Component

Human fumarylacetoacetate hydrolase / FAH

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 it acts on

  1. In 13 unrelated hereditary-tyrosinemia-I families, FAH nonsense variants reduced transcript abundance and splice-site variants altered exon inclusion.

    Human fumarylacetoacetate hydrolase / FAH → Human FAH transcript abundance and splicing source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary abstract
    experimental_model
    Human family genotyping and RNA analysis.
    limitations
    No strict genotype-severity relationship was established in this series.
    nutrient_topic
    L-Tyrosine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Tyrosine
    plain_language
    The disease can arise before a functional enzyme is made.
    primary_references
    Hereditary tyrosinemia type 1: novel missense, nonsense and splice consensus mutations in the human fumarylacetoacetate hydrolase gene; variability of the genotype-phenotype relationship. · 1996 · https://pubmed.ncbi.nlm.nih.gov/8557261/ · DOI 10.1007/BF00218833
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    L-Tyrosine: catecholamines, thyroid chemistry, pigment, metabolism and cross-nutrient mechanisms (2026-09-19) · lines 276–282

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human family genotyping and RNA analysis. · source_derived_draft · unverified_draft

    ## l-tyrosine-fah-genetic The disease can arise before a functional enzyme is made. In 13 unrelated hereditary-tyrosinemia-I families, FAH nonsense variants reduced transcript abundance and splice-site variants altered exon inclusion. Model: Human family genotyping and RNA analysis. Limitations: No strict genotype-severity relationship was established in this series. Evidence access: Primary abstract Hereditary tyrosinemia type 1: novel missense, nonsense and splice consensus mutations in the human fumarylacetoacetate hydrolase gene; variability of the genotype-phenotype relationship. · 1996 · https://pubmed.ncbi.nlm.nih.gov/8557261/ · DOI 10.1007/BF00218833
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Succinylacetone competitively inhibited purified human erythrocyte ALAD; the study reported submicromolar inhibition constants across human and animal preparations.

    Succinylacetone → Human delta-aminolevulinate dehydratase / ALAD source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary abstract
    experimental_model
    Purified human erythrocyte enzyme plus mouse/bovine preparations; four affected patients.
    limitations
    The metabolite is associated with FAH deficiency, not demonstrated as a consequence of ordinary tyrosine supplements.
    nutrient_topic
    L-Tyrosine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Tyrosine
    plain_language
    A blocked tyrosine pathway can interfere with heme production.
    primary_references
    Hereditary tyrosinemia and the heme biosynthetic pathway. Profound inhibition of delta-aminolevulinic acid dehydratase activity by succinylacetone. · 1983 · https://pubmed.ncbi.nlm.nih.gov/6826727/ · DOI 10.1172/jci110809
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    L-Tyrosine: catecholamines, thyroid chemistry, pigment, metabolism and cross-nutrient mechanisms (2026-09-19) · lines 284–290

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Purified human erythrocyte enzyme plus mouse/bovine preparations; four affected patients. · source_derived_draft · unverified_draft

    ## l-tyrosine-sa-alad A blocked tyrosine pathway can interfere with heme production. Succinylacetone competitively inhibited purified human erythrocyte ALAD; the study reported submicromolar inhibition constants across human and animal preparations. Model: Purified human erythrocyte enzyme plus mouse/bovine preparations; four affected patients. Limitations: The metabolite is associated with FAH deficiency, not demonstrated as a consequence of ordinary tyrosine supplements. Evidence access: Primary abstract Hereditary tyrosinemia and the heme biosynthetic pathway. Profound inhibition of delta-aminolevulinic acid dehydratase activity by succinylacetone. · 1983 · https://pubmed.ncbi.nlm.nih.gov/6826727/ · DOI 10.1172/jci110809
    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