Component

Putrescine

Study-scoped entity; inspect species, exposure and experimental limitations on each claim.

19 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. Putrescine and idazoxan inhibited rat brain mitochondrial agmatine uptake despite being ineffective in the compared liver mitochondrial preparation.

    Putrescine → Rat brain mitochondrial agmatine uptake source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Isolated rat brain versus liver mitochondria.
    limitations
    A pharmacological pattern does not establish a particular I2 receptor protein as the transporter.
    nutrient_topic
    Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
    plain_language
    Compartment and organ identity change which interactions occur.
    primary_references
    Agmatine transport in brain mitochondria: a different mechanism from that in liver mitochondria. · 2010 · https://pubmed.ncbi.nlm.nih.gov/19997762/ · DOI 10.1007/s00726-009-0401-1

    Agmatine Sulfate: transport, guanidino metabolism, ion channels and cross-nutrient mechanisms (2026-09-20) · lines 380–386

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Isolated rat brain versus liver mitochondria. · source_derived_draft · unverified_draft

    ## agmatine-sulfate-brain-mito-transport Compartment and organ identity change which interactions occur. Putrescine and idazoxan inhibited rat brain mitochondrial agmatine uptake despite being ineffective in the compared liver mitochondrial preparation. Model: Isolated rat brain versus liver mitochondria. Limitations: A pharmacological pattern does not establish a particular I2 receptor protein as the transporter. Evidence access: Primary abstract Agmatine transport in brain mitochondria: a different mechanism from that in liver mitochondria. · 2010 · https://pubmed.ncbi.nlm.nih.gov/19997762/ · DOI 10.1007/s00726-009-0401-1
    Complete structured claim and evidence

  2. Putrescine had little NMDA-blocking effect compared with agmatine or arcaine in the same experiments.

    Putrescine → Rat NMDA-type glutamate receptors, subunits unresolved source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Rat neuron comparison of guanidine-containing and diamine compounds.
    limitations
    The result supports structural specificity; it does not measure metabolic conversion during recording.
    nutrient_topic
    Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
    plain_language
    Converting agmatine to a related amine can change channel activity.
    primary_references
    Agmatine selectively blocks the N-methyl-D-aspartate subclass of glutamate receptor channels in rat hippocampal neurons. · 1999 · https://pubmed.ncbi.nlm.nih.gov/9918557/

    Agmatine Sulfate: transport, guanidino metabolism, ion channels and cross-nutrient mechanisms (2026-09-20) · lines 276–282

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Rat neuron comparison of guanidine-containing and diamine compounds. · source_derived_draft · unverified_draft

    ## agmatine-sulfate-putrescine-nmda Converting agmatine to a related amine can change channel activity. Putrescine had little NMDA-blocking effect compared with agmatine or arcaine in the same experiments. Model: Rat neuron comparison of guanidine-containing and diamine compounds. Limitations: The result supports structural specificity; it does not measure metabolic conversion during recording. Evidence access: Primary abstract Agmatine selectively blocks the N-methyl-D-aspartate subclass of glutamate receptor channels in rat hippocampal neurons. · 1999 · https://pubmed.ncbi.nlm.nih.gov/9918557/
    Complete structured claim and evidence

  3. Putrescine stimulated human AMD1 autoprocessing and decarboxylation through a binding pocket separate from the active site.

    Putrescine → Human S-adenosylmethionine decarboxylase / AMD1 source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human AMD1 structures, binding measurements and targeted mutants.
    limitations
    Feedback demonstrated at enzyme level; not a measured systemic methyl-donor drain.
    nutrient_topic
    L-Arginine collection; tissue, species, dose and formulation distinctions retained. · L-Arginine
    plain_language
    A pathway product helps activate production of the next branch’s donor.
    primary_references
    Structural basis for putrescine activation of human S-adenosylmethionine decarboxylase. · 2008 · https://pubmed.ncbi.nlm.nih.gov/19053272/ · DOI 10.1021/bi801732m

    L-Arginine: transport, metabolic branches, nutrient interactions, availability and discovery questions (2026-09-18) · lines 142–148

