Component

Isovaleryl-CoA

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

3 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. Purified GLYAT formed N-isovalerylglycine from isovaleryl-CoA and glycine in vitro, with lower affinity than for its preferred substrate.

    Human glycine N-acyltransferase / GLYAT → N-Isovalerylglycine source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text
    experimental_model
    Recombinant enzyme validation alongside docking.
    limitations
    The causal evidence recorded here is the enzyme assay, not the docking prediction; whole-body contribution is unresolved.
    nutrient_topic
    Glycine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Glycine
    plain_language
    Glycine conjugation can intersect with leucine-breakdown metabolites.
    primary_references
    The glycine N-acyltransferases, GLYAT and GLYATL1, contribute to the detoxification of isovaleryl-CoA - an in-silico and in vitro validation. · 2023 · https://pubmed.ncbi.nlm.nih.gov/36817957/ · DOI 10.1016/j.csbj.2023.01.041

    Glycine: supply, one-carbon allocation, receptors and cross-nutrient mechanisms (2026-09-19) · lines 290–296

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Recombinant enzyme validation alongside docking. · source_derived_draft · unverified_draft

    ## glycine-glyat-isovaleryl Glycine conjugation can intersect with leucine-breakdown metabolites. Purified GLYAT formed N-isovalerylglycine from isovaleryl-CoA and glycine in vitro, with lower affinity than for its preferred substrate. Model: Recombinant enzyme validation alongside docking. Limitations: The causal evidence recorded here is the enzyme assay, not the docking prediction; whole-body contribution is unresolved. Evidence access: Primary full text The glycine N-acyltransferases, GLYAT and GLYATL1, contribute to the detoxification of isovaleryl-CoA - an in-silico and in vitro validation. · 2023 · https://pubmed.ncbi.nlm.nih.gov/36817957/ · DOI 10.1016/j.csbj.2023.01.041
    Complete structured claim and evidence

  2. Purified GLYATL1 also supported N-isovalerylglycine formation in vitro, less favorably than its preferred substrate reaction.

    Human glycine N-acyltransferase-like 1 / GLYATL1 → N-Isovalerylglycine source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text
    experimental_model
    Purified enzyme assays.
    limitations
    Does not establish which enzyme dominates in a patient.
    nutrient_topic
    Glycine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Glycine
    plain_language
    A related enzyme provides another possible route to the same product.
    primary_references
    The glycine N-acyltransferases, GLYAT and GLYATL1, contribute to the detoxification of isovaleryl-CoA - an in-silico and in vitro validation. · 2023 · https://pubmed.ncbi.nlm.nih.gov/36817957/ · DOI 10.1016/j.csbj.2023.01.041

    Glycine: supply, one-carbon allocation, receptors and cross-nutrient mechanisms (2026-09-19) · lines 298–304

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

    ## glycine-glyatl1-isovaleryl A related enzyme provides another possible route to the same product. Purified GLYATL1 also supported N-isovalerylglycine formation in vitro, less favorably than its preferred substrate reaction. Model: Purified enzyme assays. Limitations: Does not establish which enzyme dominates in a patient. Evidence access: Primary full text The glycine N-acyltransferases, GLYAT and GLYATL1, contribute to the detoxification of isovaleryl-CoA - an in-silico and in vitro validation. · 2023 · https://pubmed.ncbi.nlm.nih.gov/36817957/ · DOI 10.1016/j.csbj.2023.01.041
    Complete structured claim and evidence

  3. Increasing glycine did not increase N-isovalerylglycine formation in the reported in-vitro conjugation experiments.

    Glycine → N-Isovalerylglycine source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text
    experimental_model
    GLYAT/GLYATL1 enzyme experiments.
    limitations
    Not evidence that glycine treatment never works in isovaleric acidemia; substrate, enzyme and kinetic context matter.
    nutrient_topic
    Glycine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Glycine
    plain_language
    Adding substrate did not keep increasing this disposal reaction.
    primary_references
    The glycine N-acyltransferases, GLYAT and GLYATL1, contribute to the detoxification of isovaleryl-CoA - an in-silico and in vitro validation. · 2023 · https://pubmed.ncbi.nlm.nih.gov/36817957/ · DOI 10.1016/j.csbj.2023.01.041

    Glycine: supply, one-carbon allocation, receptors and cross-nutrient mechanisms (2026-09-19) · lines 306–312

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · GLYAT/GLYATL1 enzyme experiments. · source_derived_draft · unverified_draft

    ## glycine-isovaleryl-glycine-limit Adding substrate did not keep increasing this disposal reaction. Increasing glycine did not increase N-isovalerylglycine formation in the reported in-vitro conjugation experiments. Model: GLYAT/GLYATL1 enzyme experiments. Limitations: Not evidence that glycine treatment never works in isovaleric acidemia; substrate, enzyme and kinetic context matter. Evidence access: Primary full text The glycine N-acyltransferases, GLYAT and GLYATL1, contribute to the detoxification of isovaleryl-CoA - an in-silico and in vitro validation. · 2023 · https://pubmed.ncbi.nlm.nih.gov/36817957/ · DOI 10.1016/j.csbj.2023.01.041
    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