Component

Fumarylacetoacetate

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

2 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. Mouse FAH structural and biochemical studies support cleavage of fumarylacetoacetate into fumarate and acetoacetate.

    Mouse fumarylacetoacetate hydrolase / Fah → Fumarylacetoacetate source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Mouse enzyme structure and physiological-product complexes.
    limitations
    The product-bound structure is mouse evidence; the separate human FAH gene/disease record is retained.
    nutrient_topic
    L-Tyrosine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Tyrosine
    plain_language
    The pathway connects the amino-acid carbon skeleton to central metabolism.
    primary_references
    Crystal structure and mechanism of a carbon-carbon bond hydrolase. · 1999 · https://pubmed.ncbi.nlm.nih.gov/10508789/ · DOI 10.1016/s0969-2126(99)80170-1

    L-Tyrosine: catecholamines, thyroid chemistry, pigment, metabolism and cross-nutrient mechanisms (2026-09-19) · lines 260–266

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Mouse enzyme structure and physiological-product complexes. · source_derived_draft · unverified_draft

    ## l-tyrosine-fah-products The pathway connects the amino-acid carbon skeleton to central metabolism. Mouse FAH structural and biochemical studies support cleavage of fumarylacetoacetate into fumarate and acetoacetate. Model: Mouse enzyme structure and physiological-product complexes. Limitations: The product-bound structure is mouse evidence; the separate human FAH gene/disease record is retained. Evidence access: Primary abstract Crystal structure and mechanism of a carbon-carbon bond hydrolase. · 1999 · https://pubmed.ncbi.nlm.nih.gov/10508789/ · DOI 10.1016/s0969-2126(99)80170-1
    Complete structured claim and evidence

  2. Human GSTZ1/MAAI catalyzes glutathione-dependent isomerization of maleylacetoacetate to fumarylacetoacetate.

    Human maleylacetoacetate isomerase / GSTZ1 → Fumarylacetoacetate source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human MAAI crystal structure with glutathione and a substrate-mimicking sulfate ion.
    limitations
    Glutathione dependence does not imply stoichiometric depletion by ordinary tyrosine intake.
    nutrient_topic
    L-Tyrosine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Tyrosine
    plain_language
    Glutathione has a catalytic role in nutrient breakdown as well as antioxidant roles.
    primary_references
    Crystal structure of maleylacetoacetate isomerase/glutathione transferase zeta reveals the molecular basis for its remarkable catalytic promiscuity. · 2001 · https://pubmed.ncbi.nlm.nih.gov/11327815/ · DOI 10.1021/bi002249z

    L-Tyrosine: catecholamines, thyroid chemistry, pigment, metabolism and cross-nutrient mechanisms (2026-09-19) · lines 252–258

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human MAAI crystal structure with glutathione and a substrate-mimicking sulfate ion. · source_derived_draft · unverified_draft

    ## l-tyrosine-gst-isomerase Glutathione has a catalytic role in nutrient breakdown as well as antioxidant roles. Human GSTZ1/MAAI catalyzes glutathione-dependent isomerization of maleylacetoacetate to fumarylacetoacetate. Model: Human MAAI crystal structure with glutathione and a substrate-mimicking sulfate ion. Limitations: Glutathione dependence does not imply stoichiometric depletion by ordinary tyrosine intake. Evidence access: Primary abstract Crystal structure of maleylacetoacetate isomerase/glutathione transferase zeta reveals the molecular basis for its remarkable catalytic promiscuity. · 2001 · https://pubmed.ncbi.nlm.nih.gov/11327815/ · DOI 10.1021/bi002249z
    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