    L-Methionine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Methionine
    plain_language
    A product of polyamine synthesis must be recycled or removed.
    primary_references
    MTAP Deletions in Cancer Create Vulnerability to Targeting of the MAT2A/PRMT5/RIOK1 Axis. · 2016 · https://pubmed.ncbi.nlm.nih.gov/27068473/ · DOI 10.1016/j.celrep.2016.03.043
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    L-Methionine: transport, methylation, sulfur metabolism and cross-nutrient mechanisms (2026-09-19) · lines 284–290

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human cancer-cell shRNA/metabolomics and biochemical profiling. · source_derived_draft · unverified_draft

    ## methionine-mtap-salvage A product of polyamine synthesis must be recycled or removed. MTAP loss caused methylthioadenosine accumulation in the study cancer-cell systems, identifying salvage failure as a change in the intracellular metabolite environment. Model: Human cancer-cell shRNA/metabolomics and biochemical profiling. Limitations: Extracellular stromal clearance and in-vivo exposure can differ from isolated culture. Evidence access: Primary abstract MTAP Deletions in Cancer Create Vulnerability to Targeting of the MAT2A/PRMT5/RIOK1 Axis. · 2016 · https://pubmed.ncbi.nlm.nih.gov/27068473/ · DOI 10.1016/j.celrep.2016.03.043
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Reduced APIP expression or added MTA increased Salmonella-induced cell death in the human-cell study.

    Human methylthioribulose-1-phosphate dehydratase / APIP → Salmonella-induced caspase-1 cell death in human-cell assays source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary abstract
    experimental_model
    Human genetic association and cellular expression/metabolite experiments.
    limitations
    Cell-death programs and infection context matter; not a dietary immunity claim.
    nutrient_topic
    L-Methionine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Methionine
    plain_language
    A salvage pathway also intersected with inflammatory cell death.
    primary_references
    Functional genetic screen of human diversity reveals that a methionine salvage enzyme regulates inflammatory cell death. · 2012 · https://pubmed.ncbi.nlm.nih.gov/22837397/ · DOI 10.1073/pnas.1206701109
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    L-Methionine: transport, methylation, sulfur metabolism and cross-nutrient mechanisms (2026-09-19) · lines 324–330

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human genetic association and cellular expression/metabolite experiments. · source_derived_draft · unverified_draft

    ## methionine-apip-inflammatory-death A salvage pathway also intersected with inflammatory cell death. Reduced APIP expression or added MTA increased Salmonella-induced cell death in the human-cell study. Model: Human genetic association and cellular expression/metabolite experiments. Limitations: Cell-death programs and infection context matter; not a dietary immunity claim. Evidence access: Primary abstract Functional genetic screen of human diversity reveals that a methionine salvage enzyme regulates inflammatory cell death. · 2012 · https://pubmed.ncbi.nlm.nih.gov/22837397/ · DOI 10.1073/pnas.1206701109
    Complete structured claim and evidence

  2. APIP depletion impaired HeLa growth when methionine was replaced by MTA, supporting its role in the salvage pathway.

    Human methylthioribulose-1-phosphate dehydratase / APIP → Growth of human cells supplied MTA instead of methionine source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary abstract
    experimental_model
    Human HeLa knockdown with supporting microbial reporter assays.
    limitations
    Alternative-substrate culture does not establish the fraction of dietary requirements normally met by salvage.
    nutrient_topic
    L-Methionine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Methionine
    plain_language
    Recycling sulfur back to methionine needs additional enzymes beyond MTAP.
    primary_references
    Functional identification of APIP as human mtnB, a key enzyme in the methionine salvage pathway. · 2012 · https://pubmed.ncbi.nlm.nih.gov/23285211/ · DOI 10.1371/journal.pone.0052877
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    L-Methionine: transport, methylation, sulfur metabolism and cross-nutrient mechanisms (2026-09-19) · lines 308–314

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human HeLa knockdown with supporting microbial reporter assays. · source_derived_draft · unverified_draft

    ## methionine-apip-salvage Recycling sulfur back to methionine needs additional enzymes beyond MTAP. APIP depletion impaired HeLa growth when methionine was replaced by MTA, supporting its role in the salvage pathway. Model: Human HeLa knockdown with supporting microbial reporter assays. Limitations: Alternative-substrate culture does not establish the fraction of dietary requirements normally met by salvage. Evidence access: Primary abstract Functional identification of APIP as human mtnB, a key enzyme in the methionine salvage pathway. · 2012 · https://pubmed.ncbi.nlm.nih.gov/23285211/ · DOI 10.1371/journal.pone.0052877
    Complete structured claim and evidence

  3. Mutation of the predicted zinc-binding site abolished APIP salvage function, whereas three tested potential phosphorylation-site mutations did not.

