Component

FAD synthesis

FLAD1-catalyzed adenylylation of FMN using ATP.

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

What acts on it

  1. FAD-saturated p.Ser495del and p.Arg530Cys FADS2 remained substantially less catalytically active than wild type.

    FAD → FAD synthesis source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_location
    Figure 5
    experimental_model
    FAD-saturated purified FADS2 variants
    exposure
    Molar-excess FAD reconstitution followed by catalytic assays.
    limitations
    The two variants differ in binding/stability responses; the result concerns maximal in vitro activity.
    nutrient_topic
    Riboflavin research collection; topical membership is not evidence of a direct dietary effect. · Riboflavin (vitamin B2)
    organism
    Homo sapiens protein
    plain_language
    Stabilizing a variant does not necessarily restore normal enzyme output.
    primary_references
    [transport-flad1-disease-2016] Riboflavin-Responsive and -Non-responsive Mutations in FAD Synthase Cause Multiple Acyl-CoA Dehydrogenase and Combined Respiratory-Chain Deficiency (2016). https://pmc.ncbi.nlm.nih.gov/articles/PMC4908180/ DOI: 10.1016/j.ajhg.2016.04.006
    tissue_or_cell_type
    Purified protein
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Riboflavin: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 412–423

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · FAD-saturated purified FADS2 variants · source_derived_draft · unverified_draft

    ### transport-flad1-residual-catalytic-defect FAD-saturated p.Ser495del and p.Arg530Cys FADS2 remained substantially less catalytically active than wild type. Condition category: machinery_impairment nutrient_topic: Riboflavin research collection; topical membership is not evidence of a direct dietary effect. plain_language: Stabilizing a variant does not necessarily restore normal enzyme output. organism: Homo sapiens protein tissue_or_cell_type: Purified protein experimental_model: FAD-saturated purified FADS2 variants limitations: The two variants differ in binding/stability responses; the result concerns maximal in vitro activity. exposure: Molar-excess FAD reconstitution followed by catalytic assays. evidence_location: Figure 5 [transport-flad1-disease-2016] Riboflavin-Responsive and -Non-responsive Mutations in FAD Synthase Cause Multiple Acyl-CoA Dehydrogenase and Combined Respiratory-Chain Deficiency (2016). https://pmc.ncbi.nlm.nih.gov/articles/PMC4908180/ DOI: 10.1016/j.ajhg.2016.04.006
    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