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human AMD1 structures, binding measurements and targeted mutants. · source_derived_draft · unverified_draft

    ## arg-amd-feedback A pathway product helps activate production of the next branch’s donor. Putrescine stimulated human AMD1 autoprocessing and decarboxylation through a binding pocket separate from the active site. Model: Human AMD1 structures, binding measurements and targeted mutants. Limitations: Feedback demonstrated at enzyme level; not a measured systemic methyl-donor drain. Evidence access: Primary abstract Structural basis for putrescine activation of human S-adenosylmethionine decarboxylase. · 2008 · https://pubmed.ncbi.nlm.nih.gov/19053272/ · DOI 10.1021/bi801732m
    Complete structured claim and evidence

  4. Human SRM uses putrescine as the amine acceptor for aminopropyl transfer from decarboxylated SAM.

    Putrescine → Spermidine source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human enzyme structural, biochemical and mutagenesis experiments.
    limitations
    This consumes an aminopropyl donor, not a direct methyl transfer from ordinary SAM.
    nutrient_topic
    L-Arginine collection; tissue, species, dose and formulation distinctions retained. · L-Arginine
    plain_language
    Polyamine synthesis combines an ornithine-derived branch with a SAM-derived branch.
    primary_references
    Structure and mechanism of spermidine synthases. · 2007 · https://pubmed.ncbi.nlm.nih.gov/17585781/ · DOI 10.1021/bi602498k

    L-Arginine: transport, metabolic branches, nutrient interactions, availability and discovery questions (2026-09-18) · lines 134–140

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

    ## arg-srm Polyamine synthesis combines an ornithine-derived branch with a SAM-derived branch. Human SRM uses putrescine as the amine acceptor for aminopropyl transfer from decarboxylated SAM. Model: Human enzyme structural, biochemical and mutagenesis experiments. Limitations: This consumes an aminopropyl donor, not a direct methyl transfer from ordinary SAM. Evidence access: Primary abstract Structure and mechanism of spermidine synthases. · 2007 · https://pubmed.ncbi.nlm.nih.gov/17585781/ · DOI 10.1021/bi602498k
    Complete structured claim and evidence

What acts on it

  1. ODC catalyzes conversion of ornithine into putrescine.

    L-Ornithine → Putrescine source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract and indexed primary full-text introduction, PMC1904517
    experimental_model
    Human ODC study; reaction identified in the primary paper introduction.
    limitations
    Reaction identity does not establish net pathway flux after supplementation.
    nutrient_topic
    L-Arginine collection; tissue, species, dose and formulation distinctions retained. · L-Arginine
    plain_language
    This reaction opens the polyamine branch.
    primary_references
    A structural insight into the inhibition of human and Leishmania donovani ornithine decarboxylases by 1-amino-oxy-3-aminopropane. · 2007 · https://pubmed.ncbi.nlm.nih.gov/17407445/ · DOI 10.1042/bj20070188

    L-Arginine: transport, metabolic branches, nutrient interactions, availability and discovery questions (2026-09-18) · lines 110–116

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human ODC study; reaction identified in the primary paper introduction. · source_derived_draft · unverified_draft

    ## arg-odc-reaction This reaction opens the polyamine branch. ODC catalyzes conversion of ornithine into putrescine. Model: Human ODC study; reaction identified in the primary paper introduction. Limitations: Reaction identity does not establish net pathway flux after supplementation. Evidence access: Primary abstract and indexed primary full-text introduction, PMC1904517 A structural insight into the inhibition of human and Leishmania donovani ornithine decarboxylases by 1-amino-oxy-3-aminopropane. · 2007 · https://pubmed.ncbi.nlm.nih.gov/17407445/ · DOI 10.1042/bj20070188
    Complete structured claim and evidence

