Component

Urea

Urea, the product of arginase-catalyzed arginine hydrolysis.

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

Where it participates (unsigned role)

  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 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

  3. 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

  4. Purified recombinant human ARG2 catalyzes arginine hydrolysis to ornithine and urea.

    Human arginase 2 / ARG2 → L-Arginine source_derived_draftungraded
    Experimental context and source evidence
    experimental_model
    Recombinant human ARG2 expressed in E. coli and purified
    exposure
    Substrate/product kinetics
    limitations
    Primary experimental scope only; no human dietary threshold, clinical treatment rule, or universal metal substitution is established.
    nutrient_topic
    Manganese research collection; topical membership is not evidence of a direct dietary effect. · Manganese
    organism
    Homo sapiens protein
    plain_language
    ARG2 breaks arginine into ornithine and urea.
    primary_references
    [mn-enz-11370664] Expression, purification, and characterization of human type II arginase. (2001). https://pubmed.ncbi.nlm.nih.gov/11370664/ DOI: 10.1006/abbi.2001.2324
    tissue_or_cell_type
    Purified ARG2

    Manganese: enzyme cofactors, glycosylation, transport and nutrient interactions (2026-09-17) · lines 572–582

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human ARG2 expressed in E. coli and purified · source_derived_draft · unverified_draft

    ### mn-enz-arg2-hydrolysis Purified recombinant human ARG2 catalyzes arginine hydrolysis to ornithine and urea. Condition category: normal nutrient_topic: Manganese research collection; topical membership is not evidence of a direct dietary effect. plain_language: ARG2 breaks arginine into ornithine and urea. organism: Homo sapiens protein tissue_or_cell_type: Purified ARG2 experimental_model: Recombinant human ARG2 expressed in E. coli and purified limitations: Primary experimental scope only; no human dietary threshold, clinical treatment rule, or universal metal substitution is established. exposure: Substrate/product kinetics [mn-enz-11370664] Expression, purification, and characterization of human type II arginase. (2001). https://pubmed.ncbi.nlm.nih.gov/11370664/ DOI: 10.1006/abbi.2001.2324
    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