Component

Taurocyamine / guanidinotaurine

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

4 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. 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

  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

  3. Purified human GATM transferred an amidino group from arginine to taurine, producing taurocyamine in vitro.

    Human glycine amidinotransferase AGAT / GATM → Taurocyamine / guanidinotaurine source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text; Figure 4B
    experimental_model
    Recombinant human GATM substrate comparison.
    limitations
    Taurine is a secondary substrate in this assay; tissue flux and clinically important depletion were not established.
    nutrient_topic
    Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
    plain_language
    Creatine-synthesis machinery also accepts a taurine-related side reaction.
    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 188–194

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

    ## agmatine-sulfate-gatm-taurine Creatine-synthesis machinery also accepts a taurine-related side reaction. Purified human GATM transferred an amidino group from arginine to taurine, producing taurocyamine in vitro. Model: Recombinant human GATM substrate comparison. Limitations: Taurine is a secondary substrate in this assay; tissue flux and clinically important depletion were not established. 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

Where it participates (unsigned role)

  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.

    Evidence, AI assistance and curation standards