Component

Human fatty acid synthase / FASN

Human fatty acid synthase / FASN. Identity is distinct from its gene and experimentally modified states; see each claim for organism and scope.

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

Where it participates (unsigned role)

  1. SAC reduced SREBP-1 levels and expression of lipogenic targets including ACC and FAS in HepG2 cells.

    S-allyl-L-cysteine / SAC → Sterol regulatory element-binding protein 1 / SREBP-1 source_derived_draftungraded
    Experimental context and source evidence
    acting_entity
    s-allylcysteine
    dose
    Not specified in accessed abstract
    duration
    Not specified in accessed abstract
    evidence_access
    Primary abstract
    experimental_comparison
    SAC addition; pathway inhibitor comparisons
    experimental_model
    Free-fatty-acid-treated HepG2 cells
    interpretation_status
    Source-derived research curation; not independent primary verification
    limitations
    SREBP-1 isoform and direct molecular target are unresolved in the accessed abstract.
    nutrient_topic
    S-allylcysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · S-allyl-L-cysteine / SAC
    organism
    Homo sapiens
    plain_language
    The lipid-production program changed as well as kinase activity.
    primary_references
    [23465592] S-allyl cysteine attenuates free fatty acid-induced lipogenesis in human HepG2 cells through activation of the AMP-activated protein kinase-dependent pathway. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23465592/ · DOI 10.1016/j.jnutbio.2012.12.006
    route
    Cell culture
    tissue_or_cell_type
    Free-fatty-acid-treated HepG2 cells

    S-allylcysteine: sulfur signaling, redox responses and cross-nutrient mechanisms (2026-09-20) · lines 203–210

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Free-fatty-acid-treated HepG2 cells · source_derived_draft · unverified_draft

    ## s-allylcysteine-srebp The lipid-production program changed as well as kinase activity. SAC reduced SREBP-1 levels and expression of lipogenic targets including ACC and FAS in HepG2 cells. Model: Free-fatty-acid-treated HepG2 cells Limitations: SREBP-1 isoform and direct molecular target are unresolved in the accessed abstract. Evidence access: Primary abstract [23465592] S-allyl cysteine attenuates free fatty acid-induced lipogenesis in human HepG2 cells through activation of the AMP-activated protein kinase-dependent pathway. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23465592/ · DOI 10.1016/j.jnutbio.2012.12.006 Structured context: {"organism": "Homo sapiens", "tissue_or_cell_type": "Free-fatty-acid-treated HepG2 cells", "dose": "Not specified in accessed abstract", "duration": "Not specified in accessed abstract", "route": "Cell culture", "experimental_comparison": "SAC addition; pathway inhibitor comparisons", "acting_entity": "s-allylcysteine", "interpretation_status": "Source-derived research curation; not independent primary verification"}
    Complete structured claim and evidence

  2. Human AASDHPPT transfers the 4′-phosphopantetheine moiety of CoA to a conserved serine in the human FASN acyl-carrier domain.

    Coenzyme A → Human FASN phosphopantetheinylated ACP domain source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    false
    evidence_location
    Abstract, substrate-specificity result
    experimental_model
    Recombinant human phosphopantetheinyl transferase and FASN ACP substrate
    exposure
    In-vitro enzymatic transfer from CoA; no dietary intervention.
    limitations
    Abstract-limited extraction; catalytic activation is distinguished from measuring whole-cell fatty-acid flux. This experiment does not establish a dietary pantothenate threshold or benefit from B5 supplementation.
    nutrient_topic
    Pantothenic acid (vitamin B5) research collection; topical membership is not evidence of a direct dietary effect. · Pantothenate (vitamin B5)
    organism
    Homo sapiens
    plain_language
    CoA supplies the movable chemical arm used by the fatty-acid synthase carrier domain.
    primary_references
    [b5-met-joshi2003] Cloning, expression, and characterization of a human 4'-phosphopantetheinyl transferase with broad substrate specificity. (2003). https://pubmed.ncbi.nlm.nih.gov/12815048/ DOI: 10.1074/jbc.m305459200
    tissue_or_cell_type
    Cytosolic FASN ACP domain

    Pantothenic acid (vitamin B5): coenzyme A, deficiency and nutrient interactions (2026-09-17) · lines 795–807

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human phosphopantetheinyl transferase and FASN ACP substrate · source_derived_draft · unverified_draft

    ### b5-met-aasdhppt-fasn Human AASDHPPT transfers the 4′-phosphopantetheine moiety of CoA to a conserved serine in the human FASN acyl-carrier domain. Condition category: normal nutrient_topic: Pantothenic acid (vitamin B5) research collection; topical membership is not evidence of a direct dietary effect. plain_language: CoA supplies the movable chemical arm used by the fatty-acid synthase carrier domain. organism: Homo sapiens tissue_or_cell_type: Cytosolic FASN ACP domain experimental_model: Recombinant human phosphopantetheinyl transferase and FASN ACP substrate limitations: Abstract-limited extraction; catalytic activation is distinguished from measuring whole-cell fatty-acid flux. This experiment does not establish a dietary pantothenate threshold or benefit from B5 supplementation. exposure: In-vitro enzymatic transfer from CoA; no dietary intervention. cross_nutrient: false evidence_location: Abstract, substrate-specificity result [b5-met-joshi2003] Cloning, expression, and characterization of a human 4'-phosphopantetheinyl transferase with broad substrate specificity. (2003). https://pubmed.ncbi.nlm.nih.gov/12815048/ DOI: 10.1074/jbc.m305459200
    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