  2. Tracer carbon appeared in putrescine and proline; arginase inhibition reduced these labeled products.

    L-Arginine → Putrescine source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Full-text results, Figures 2 and 6, Europe PMC PMC5075284; primary abstract.
    experimental_model
    Primary human activated T cells; isotope tracing and functional assays.
    limitations
    Flux is model-specific; not evidence of clinical wound healing.
    nutrient_topic
    L-Arginine collection; tissue, species, dose and formulation distinctions retained. · L-Arginine
    plain_language
    Arginine fed more than the NO pathway.
    primary_references
    L-Arginine Modulates T Cell Metabolism and Enhances Survival and Anti-tumor Activity. · 2016 · https://pubmed.ncbi.nlm.nih.gov/27745970/ · DOI 10.1016/j.cell.2016.09.031

    L-Arginine: transport, metabolic branches, nutrient interactions, availability and discovery questions (2026-09-18) · lines 222–228

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Primary human activated T cells; isotope tracing and functional assays. · source_derived_draft · unverified_draft

    ## arg-tcell-carbon Arginine fed more than the NO pathway. Tracer carbon appeared in putrescine and proline; arginase inhibition reduced these labeled products. Model: Primary human activated T cells; isotope tracing and functional assays. Limitations: Flux is model-specific; not evidence of clinical wound healing. Evidence access: Full-text results, Figures 2 and 6, Europe PMC PMC5075284; primary abstract. L-Arginine Modulates T Cell Metabolism and Enhances Survival and Anti-tumor Activity. · 2016 · https://pubmed.ncbi.nlm.nih.gov/27745970/ · DOI 10.1016/j.cell.2016.09.031
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Agmatine promoted an antizyme-mRNA frameshift producing full-length antizyme; anti-antizyme antibody or antizyme inhibitor suppressed associated inhibitory activity.

    Agmatine → Agmatine-dependent antizyme translational frameshift in the 1998 experiments source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Cell and translation assays; exact construct and cell species not resolved in accessed abstract.
    limitations
    This is not assigned to a human isoform without checking the complete preparation.
    nutrient_topic
    Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
    plain_language
    It can influence production of a regulator of polyamine metabolism.
    primary_references
    Agmatine suppresses proliferation by frameshift induction of antizyme and attenuation of cellular polyamine levels. · 1998 · https://pubmed.ncbi.nlm.nih.gov/9624108/ · DOI 10.1074/jbc.273.25.15313

    Agmatine Sulfate: transport, guanidino metabolism, ion channels and cross-nutrient mechanisms (2026-09-20) · lines 340–346

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Cell and translation assays; exact construct and cell species not resolved in accessed abstract. · source_derived_draft · unverified_draft

    ## agmatine-sulfate-antizyme-frameshift It can influence production of a regulator of polyamine metabolism. Agmatine promoted an antizyme-mRNA frameshift producing full-length antizyme; anti-antizyme antibody or antizyme inhibitor suppressed associated inhibitory activity. Model: Cell and translation assays; exact construct and cell species not resolved in accessed abstract. Limitations: This is not assigned to a human isoform without checking the complete preparation. Evidence access: Primary abstract Agmatine suppresses proliferation by frameshift induction of antizyme and attenuation of cellular polyamine levels. · 1998 · https://pubmed.ncbi.nlm.nih.gov/9624108/ · DOI 10.1074/jbc.273.25.15313
    Complete structured claim and evidence

  2. Difluoromethylornithine-induced polyamine depletion increased agmatine uptake in cultured rat hepatocytes.

    Difluoromethylornithine / eflornithine → Agmatine uptake in polyamine-depleted rat hepatocytes source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary abstract
    experimental_model
    Pharmacological ODC inhibition in rat hepatocyte culture.
    limitations
    This is experimentally induced cellular polyamine depletion, not ordinary dietary agmatine deficiency.
    nutrient_topic
    Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
    plain_language
    A depleted downstream pool can change entry of another compound.
    primary_references
    Transport and metabolism of agmatine in rat hepatocyte cultures. · 2001 · https://pubmed.ncbi.nlm.nih.gov/11179960/ · DOI 10.1046/j.1432-1327.2001.01955.x
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Agmatine Sulfate: transport, guanidino metabolism, ion channels and cross-nutrient mechanisms (2026-09-20) · lines 84–90

