Component

4-Guanidinobutyrate

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

What acts on it

  1. Both purified human AGMAT variants hydrolyzed guanidinobutyrate, supporting a guanidino-acid hydrolase function.

    Human AGMAT, guanidino acid hydrolase candidate / historically annotated agmatinase → 4-Guanidinobutyrate source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text; Figures 2 and 3
    experimental_model
    Purified recombinant human R105 and G105 variants.
    limitations
    Measured Km values for the tested guanidino acids exceeded 50 mM; physiological substrate flux remains unresolved.
    nutrient_topic
    Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
    plain_language
    The same protein was active when supplied a different substrate.
    primary_references
    Guanidino acid hydrolysis by the human enzyme annotated as agmatinase. · 2022 · https://pubmed.ncbi.nlm.nih.gov/36543883/ · DOI 10.1038/s41598-022-26655-4

    Agmatine Sulfate: transport, guanidino metabolism, ion channels and cross-nutrient mechanisms (2026-09-20) · lines 124–130

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Purified recombinant human R105 and G105 variants. · source_derived_draft · unverified_draft

    ## agmatine-sulfate-agmat-gba The same protein was active when supplied a different substrate. Both purified human AGMAT variants hydrolyzed guanidinobutyrate, supporting a guanidino-acid hydrolase function. Model: Purified recombinant human R105 and G105 variants. Limitations: Measured Km values for the tested guanidino acids exceeded 50 mM; physiological substrate flux remains unresolved. Evidence access: Primary full text; Figures 2 and 3 Guanidino acid hydrolysis by the human enzyme annotated as agmatinase. · 2022 · https://pubmed.ncbi.nlm.nih.gov/36543883/ · DOI 10.1038/s41598-022-26655-4
    Complete structured claim and evidence

  2. Human GATM used GABA as an amidino acceptor to form guanidinobutyrate in vitro.

    Human glycine amidinotransferase AGAT / GATM → 4-Guanidinobutyrate source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text; Figure 4B
    experimental_model
    Purified human GATM.
    limitations
    Presence of this route does not prove a change in brain inhibitory neurotransmission after agmatine supplementation.
    nutrient_topic
    Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
    plain_language
    The same guanidino metabolite has another possible source besides agmatine oxidation.
    primary_references
    Guanidino acid hydrolysis by the human enzyme annotated as agmatinase. · 2022 · https://pubmed.ncbi.nlm.nih.gov/36543883/ · DOI 10.1038/s41598-022-26655-4

    Agmatine Sulfate: transport, guanidino metabolism, ion channels and cross-nutrient mechanisms (2026-09-20) · lines 196–202

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Purified human GATM. · source_derived_draft · unverified_draft

    ## agmatine-sulfate-gatm-gaba The same guanidino metabolite has another possible source besides agmatine oxidation. Human GATM used GABA as an amidino acceptor to form guanidinobutyrate in vitro. Model: Purified human GATM. Limitations: Presence of this route does not prove a change in brain inhibitory neurotransmission after agmatine supplementation. Evidence access: Primary full text; Figure 4B Guanidino acid hydrolysis by the human enzyme annotated as agmatinase. · 2022 · https://pubmed.ncbi.nlm.nih.gov/36543883/ · DOI 10.1038/s41598-022-26655-4
    Complete structured claim and evidence

  3. About 50% of taken-up radiolabeled agmatine was recovered as 4-guanidinobutyrate in the rat hepatocyte experiment.

    Agmatine → 4-Guanidinobutyrate source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Rat hepatocyte culture; HPLC and mass spectrometry.
    limitations
    The percentage is specific to this experiment and is not a human whole-body metabolic fraction.
    nutrient_topic
    Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
    plain_language
    Oxidation can redirect the molecule away from the polyamine route.
    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

    Agmatine Sulfate: transport, guanidino metabolism, ion channels and cross-nutrient mechanisms (2026-09-20) · lines 92–98

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Rat hepatocyte culture; HPLC and mass spectrometry. · source_derived_draft · unverified_draft

    ## agmatine-sulfate-rat-gba Oxidation can redirect the molecule away from the polyamine route. About 50% of taken-up radiolabeled agmatine was recovered as 4-guanidinobutyrate in the rat hepatocyte experiment. Model: Rat hepatocyte culture; HPLC and mass spectrometry. Limitations: The percentage is specific to this experiment and is not a human whole-body metabolic fraction. 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

Where it participates (unsigned role)

  1. Adding diamine oxidase or inhibiting aldehyde dehydrogenase increased agmatine-associated suppression of inducible NO generation; aldehyde removal or trapping attenuated it.

