Component
Succinylacetone
Pharmacological inhibitor of heme biosynthesis.
3 recorded relationships. Experimental role, claim status and evidence remain attached to each record.
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.
Other things that act on it
Enzymes, hormones, genes, and other components with a recorded effect. These are not nutrients, so they do not count toward the arrows above. Each finding names the chapter that recorded it.
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.
What it acts on
Succinylacetone competitively inhibited purified human erythrocyte ALAD; the study reported submicromolar inhibition constants across human and animal preparations.
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 evidenceAdding succinylacetone to avian hepatocytes reduced cellular heme and cytochrome P450 content.
Experimental context and source evidence
- availability_state
- machinery_impairment Imported condition classification; unverified.
- evidence_access
- Primary abstract
- experimental_model
- Cultured avian hepatocytes with direct metabolite exposure.
- limitations
- The cellular effect is avian; the human ALAD inhibition is recorded separately.
- nutrient_topic
- L-Tyrosine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Tyrosine
- plain_language
- One pathway blockage can reduce machinery used by other pathways.
- 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 292–298
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Cultured avian hepatocytes with direct metabolite exposure. · source_derived_draft · unverified_draft
## l-tyrosine-sa-heme One pathway blockage can reduce machinery used by other pathways. Adding succinylacetone to avian hepatocytes reduced cellular heme and cytochrome P450 content. Model: Cultured avian hepatocytes with direct metabolite exposure. Limitations: The cellular effect is avian; the human ALAD inhibition is recorded separately. 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 evidenceIn CHO cells expressing human TPO, inhibition of heme biosynthesis by succinylacetone decreased surface TPO expression by approximately 80%.
Experimental context and source evidence
- cross_nutrient
- true
- evidence_span
- {"source_cache": "artifacts/iodine-synthesis-sources/10187846.json", "json_field": "abstractText", "text_sha256": "97f8a86c7effd5754e2b61c65d769de9e86678a7398c5eb20a0e88ac49a8fdbb", "text_characters": 1855, "note": "Exact publisher passage retained in the cited local source cache; locator and digest supplied here."}
- experimental_model
- CHO cells expressing human TPO; additional primary thyroid cultures
- exposure
- Succinylacetone; concentration not stated in abstract.
- limitations
- Pharmacological heme synthesis perturbation; not evidence of a dietary iron threshold.
- nutrient_topic
- Iodine research collection; topical membership is not evidence of a direct dietary effect. · Iodine
- organism
- Homo sapiens protein; Cricetulus griseus host cells
- plain_language
- Blocking heme production kept much of TPO from reaching the surface.
- primary_references
- [iodine-syn-tpo1999] Role of heme in intracellular trafficking of thyroperoxidase and involvement of H2O2 generated at the apical surface of thyroid cells in autocatalytic covalent heme binding. (1999). https://pubmed.ncbi.nlm.nih.gov/10187846/ DOI: 10.1074/jbc.274.15.10533
- tissue_or_cell_type
- CHO endoplasmic reticulum and cell surface
Iodine: thyroid hormone production, deficiency, excess and nutrient interactions (2026-09-17) · lines 576–588
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · CHO cells expressing human TPO; additional primary thyroid cultures · source_derived_draft · unverified_draft
### iodine-syn-heme-trafficking In CHO cells expressing human TPO, inhibition of heme biosynthesis by succinylacetone decreased surface TPO expression by approximately 80%. Condition category: normal nutrient_topic: Iodine research collection; topical membership is not evidence of a direct dietary effect. plain_language: Blocking heme production kept much of TPO from reaching the surface. organism: Homo sapiens protein; Cricetulus griseus host cells tissue_or_cell_type: CHO endoplasmic reticulum and cell surface experimental_model: CHO cells expressing human TPO; additional primary thyroid cultures limitations: Pharmacological heme synthesis perturbation; not evidence of a dietary iron threshold. exposure: Succinylacetone; concentration not stated in abstract. cross_nutrient: true evidence_span: {"source_cache": "artifacts/iodine-synthesis-sources/10187846.json", "json_field": "abstractText", "text_sha256": "97f8a86c7effd5754e2b61c65d769de9e86678a7398c5eb20a0e88ac49a8fdbb", "text_characters": 1855, "note": "Exact publisher passage retained in the cited local source cache; locator and digest supplied here."} [iodine-syn-tpo1999] Role of heme in intracellular trafficking of thyroperoxidase and involvement of H2O2 generated at the apical surface of thyroid cells in autocatalytic covalent heme binding. (1999). https://pubmed.ncbi.nlm.nih.gov/10187846/ DOI: 10.1074/jbc.274.15.10533
Complete structured claim and evidence
The events it takes part in
A mechanism often involves more than two components. These are the full events, with every participant and its role.
Situations it appears in
Low-supply and faulty-machinery situations recorded in the chapters where this component plays a part.
In the sources
Preserved passages that mention this component, quoted exactly. Open one to read it in context.
Open hypotheses
Proposed ideas that involve this component. They are labeled as hypotheses and do not change any recorded statement.
This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.