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Pharmacological ODC inhibition in rat hepatocyte culture. · source_derived_draft · unverified_draft

    ## agmatine-sulfate-depleted-polyamines A depleted downstream pool can change entry of another compound. Difluoromethylornithine-induced polyamine depletion increased agmatine uptake in cultured rat hepatocytes. Model: Pharmacological ODC inhibition in rat hepatocyte culture. Limitations: This is experimentally induced cellular polyamine depletion, not ordinary dietary agmatine deficiency. Evidence access: Primary abstract Transport and metabolism of agmatine in rat hepatocyte cultures. · 2001 · https://pubmed.ncbi.nlm.nih.gov/11179960/ · DOI 10.1046/j.1432-1327.2001.01955.x
    Complete structured claim and evidence

  3. Agmatine entered rat liver mitochondrial matrix through membrane-potential-dependent transport; putrescine, arginine, ornithine and lysine did not inhibit uptake.

    Rat liver mitochondrial membrane potential → Rat liver mitochondrial agmatine uptake source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Isolated rat liver mitochondria; force-flux and inhibitor analysis.
    limitations
    The proposed transporter was not genetically identified; no single universal agmatine carrier is asserted.
    nutrient_topic
    Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
    plain_language
    Mitochondrial entry has different requirements from plasma-membrane entry.
    primary_references
    Agmatine is transported into liver mitochondria by a specific electrophoretic mechanism. · 2006 · https://pubmed.ncbi.nlm.nih.gov/16509824/ · DOI 10.1042/BJ20060003

    Agmatine Sulfate: transport, guanidino metabolism, ion channels and cross-nutrient mechanisms (2026-09-20) · lines 372–378

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Isolated rat liver mitochondria; force-flux and inhibitor analysis. · source_derived_draft · unverified_draft

    ## agmatine-sulfate-liver-mito-transport Mitochondrial entry has different requirements from plasma-membrane entry. Agmatine entered rat liver mitochondrial matrix through membrane-potential-dependent transport; putrescine, arginine, ornithine and lysine did not inhibit uptake. Model: Isolated rat liver mitochondria; force-flux and inhibitor analysis. Limitations: The proposed transporter was not genetically identified; no single universal agmatine carrier is asserted. Evidence access: Primary abstract Agmatine is transported into liver mitochondria by a specific electrophoretic mechanism. · 2006 · https://pubmed.ncbi.nlm.nih.gov/16509824/ · DOI 10.1042/BJ20060003
    Complete structured claim and evidence

  4. Transformed mouse NIH/3T3 cells took up agmatine through an energy- and membrane-potential-dependent saturable system with apparent Km 2.5 micromolar.

    Mouse transformed NIH/3T3 polyamine transport system → Agmatine source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Mouse transformed fibroblast transport experiments.
    limitations
    The molecular transporter gene was not identified; this system is not automatically OCT2 or MATE1.
    nutrient_topic
    Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
    plain_language
    Different cells can have much higher-affinity uptake than a single recombinant transporter.
    primary_references
    Polyamine transport system mediates agmatine transport in mammalian cells. · 2001 · https://pubmed.ncbi.nlm.nih.gov/11401856/ · DOI 10.1152/ajpcell.2001.281.1.C329
    transport_effect
    raises Cells took up agmatine through an energy- and membrane-potential-dependent saturable system.
    transport_pool
    the expressing cell Cells took up agmatine through an energy- and membrane-potential-dependent saturable system.

    Agmatine Sulfate: transport, guanidino metabolism, ion channels and cross-nutrient mechanisms (2026-09-20) · lines 60–66

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Mouse transformed fibroblast transport experiments. · source_derived_draft · unverified_draft

    ## agmatine-sulfate-polyamine-carrier Different cells can have much higher-affinity uptake than a single recombinant transporter. Transformed mouse NIH/3T3 cells took up agmatine through an energy- and membrane-potential-dependent saturable system with apparent Km 2.5 micromolar. Model: Mouse transformed fibroblast transport experiments. Limitations: The molecular transporter gene was not identified; this system is not automatically OCT2 or MATE1. Evidence access: Primary abstract Polyamine transport system mediates agmatine transport in mammalian cells. · 2001 · https://pubmed.ncbi.nlm.nih.gov/11401856/ · DOI 10.1152/ajpcell.2001.281.1.C329
    Complete structured claim and evidence

