Component

Saccharomyces cerevisiae Sdh1

Yeast succinate dehydrogenase flavoprotein subunit; homolog of human SDHA.

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 acts on it

  1. Human SDHAF2 G78R failed to restore Sdh1 flavination in sdh5-null yeast, whereas wild-type human SDHAF2 restored it to about 77% of wild-type yeast.

    Human SDHAF2 Gly78Arg → Saccharomyces cerevisiae Sdh1 source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_spans
    [{"source_bundle": "artifacts/riboflavin_metabolism_sources.json", "source_key": "PMC3881419", "locator": "HTML article p", "paragraph_index": 22, "char_start": 0, "char_end": 998, "evidence_access": "full-text"}]
    experimental_model
    Yeast genetics, recombinant coexpression, human HEK293 binding assays and familial paraganglioma tissue.
    exposure
    Expression from yeast SDH5 promoter; normalized FAD fluorescence.
    limitations
    Cross-species complementation; not a riboflavin-supplement rescue experiment.
    nutrient_topic
    Riboflavin research collection; topical membership is not evidence of a direct dietary effect. · Riboflavin (vitamin B2)
    organism
    Homo sapiens protein in Saccharomyces cerevisiae
    plain_language
    The inherited altered assembly factor failed a functional rescue test.
    primary_references
    [hao-2009-sdh5] SDH5, a gene required for flavination of succinate dehydrogenase, is mutated in paraganglioma (2009). https://pubmed.ncbi.nlm.nih.gov/19628817/ DOI: 10.1126/science.1175689
    tissue_or_cell_type
    Yeast complementation
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Riboflavin: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 702–713

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Yeast genetics, recombinant coexpression, human HEK293 binding assays and familial paraganglioma tissue. · source_derived_draft · unverified_draft

    ### b2-met-sdhaf2-g78r-rescue Human SDHAF2 G78R failed to restore Sdh1 flavination in sdh5-null yeast, whereas wild-type human SDHAF2 restored it to about 77% of wild-type yeast. Condition category: machinery_impairment nutrient_topic: Riboflavin research collection; topical membership is not evidence of a direct dietary effect. plain_language: The inherited altered assembly factor failed a functional rescue test. organism: Homo sapiens protein in Saccharomyces cerevisiae tissue_or_cell_type: Yeast complementation experimental_model: Yeast genetics, recombinant coexpression, human HEK293 binding assays and familial paraganglioma tissue. limitations: Cross-species complementation; not a riboflavin-supplement rescue experiment. exposure: Expression from yeast SDH5 promoter; normalized FAD fluorescence. evidence_spans: [{"source_bundle": "artifacts/riboflavin_metabolism_sources.json", "source_key": "PMC3881419", "locator": "HTML article p", "paragraph_index": 22, "char_start": 0, "char_end": 998, "evidence_access": "full-text"}] [hao-2009-sdh5] SDH5, a gene required for flavination of succinate dehydrogenase, is mutated in paraganglioma (2009). https://pubmed.ncbi.nlm.nih.gov/19628817/ DOI: 10.1126/science.1175689
    Complete structured claim and evidence

  2. Deleting yeast SDH5 eliminated detected covalent FAD attachment to Sdh1 even though Sdh1 protein remained present.

    Saccharomyces cerevisiae sdh5 deletion → Saccharomyces cerevisiae Sdh1 source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_spans
    [{"source_bundle": "artifacts/riboflavin_metabolism_sources.json", "source_key": "PMC3881419", "locator": "HTML article p", "paragraph_index": 13, "char_start": 0, "char_end": 660, "evidence_access": "full-text"}]
    experimental_model
    Yeast genetics, recombinant coexpression, human HEK293 binding assays and familial paraganglioma tissue.
    exposure
    SDH5 deletion; SDS-PAGE FAD fluorescence and immunoblot.
    limitations
    Not proof of universal SDHAF2 requirement in mammalian cells.
    nutrient_topic
    Riboflavin research collection; topical membership is not evidence of a direct dietary effect. · Riboflavin (vitamin B2)
    organism
    Saccharomyces cerevisiae
    plain_language
    An assembly defect removed the cofactor attachment without simply removing all of the target protein.
    primary_references
    [hao-2009-sdh5] SDH5, a gene required for flavination of succinate dehydrogenase, is mutated in paraganglioma (2009). https://pubmed.ncbi.nlm.nih.gov/19628817/ DOI: 10.1126/science.1175689
    tissue_or_cell_type
    Yeast mitochondria
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Riboflavin: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 689–700

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Yeast genetics, recombinant coexpression, human HEK293 binding assays and familial paraganglioma tissue. · source_derived_draft · unverified_draft

    ### b2-met-yeast-sdh5-flavination Deleting yeast SDH5 eliminated detected covalent FAD attachment to Sdh1 even though Sdh1 protein remained present. Condition category: machinery_impairment nutrient_topic: Riboflavin research collection; topical membership is not evidence of a direct dietary effect. plain_language: An assembly defect removed the cofactor attachment without simply removing all of the target protein. organism: Saccharomyces cerevisiae tissue_or_cell_type: Yeast mitochondria experimental_model: Yeast genetics, recombinant coexpression, human HEK293 binding assays and familial paraganglioma tissue. limitations: Not proof of universal SDHAF2 requirement in mammalian cells. exposure: SDH5 deletion; SDS-PAGE FAD fluorescence and immunoblot. evidence_spans: [{"source_bundle": "artifacts/riboflavin_metabolism_sources.json", "source_key": "PMC3881419", "locator": "HTML article p", "paragraph_index": 13, "char_start": 0, "char_end": 660, "evidence_access": "full-text"}] [hao-2009-sdh5] SDH5, a gene required for flavination of succinate dehydrogenase, is mutated in paraganglioma (2009). https://pubmed.ncbi.nlm.nih.gov/19628817/ DOI: 10.1126/science.1175689
    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