    4-Guanidinobutyraldehyde / agmatine aldehyde → Agmatine-associated inducible NO suppression in cytokine-stimulated cultures source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Cytokine-stimulated cell preparations; enzyme additions, inhibitors and aldehyde trapping.
    limitations
    The accessed abstract does not fully specify each cell species, dose or enzyme isoform. It supports aldehyde involvement rather than a direct binding target.
    nutrient_topic
    Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
    plain_language
    How a compound is metabolized can change its signaling effect.
    primary_references
    Suppression of inducible nitric oxide generation by agmatine aldehyde: beneficial effects in sepsis. · 2001 · https://pubmed.ncbi.nlm.nih.gov/11473357/ · DOI 10.1002/jcp.1119

    Agmatine Sulfate: transport, guanidino metabolism, ion channels and cross-nutrient mechanisms (2026-09-20) · lines 108–114

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Cytokine-stimulated cell preparations; enzyme additions, inhibitors and aldehyde trapping. · source_derived_draft · unverified_draft

    ## agmatine-sulfate-aldehyde-no How a compound is metabolized can change its signaling effect. Adding diamine oxidase or inhibiting aldehyde dehydrogenase increased agmatine-associated suppression of inducible NO generation; aldehyde removal or trapping attenuated it. Model: Cytokine-stimulated cell preparations; enzyme additions, inhibitors and aldehyde trapping. Limitations: The accessed abstract does not fully specify each cell species, dose or enzyme isoform. It supports aldehyde involvement rather than a direct binding target. Evidence access: Primary abstract Suppression of inducible nitric oxide generation by agmatine aldehyde: beneficial effects in sepsis. · 2001 · https://pubmed.ncbi.nlm.nih.gov/11473357/ · DOI 10.1002/jcp.1119
    Complete structured claim and evidence

  2. Four purified human creatine-kinase isoforms phosphorylated creatine but not taurocyamine, guanidinobutyrate or guanidinopropionate at 10 mM test substrate.

    Human CKB, CKM, CKMT1 and CKMT2 substrate panel → Taurocyamine / guanidinotaurine source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text; Figure 4A
    experimental_model
    Human recombinant kinases; radiolabeled ATP and TLC; annelid taurocyamine kinase positive control.
    limitations
    The experimental result does not exclude every reaction at other conditions, but does not support replacing creatine.
    nutrient_topic
    Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
    plain_language
    Related guanidino compounds are not automatically interchangeable energy buffers.
    primary_references
    Guanidino acid hydrolysis by the human enzyme annotated as agmatinase. · 2022 · https://pubmed.ncbi.nlm.nih.gov/36543883/ · DOI 10.1038/s41598-022-26655-4

    Agmatine Sulfate: transport, guanidino metabolism, ion channels and cross-nutrient mechanisms (2026-09-20) · lines 212–218

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human recombinant kinases; radiolabeled ATP and TLC; annelid taurocyamine kinase positive control. · source_derived_draft · unverified_draft

    ## agmatine-sulfate-creatine-specificity Related guanidino compounds are not automatically interchangeable energy buffers. Four purified human creatine-kinase isoforms phosphorylated creatine but not taurocyamine, guanidinobutyrate or guanidinopropionate at 10 mM test substrate. Model: Human recombinant kinases; radiolabeled ATP and TLC; annelid taurocyamine kinase positive control. Limitations: The experimental result does not exclude every reaction at other conditions, but does not support replacing creatine. Evidence access: Primary full text; Figure 4A Guanidino acid hydrolysis by the human enzyme annotated as agmatinase. · 2022 · https://pubmed.ncbi.nlm.nih.gov/36543883/ · DOI 10.1038/s41598-022-26655-4
    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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