  5. Polyamines inhibited MATE1-mediated agmatine transport, whereas L-arginine did not inhibit it in the tested system.

    Polyamine competitor pool in the human MATE1 agmatine assay → Human MATE1-mediated agmatine transport source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human MATE1-expressing HEK293 cells.
    limitations
    The primary abstract groups the polyamine competitors; no individual potency rank is assigned.
    nutrient_topic
    Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
    plain_language
    A shared precursor is not necessarily a transport competitor.
    primary_references
    OCT2 and MATE1 provide bidirectional agmatine transport. · 2011 · https://pubmed.ncbi.nlm.nih.gov/21128598/ · DOI 10.1021/mp100180a

    Agmatine Sulfate: transport, guanidino metabolism, ion channels and cross-nutrient mechanisms (2026-09-20) · lines 52–58

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human MATE1-expressing HEK293 cells. · source_derived_draft · unverified_draft

    ## agmatine-sulfate-polyamine-competition A shared precursor is not necessarily a transport competitor. Polyamines inhibited MATE1-mediated agmatine transport, whereas L-arginine did not inhibit it in the tested system. Model: Human MATE1-expressing HEK293 cells. Limitations: The primary abstract groups the polyamine competitors; no individual potency rank is assigned. Evidence access: Primary abstract OCT2 and MATE1 provide bidirectional agmatine transport. · 2011 · https://pubmed.ncbi.nlm.nih.gov/21128598/ · DOI 10.1021/mp100180a
    Complete structured claim and evidence

  6. Agmatine lowered intracellular polyamines and suppressed transformed-cell proliferation; polyamine supplementation reversed growth suppression.

    Polyamine supplementation pool in the 1998 agmatine experiments → Agmatine-associated growth suppression in the 1998 transformed-cell model source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Transformed-cell supplementation experiment.
    limitations
    The accessed abstract reports polyamine supplementation as a group, not a spermidine-only rescue or cancer therapy.
    nutrient_topic
    Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
    plain_language
    Restoring a downstream pool changed the cellular outcome.
    primary_references
    Agmatine suppresses proliferation by frameshift induction of antizyme and attenuation of cellular polyamine levels. · 1998 · https://pubmed.ncbi.nlm.nih.gov/9624108/ · DOI 10.1074/jbc.273.25.15313

    Agmatine Sulfate: transport, guanidino metabolism, ion channels and cross-nutrient mechanisms (2026-09-20) · lines 348–354

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Transformed-cell supplementation experiment. · source_derived_draft · unverified_draft

    ## agmatine-sulfate-polyamine-rescue Restoring a downstream pool changed the cellular outcome. Agmatine lowered intracellular polyamines and suppressed transformed-cell proliferation; polyamine supplementation reversed growth suppression. Model: Transformed-cell supplementation experiment. Limitations: The accessed abstract reports polyamine supplementation as a group, not a spermidine-only rescue or cancer therapy. Evidence access: Primary abstract Agmatine suppresses proliferation by frameshift induction of antizyme and attenuation of cellular polyamine levels. · 1998 · https://pubmed.ncbi.nlm.nih.gov/9624108/ · DOI 10.1074/jbc.273.25.15313
    Complete structured claim and evidence

  7. Rat ALP catalytic activity required manganese; D217A and specified multi-residue substitutions abolished measured agmatinase activity.

