Component
AMPylated GLUD1
GLUD1 modified by covalent AMP attachment; distinct from free AMP.
2 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.
Other things that act on it
Enzymes, hormones, genes, and other components with a recorded effect. These are not nutrients, so they do not count toward the arrows above. Each finding names the chapter that recorded it.
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.
What it acts on
AMPylation decreased GLUD1 enzymatic activity in the tested assays.
Experimental context and source evidence
- cell_type
- experimental assay
- experimental_model
- Modified-enzyme activity measurements
- limitations
- No human dietary response established.
- organism
- mammalian
Selenium: literature corrections and mechanism additions · lines 498–508
Metabolic Ledger literature curation, 17 September 2026; primary papers linked individually · supports · Modified-enzyme activity measurements · secondary_verified · secondary_verified
## glud1-ampylation-decreases-activity The AMP modification reduced GLUD1 activity in these experiments. AMPylation decreased GLUD1 enzymatic activity in the tested assays. Organism: mammalian Cell type: experimental assay Experimental model: Modified-enzyme activity measurements Limitations: No human dietary response established. 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
Where it participates (unsigned role)
SELENOO catalyzes AMP attachment to GLUD1.
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
The events it takes part in
A mechanism often involves more than two components. These are the full events, with every participant and its role.
Situations it appears in
Low-supply and faulty-machinery situations recorded in the chapters where this component plays a part.
In the sources
Preserved passages that mention this component, quoted exactly. Open one to read it in context.
Open hypotheses
Proposed ideas that involve this component. They are labeled as hypotheses and do not change any recorded statement.
This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.