Component

SELENOO

Mitochondrial selenoprotein with experimentally described NAD hydrolysis and protein AMPylation activities.

5 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 it acts on

  1. SELENOO catalyzes AMP attachment to GLUD1.

    SELENOO → GLUD1 source_derived_draftliterature_reviewed:direct_experimental
    Experimental context and source evidence
    cell_type
    experimental cells
    experimental_model
    Biochemical AMPylation assays
    limitations
    Substrate identification does not establish every tissue context.
    organism
    mammalian

    Selenium: literature corrections and mechanism additions · lines 486–496

    Metabolic Ledger literature curation, 17 September 2026; primary papers linked individually · supports · Biochemical AMPylation assays · secondary_verified · secondary_verified

    ## selenoo-ampylates-glud1 SELENOO can modify the metabolic enzyme GLUD1 with AMP. SELENOO catalyzes AMP attachment to GLUD1. Organism: mammalian Cell type: experimental cells Experimental model: Biochemical AMPylation assays Limitations: Substrate identification does not establish every tissue context. Primary reference: [A repurposed AMP binding domain reveals mitochondrial protein AMPylation as a regulator of cellular metabolism](https://www.nature.com/articles/s41467-025-63014-z)
    Complete structured claim and evidence

  2. SELENOO transfers AMP from ATP onto SDHA in the reported AMPylation experiments.

    SELENOO → SDHA source_derived_draftliterature_reviewed:direct_experimental
    Experimental context and source evidence
    cell_type
    melanoma-related assays
    experimental_model
    Biochemical substrate experiments
    limitations
    Keep this reaction separate from NAD hydrolysis.
    organism
    mammalian

    Selenium: literature corrections and mechanism additions · lines 462–472

    Metabolic Ledger literature curation, 17 September 2026; primary papers linked individually · supports · Biochemical substrate experiments · secondary_verified · secondary_verified

    ## selenoo-ampylates-sdha SELENOO can attach an AMP group to a respiratory enzyme. SELENOO transfers AMP from ATP onto SDHA in the reported AMPylation experiments. Organism: mammalian Cell type: melanoma-related assays Experimental model: Biochemical substrate experiments Limitations: Keep this reaction separate from NAD hydrolysis. Primary reference: [Selenoprotein O Promotes Melanoma Metastasis and Regulates Mitochondrial Complex II Activity](https://pubmed.ncbi.nlm.nih.gov/39700395/)
    Complete structured claim and evidence

  3. SELENOO catalyzes NAD+ hydrolysis to NMN and AMP.

    SELENOO → NAD+ source_derived_draftliterature_reviewed:direct_experimental
    Experimental context and source evidence
    cell_type
    experimental cells
    experimental_model
    Biochemical and cellular assays
    limitations
    Recent 2026 finding; no dietary-dose inference.
    organism
    mammalian

    Selenium: literature corrections and mechanism additions · lines 438–448

    Metabolic Ledger literature curation, 17 September 2026; primary papers linked individually · supports · Biochemical and cellular assays · secondary_verified · secondary_verified

    ## selenoo-hydrolyzes-nad SELENOO can split NAD into two smaller molecules. SELENOO catalyzes NAD+ hydrolysis to NMN and AMP. Organism: mammalian Cell type: experimental cells Experimental model: Biochemical and cellular assays Limitations: Recent 2026 finding; no dietary-dose inference. Primary reference: [NAD+ hydrolysis catalyzed by SelO is required for mitochondrial homeostasis](https://pubmed.ncbi.nlm.nih.gov/41806834/)
    Complete structured claim and evidence

  4. SELENOO deletion increased complex-II activity in the tested melanoma model.

    SELENOO → Respiratory complex II source_derived_draftliterature_reviewed:direct_experimental
    Experimental context and source evidence
    cell_type
    melanoma
    experimental_model
    Selenoo deletion
    limitations
    Does not isolate SDHA AMPylation as the sole cause.
    organism
    mouse

    Selenium: literature corrections and mechanism additions · lines 474–484

    Metabolic Ledger literature curation, 17 September 2026; primary papers linked individually · supports · Selenoo deletion · secondary_verified · secondary_verified

    ## selenoo-loss-increases-complex-ii-activity Removing SELENOO increased respiratory complex-II activity in this model. SELENOO deletion increased complex-II activity in the tested melanoma model. Organism: mouse Cell type: melanoma Experimental model: Selenoo deletion Limitations: Does not isolate SDHA AMPylation as the sole cause. Primary reference: [Selenoprotein O Promotes Melanoma Metastasis and Regulates Mitochondrial Complex II Activity](https://pubmed.ncbi.nlm.nih.gov/39700395/)
    Complete structured claim and evidence

What acts on it

  1. Mn2+ supports the reported SELENOO NAD-hydrolysis activity.

    Mn2+ → SELENOO source_derived_draftliterature_reviewed:direct_experimental
    Experimental context and source evidence
    cell_type
    experimental cells
    experimental_model
    Metal-dependent enzyme assays
    limitations
    Cofactor dependence does not establish nutritional limitation.
    organism
    mammalian

    Selenium: literature corrections and mechanism additions · lines 450–460

    Metabolic Ledger literature curation, 17 September 2026; primary papers linked individually · supports · Metal-dependent enzyme assays · secondary_verified · secondary_verified

    ## manganese-supports-selenoo-nadase Manganese acts as a cofactor in this reaction. Mn2+ supports the reported SELENOO NAD-hydrolysis activity. Organism: mammalian Cell type: experimental cells Experimental model: Metal-dependent enzyme assays Limitations: Cofactor dependence does not establish nutritional limitation. Primary reference: [NAD+ hydrolysis catalyzed by SelO is required for mitochondrial homeostasis](https://pubmed.ncbi.nlm.nih.gov/41806834/)
    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