Component

2-Amino-3-carboxymuconate 6-semialdehyde

ACMS; immediate HAAO ring-cleavage intermediate that can spontaneously cyclize to quinolinate.

1 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.

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. Human HAAO expressed in HEK-293 cells was enzymatically active toward 3-hydroxyanthranilate, with an apparent substrate Km near 2 micromolar in the study of the quinolinate-producing pathway step.

    Experimental context and source evidence
    cross_nutrient
    This step follows the canonical PLP-dependent KYNU reaction and uses a nonheme iron enzyme.
    evidence_span
    {"source_cache": "artifacts/niacin-precursors-sources/haao1994.abstract.txt", "locator": "Indexed primary abstract", "start_char": 0, "end_char": 1874, "file_sha256": "a79697b138bcb2957b0eff9580266c7879a1c5853aba34898f891559b4e435f8", "text_sha256": "a79697b138bcb2957b0eff9580266c7879a1c5853aba34898f891559b4e435f8"}
    experimental_model
    Human HAAO cDNA from HepG2 library, expressed in HEK-293 cells and assayed biochemically
    exposure
    Biochemical or structural assay; no dietary intervention
    limitations
    The immediate HAAO product is ACMS, which cyclizes to quinolinate; the indexed abstract uses pathway-level quinolinate wording. This claim does not assert direct NAD+ synthesis.
    nutrient_topic
    Niacin research collection; topical membership is not evidence of a direct dietary effect. · Niacin (vitamin B3)
    organism
    Homo sapiens
    plain_language
    Expressed human HAAO processed the product made by B6-dependent KYNU.
    primary_references
    [b3-pre-haao1994] Molecular cloning and functional expression of human 3-hydroxyanthranilic-acid dioxygenase. (1994). https://pubmed.ncbi.nlm.nih.gov/7514594/ DOI: 10.1016/s0021-9258(17)36717-0 [b3-pre-haao2017] Crystal structures of human 3-hydroxyanthranilate 3,4-dioxygenase with native and non-native metals bound in the active site. (2017). https://pubmed.ncbi.nlm.nih.gov/28375145/ DOI: 10.1107/s2059798317002029
    supporting_evidence_spans
    [{"source_cache": "artifacts/niacin-precursors-sources/haao2017.paragraphs.txt", "locator": "Normalized full-text paragraphs 14–14 (0-based)", "start_char": 4395, "end_char": 7197, "file_sha256": "d02386a59595104ccae2e62943e69030930da86ec005769b469f2001e31a6eb5", "text_sha256": "3b52b56d1b671c24721b47204cd30d19cd004f8a461fecd4875e94d3f491dbf6"}]
    tissue_or_cell_type
    HEK-293 cells expressing human HAAO; biochemical activity assay

    Niacin: NAD metabolism, deficiency and nutrient interactions (2026-09-17) · lines 521–535

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human HAAO cDNA from HepG2 library, expressed in HEK-293 cells and assayed biochemically · source_derived_draft · unverified_draft

    ### b3-pre-haao-human-activity Human HAAO expressed in HEK-293 cells was enzymatically active toward 3-hydroxyanthranilate, with an apparent substrate Km near 2 micromolar in the study of the quinolinate-producing pathway step. Condition category: normal nutrient_topic: Niacin research collection; topical membership is not evidence of a direct dietary effect. plain_language: Expressed human HAAO processed the product made by B6-dependent KYNU. organism: Homo sapiens tissue_or_cell_type: HEK-293 cells expressing human HAAO; biochemical activity assay experimental_model: Human HAAO cDNA from HepG2 library, expressed in HEK-293 cells and assayed biochemically limitations: The immediate HAAO product is ACMS, which cyclizes to quinolinate; the indexed abstract uses pathway-level quinolinate wording. This claim does not assert direct NAD+ synthesis. exposure: Biochemical or structural assay; no dietary intervention cross_nutrient: This step follows the canonical PLP-dependent KYNU reaction and uses a nonheme iron enzyme. evidence_span: {"source_cache": "artifacts/niacin-precursors-sources/haao1994.abstract.txt", "locator": "Indexed primary abstract", "start_char": 0, "end_char": 1874, "file_sha256": "a79697b138bcb2957b0eff9580266c7879a1c5853aba34898f891559b4e435f8", "text_sha256": "a79697b138bcb2957b0eff9580266c7879a1c5853aba34898f891559b4e435f8"} supporting_evidence_spans: [{"source_cache": "artifacts/niacin-precursors-sources/haao2017.paragraphs.txt", "locator": "Normalized full-text paragraphs 14–14 (0-based)", "start_char": 4395, "end_char": 7197, "file_sha256": "d02386a59595104ccae2e62943e69030930da86ec005769b469f2001e31a6eb5", "text_sha256": "3b52b56d1b671c24721b47204cd30d19cd004f8a461fecd4875e94d3f491dbf6"}] [b3-pre-haao1994] Molecular cloning and functional expression of human 3-hydroxyanthranilic-acid dioxygenase. (1994). https://pubmed.ncbi.nlm.nih.gov/7514594/ DOI: 10.1016/s0021-9258(17)36717-0 [b3-pre-haao2017] Crystal structures of human 3-hydroxyanthranilate 3,4-dioxygenase with native and non-native metals bound in the active site. (2017). https://pubmed.ncbi.nlm.nih.gov/28375145/ DOI: 10.1107/s2059798317002029
    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