    Mn2+ → Rat brain agmatinase-like protein / ALP experimental preparation source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary abstract
    experimental_model
    Recombinant rat protein, manganese activation and mutagenesis.
    limitations
    Mutations support residue importance but do not by themselves prove every proposed metal-coordination geometry.
    nutrient_topic
    Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
    plain_language
    The metal-dependent catalytic machinery is a separate requirement from substrate supply.
    primary_references
    Insights into the Mn2+ Binding Site in the Agmatinase-Like Protein (ALP): A Critical Enzyme for the Regulation of Agmatine Levels in Mammals. · 2020 · https://pubmed.ncbi.nlm.nih.gov/32531922/ · DOI 10.3390/ijms21114132
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Agmatine Sulfate: transport, guanidino metabolism, ion channels and cross-nutrient mechanisms (2026-09-20) · lines 156–162

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Recombinant rat protein, manganese activation and mutagenesis. · source_derived_draft · unverified_draft

    ## agmatine-sulfate-rat-alp-metal The metal-dependent catalytic machinery is a separate requirement from substrate supply. Rat ALP catalytic activity required manganese; D217A and specified multi-residue substitutions abolished measured agmatinase activity. Model: Recombinant rat protein, manganese activation and mutagenesis. Limitations: Mutations support residue importance but do not by themselves prove every proposed metal-coordination geometry. Evidence access: Primary abstract Insights into the Mn2+ Binding Site in the Agmatinase-Like Protein (ALP): A Critical Enzyme for the Regulation of Agmatine Levels in Mammals. · 2020 · https://pubmed.ncbi.nlm.nih.gov/32531922/ · DOI 10.3390/ijms21114132
    Complete structured claim and evidence

  8. Recombinant rat-brain agmatinase-like protein catalyzed agmatine hydrolysis; its central 210-residue construct retained activity with reduced kcat.

    Rat brain agmatinase-like protein / ALP experimental preparation → Agmatine source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Rat ALP recombinant constructs and enzyme kinetics.
    limitations
    ALP is not interchangeable with the AGMAT gene product; no human oral exposure outcome is shown.
    nutrient_topic
    Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
    plain_language
    A distinct protein preparation can perform the reaction missing from purified human AGMAT.
    primary_references
    Insights into the Mn2+ Binding Site in the Agmatinase-Like Protein (ALP): A Critical Enzyme for the Regulation of Agmatine Levels in Mammals. · 2020 · https://pubmed.ncbi.nlm.nih.gov/32531922/ · DOI 10.3390/ijms21114132

    Agmatine Sulfate: transport, guanidino metabolism, ion channels and cross-nutrient mechanisms (2026-09-20) · lines 148–154

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Rat ALP recombinant constructs and enzyme kinetics. · source_derived_draft · unverified_draft

    ## agmatine-sulfate-rat-alp-reaction A distinct protein preparation can perform the reaction missing from purified human AGMAT. Recombinant rat-brain agmatinase-like protein catalyzed agmatine hydrolysis; its central 210-residue construct retained activity with reduced kcat. Model: Rat ALP recombinant constructs and enzyme kinetics. Limitations: ALP is not interchangeable with the AGMAT gene product; no human oral exposure outcome is shown. Evidence access: Primary abstract Insights into the Mn2+ Binding Site in the Agmatinase-Like Protein (ALP): A Critical Enzyme for the Regulation of Agmatine Levels in Mammals. · 2020 · https://pubmed.ncbi.nlm.nih.gov/32531922/ · DOI 10.3390/ijms21114132
    Complete structured claim and evidence

  9. Rat hepatocytes exhibited high-affinity agmatine uptake with Km 0.03 mM; the system also transported putrescine but not arginine, spermidine or spermine.

    Rat hepatocyte high-affinity agmatine uptake → Agmatine source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Primary rat hepatocyte cultures and radiolabeled substrate.
    limitations
    Different selectivity from other polyamine uptake systems is a context difference, not a universal contradiction.
    nutrient_topic
    Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
    plain_language
    Competition depends on which cell and transport route is being studied.
    primary_references
    Transport and metabolism of agmatine in rat hepatocyte cultures. · 2001 · https://pubmed.ncbi.nlm.nih.gov/11179960/ · DOI 10.1046/j.1432-1327.2001.01955.x
    transport_effect
    raises Hepatocytes showed high-affinity agmatine uptake with a Km of 0.03 mM.
    transport_pool
    the hepatocyte interior Hepatocytes showed high-affinity agmatine uptake with a Km of 0.03 mM.