    Human methylthioribulose-1-phosphate dehydratase / APIP → Putative zinc-binding site of human APIP source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary abstract
    experimental_model
    Human APIP mutant-function study.
    limitations
    Mutating a metal-binding site is not the same experiment as dietary zinc deficiency or zinc rescue.
    nutrient_topic
    L-Methionine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Methionine
    plain_language
    A metal-binding site can be a separate gate in nutrient recycling.
    primary_references
    Functional identification of APIP as human mtnB, a key enzyme in the methionine salvage pathway. · 2012 · https://pubmed.ncbi.nlm.nih.gov/23285211/ · DOI 10.1371/journal.pone.0052877
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    L-Methionine: transport, methylation, sulfur metabolism and cross-nutrient mechanisms (2026-09-19) · lines 316–322

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human APIP mutant-function study. · source_derived_draft · unverified_draft

    ## methionine-apip-zinc-site A metal-binding site can be a separate gate in nutrient recycling. Mutation of the predicted zinc-binding site abolished APIP salvage function, whereas three tested potential phosphorylation-site mutations did not. Model: Human APIP mutant-function study. Limitations: Mutating a metal-binding site is not the same experiment as dietary zinc deficiency or zinc rescue. Evidence access: Primary abstract Functional identification of APIP as human mtnB, a key enzyme in the methionine salvage pathway. · 2012 · https://pubmed.ncbi.nlm.nih.gov/23285211/ · DOI 10.1371/journal.pone.0052877
    Complete structured claim and evidence

  4. MAT2A depletion preferentially reduced growth and PRMT5 methylation activity in MTAP-deleted cells.

    Human methionine adenosyltransferase 2A / MAT2A → Human protein arginine methyltransferase 5 / PRMT5 source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary abstract
    experimental_model
    Human cancer-cell genetic depletion experiments.
    limitations
    This genetic interaction is not proof of efficacy for methionine restriction or a particular drug in patients.
    nutrient_topic
    L-Methionine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Methionine
    plain_language
    Loss of a recycling enzyme can make cells more sensitive to reduced donor synthesis.
    primary_references
    MTAP Deletions in Cancer Create Vulnerability to Targeting of the MAT2A/PRMT5/RIOK1 Axis. · 2016 · https://pubmed.ncbi.nlm.nih.gov/27068473/ · DOI 10.1016/j.celrep.2016.03.043
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    L-Methionine: transport, methylation, sulfur metabolism and cross-nutrient mechanisms (2026-09-19) · lines 300–306

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human cancer-cell genetic depletion experiments. · source_derived_draft · unverified_draft

    ## methionine-mat2a-prmt5-vulnerability Loss of a recycling enzyme can make cells more sensitive to reduced donor synthesis. MAT2A depletion preferentially reduced growth and PRMT5 methylation activity in MTAP-deleted cells. Model: Human cancer-cell genetic depletion experiments. Limitations: This genetic interaction is not proof of efficacy for methionine restriction or a particular drug in patients. Evidence access: Primary abstract MTAP Deletions in Cancer Create Vulnerability to Targeting of the MAT2A/PRMT5/RIOK1 Axis. · 2016 · https://pubmed.ncbi.nlm.nih.gov/27068473/ · DOI 10.1016/j.celrep.2016.03.043
    Complete structured claim and evidence

  5. Human spermine-synthase substrate/product structures and mutagenesis support aminopropyl transfer to spermidine.

    Spermidine → Spermine source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human SMS structures and catalytic assays.
    limitations
    A pathway connection does not mean arginine is always rate limiting.
    nutrient_topic
    L-Arginine collection; tissue, species, dose and formulation distinctions retained. · L-Arginine
    plain_language
    The polyamine pathway extends beyond spermidine.
    primary_references
    Crystal structure of human spermine synthase: implications of substrate binding and catalytic mechanism. · 2008 · https://pubmed.ncbi.nlm.nih.gov/18367445/ · DOI 10.1074/jbc.m710323200

    L-Arginine: transport, metabolic branches, nutrient interactions, availability and discovery questions (2026-09-18) · lines 158–164

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human SMS structures and catalytic assays. · source_derived_draft · unverified_draft

    ## arg-sms The polyamine pathway extends beyond spermidine. Human spermine-synthase substrate/product structures and mutagenesis support aminopropyl transfer to spermidine. Model: Human SMS structures and catalytic assays. Limitations: A pathway connection does not mean arginine is always rate limiting. Evidence access: Primary abstract Crystal structure of human spermine synthase: implications of substrate binding and catalytic mechanism. · 2008 · https://pubmed.ncbi.nlm.nih.gov/18367445/ · DOI 10.1074/jbc.m710323200
    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.

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