Component

Human AGMAT, guanidino acid hydrolase candidate / historically annotated agmatinase

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 it acts on

  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. Purified recombinant human AGMAT variants R105 and G105 showed no detected agmatine hydrolysis at 10 mM substrate in the 2022 assay.

    Human AGMAT, guanidino acid hydrolase candidate / historically annotated agmatinase → Agmatine source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text; Figures 1 and 2
    experimental_model
    Human proteins expressed in E. coli; urea assay, detection limit about 0.02 nmol/s/mg.
    limitations
    This assay result revises the proposed substrate assignment; it does not prove that humans cannot metabolize agmatine by other routes.
    nutrient_topic
    Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
    plain_language
    A gene name does not guarantee the biochemical reaction usually drawn beside it.
    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 116–122

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human proteins expressed in E. coli; urea assay, detection limit about 0.02 nmol/s/mg. · source_derived_draft · unverified_draft

    ## agmatine-sulfate-agmat-reannotation A gene name does not guarantee the biochemical reaction usually drawn beside it. Purified recombinant human AGMAT variants R105 and G105 showed no detected agmatine hydrolysis at 10 mM substrate in the 2022 assay. Model: Human proteins expressed in E. coli; urea assay, detection limit about 0.02 nmol/s/mg. Limitations: This assay result revises the proposed substrate assignment; it does not prove that humans cannot metabolize agmatine by other routes. Evidence access: Primary full text; Figures 1 and 2 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. Human AGMAT R105 hydrolyzed taurocyamine more efficiently than guanidinobutyrate in the tested concentration range; R105 and G105 differed in substrate preferences.

    Human AGMAT, guanidino acid hydrolase candidate / historically annotated agmatinase → Taurocyamine / guanidinotaurine source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text; Figures 2 and 3
    experimental_model
    Purified human variants; 10 mM substrate comparison and concentration series.
    limitations
    This does not establish a clinically meaningful taurine deficit or a supplementation response.
    nutrient_topic
    Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
    plain_language
    A variant can alter which related metabolic pool is processed.
    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 132–138

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Purified human variants; 10 mM substrate comparison and concentration series. · source_derived_draft · unverified_draft

    ## agmatine-sulfate-agmat-taurocyamine A variant can alter which related metabolic pool is processed. Human AGMAT R105 hydrolyzed taurocyamine more efficiently than guanidinobutyrate in the tested concentration range; R105 and G105 differed in substrate preferences. Model: Purified human variants; 10 mM substrate comparison and concentration series. Limitations: This does not establish a clinically meaningful taurine deficit or a supplementation response. 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

  4. 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

What acts on it

  1. Expressing human AGMAT R105 in medium supplemented with 0.5 mM manganese increased its subsequent taurocyamine-hydrolysis activity approximately fourfold.

    Mn2+ → Human AGMAT, guanidino acid hydrolase candidate / historically annotated agmatinase source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text; Figure 3B
    experimental_model
    Recombinant human enzyme produced in bacterial expression culture.
    limitations
    This is not evidence that manganese supplements activate human agmatine breakdown; agmatine was not an accepted substrate.
    nutrient_topic
    Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
    plain_language
    Metal handling during enzyme production affects measured activity.
    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 140–146

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Recombinant human enzyme produced in bacterial expression culture. · source_derived_draft · unverified_draft

    ## agmatine-sulfate-agmat-manganese Metal handling during enzyme production affects measured activity. Expressing human AGMAT R105 in medium supplemented with 0.5 mM manganese increased its subsequent taurocyamine-hydrolysis activity approximately fourfold. Model: Recombinant human enzyme produced in bacterial expression culture. Limitations: This is not evidence that manganese supplements activate human agmatine breakdown; agmatine was not an accepted substrate. Evidence access: Primary full text; Figure 3B 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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