    Agmatine Sulfate: transport, guanidino metabolism, ion channels and cross-nutrient mechanisms (2026-09-20) · lines 76–82

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Primary rat hepatocyte cultures and radiolabeled substrate. · source_derived_draft · unverified_draft

    ## agmatine-sulfate-rat-liver-uptake Competition depends on which cell and transport route is being studied. Rat hepatocytes exhibited high-affinity agmatine uptake with Km 0.03 mM; the system also transported putrescine but not arginine, spermidine or spermine. Model: Primary rat hepatocyte cultures and radiolabeled substrate. Limitations: Different selectivity from other polyamine uptake systems is a context difference, not a universal contradiction. Evidence access: Primary abstract Transport and metabolism of agmatine in rat hepatocyte cultures. · 2001 · https://pubmed.ncbi.nlm.nih.gov/11179960/ · DOI 10.1046/j.1432-1327.2001.01955.x
    Complete structured claim and evidence

  10. Agmatine present in culture medium competitively inhibited radiolabeled polyamine uptake, increasing apparent Km.

    Agmatine → Rat pulmonary-endothelial polyamine uptake source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Rat pulmonary endothelial transport kinetics.
    limitations
    No universal human polyamine depletion magnitude or clinical supplement interaction is established.
    nutrient_topic
    Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
    plain_language
    Immediate transport competition can coexist with slower regulation of protein expression.
    primary_references
    Regulation of ornithine decarboxylase activity and polyamine transport by agmatine in rat pulmonary artery endothelial cells. · 2001 · https://pubmed.ncbi.nlm.nih.gov/11160620/

    Agmatine Sulfate: transport, guanidino metabolism, ion channels and cross-nutrient mechanisms (2026-09-20) · lines 364–370

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Rat pulmonary endothelial transport kinetics. · source_derived_draft · unverified_draft

    ## agmatine-sulfate-rat-polyamine-competition Immediate transport competition can coexist with slower regulation of protein expression. Agmatine present in culture medium competitively inhibited radiolabeled polyamine uptake, increasing apparent Km. Model: Rat pulmonary endothelial transport kinetics. Limitations: No universal human polyamine depletion magnitude or clinical supplement interaction is established. Evidence access: Primary abstract Regulation of ornithine decarboxylase activity and polyamine transport by agmatine in rat pulmonary artery endothelial cells. · 2001 · https://pubmed.ncbi.nlm.nih.gov/11160620/
    Complete structured claim and evidence

  11. Human AGMAT expression supported growth of polyamine-biosynthesis-deficient yeast in the presence of agmatine despite absent directly measured in vitro agmatinase activity.

    Human AGMAT, guanidino acid hydrolase candidate / historically annotated agmatinase → Yeast polyamine-deficient growth rescue by human AGMAT expression source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Saccharomyces cerevisiae TRY104Δspe1 complementation plus enzyme assays.
    limitations
    Indirect yeast rescue is retained as reported; it is not sufficient to override later direct human substrate-specificity experiments.
    nutrient_topic
    Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
    plain_language
    Growth complementation and direct enzyme catalysis answer different questions.
    primary_references
    Mammalian agmatinases constitute unusual members in the family of Mn2+-dependent ureahydrolases. · 2017 · https://pubmed.ncbi.nlm.nih.gov/27846445/ · DOI 10.1016/j.jinorgbio.2016.11.015

    Agmatine Sulfate: transport, guanidino metabolism, ion channels and cross-nutrient mechanisms (2026-09-20) · lines 164–170

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Saccharomyces cerevisiae TRY104Δspe1 complementation plus enzyme assays. · source_derived_draft · unverified_draft

    ## agmatine-sulfate-yeast-rescue Growth complementation and direct enzyme catalysis answer different questions. Human AGMAT expression supported growth of polyamine-biosynthesis-deficient yeast in the presence of agmatine despite absent directly measured in vitro agmatinase activity. Model: Saccharomyces cerevisiae TRY104Δspe1 complementation plus enzyme assays. Limitations: Indirect yeast rescue is retained as reported; it is not sufficient to override later direct human substrate-specificity experiments. Evidence access: Primary abstract Mammalian agmatinases constitute unusual members in the family of Mn2+-dependent ureahydrolases. · 2017 · https://pubmed.ncbi.nlm.nih.gov/27846445/ · DOI 10.1016/j.jinorgbio.2016.11.015
    Complete structured claim and evidence

  12. Spermidine stimulated OAZ1 +1 frameshifting in engineered yeast; its response lacked the cooperativity seen with putrescine and spermine.

    Spermidine → Saccharomyces cerevisiae Oaz1 antizyme source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text
    experimental_model
    Yeast strains with synthesis/interconversion deletions and reporter modeling.
    limitations
    Do not transfer the quantitative yeast response to human OAZ1.
    nutrient_topic
    Spermidine collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Spermidine
    plain_language
    Polyamine abundance feeds back into synthesis control.
    primary_references
    Translational recoding as a feedback controller: systems approaches reveal polyamine-specific effects on the antizyme ribosomal frameshift. · 2011 · https://pubmed.ncbi.nlm.nih.gov/21303766/ · DOI 10.1093/nar/gkq1349

    Spermidine: biosynthesis, hypusination, transport and cross-nutrient mechanisms (2026-09-19) · lines 478–484

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Yeast strains with synthesis/interconversion deletions and reporter modeling. · source_derived_draft · unverified_draft

    ## spermidine-antizyme-feedback Polyamine abundance feeds back into synthesis control. Spermidine stimulated OAZ1 +1 frameshifting in engineered yeast; its response lacked the cooperativity seen with putrescine and spermine. Model: Yeast strains with synthesis/interconversion deletions and reporter modeling. Limitations: Do not transfer the quantitative yeast response to human OAZ1. Evidence access: Primary full text Translational recoding as a feedback controller: systems approaches reveal polyamine-specific effects on the antizyme ribosomal frameshift. · 2011 · https://pubmed.ncbi.nlm.nih.gov/21303766/ · DOI 10.1093/nar/gkq1349
    Complete structured claim and evidence

  13. Oral 15 mg/day spermidine for five days did not significantly increase plasma spermidine or putrescine versus placebo.

    Spermidine → Human plasma spermidine concentration source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    biomarker_context Imported condition classification; unverified.
    evidence_access
    Primary full text
    experimental_model
    Twelve healthy adults; blinded randomized crossover pharmacokinetic study.
    limitations
    Short study and plasma sampling do not exclude intracellular changes, other regimens or long-term effects.
    nutrient_topic
    Spermidine collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Spermidine
    plain_language
    Swallowing more did not measurably raise this plasma pool.
    primary_references
    High-Dose Spermidine Supplementation Does Not Increase Spermidine Levels in Blood Plasma and Saliva of Healthy Adults: A Randomized Placebo-Controlled Pharmacokinetic and Metabolomic Study. · 2023 · https://pubmed.ncbi.nlm.nih.gov/37111071/ · DOI 10.3390/nu15081852
    trigger_kind
    biomarker_context Imported condition classification; unverified.

    Spermidine: biosynthesis, hypusination, transport and cross-nutrient mechanisms (2026-09-19) · lines 550–556

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Twelve healthy adults; blinded randomized crossover pharmacokinetic study. · source_derived_draft · unverified_draft

    ## spermidine-human-plasma-null Swallowing more did not measurably raise this plasma pool. Oral 15 mg/day spermidine for five days did not significantly increase plasma spermidine or putrescine versus placebo. Model: Twelve healthy adults; blinded randomized crossover pharmacokinetic study. Limitations: Short study and plasma sampling do not exclude intracellular changes, other regimens or long-term effects. Evidence access: Primary full text High-Dose Spermidine Supplementation Does Not Increase Spermidine Levels in Blood Plasma and Saliva of Healthy Adults: A Randomized Placebo-Controlled Pharmacokinetic and Metabolomic Study. · 2023 · https://pubmed.ncbi.nlm.nih.gov/37111071/ · DOI 10.3390/nu15081852
    Complete structured claim and evidence

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