Component
Glutaryl-CoA dehydrogenase / GCDH
Independent protein record; interpretation is limited by each linked claim and its study context.
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
High lysine intake in Gcdh-null mice increases glutarate accumulation and produces age-dependent brain injury.
Experimental context and source evidence
- affected_machinery
- GCDH
- availability_state
- machinery_impairment Imported condition classification; unverified.
- deficiency_not_equivalent
- Nutrient deficiency or normal human lysine intake
- experimental_model
- High-lysine dietary challenge of Gcdh-knockout mice
- limitations
- Genetic susceptibility and age are essential; does not show comparable toxicity in healthy humans.
- organism
- Mus musculus
- plain_language
- Lysine loading can worsen a blocked breakdown pathway.
- primary_references
- [zinnanti2006] A diet-induced mouse model for glutaric aciduria type I (2006). https://pubmed.ncbi.nlm.nih.gov/16446282/ DOI: 10.1093/brain/awl009
- tissue_or_cell_type
- Brain and systemic circulation
- trigger_kind
- machinery_impairment Imported condition classification; unverified.
L-Lysine: mechanism-first literature curation (2026-09-17) · lines 290–300
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · High-lysine dietary challenge of Gcdh-knockout mice · source_derived_draft · unverified_draft
### gcdh-high-lysine-glutarate High lysine intake in Gcdh-null mice increases glutarate accumulation and produces age-dependent brain injury. Plain language: Lysine loading can worsen a blocked breakdown pathway. Condition category: machinery_impairment organism: Mus musculus tissue_or_cell_type: Brain and systemic circulation experimental_model: High-lysine dietary challenge of Gcdh-knockout mice limitations: Genetic susceptibility and age are essential; does not show comparable toxicity in healthy humans. affected_machinery: GCDH deficiency_not_equivalent: Nutrient deficiency or normal human lysine intake [zinnanti2006] A diet-induced mouse model for glutaric aciduria type I (2006). https://pubmed.ncbi.nlm.nih.gov/16446282/ DOI: 10.1093/brain/awl009
Complete structured claim and evidence
Where it participates (unsigned role)
FAD-containing human GCDH dehydrogenates glutaryl-CoA through glutaconyl-CoA and decarboxylates it to crotonyl-CoA.
Experimental context and source evidence
- experimental_model
- Human GCDH crystallography and substrate-mechanism analysis
- limitations
- The downstream shared ECHS1/HADH/ACAT1 reactions are separate records; these individual enzyme assays do not measure the full lysine-derived flux in a person.
- organism
- Homo sapiens
- plain_language
- GCDH shortens the lysine-derived carbon chain.
- primary_references
- [fu2004] Crystal Structures of Human Glutaryl-CoA Dehydrogenase with and without an Alternate Substrate: Structural Bases of Dehydrogenation and Decarboxylation Reactions (2004). https://pubs.acs.org/doi/10.1021/bi049290c DOI: 10.1021/bi049290c
- tissue_or_cell_type
- Mitochondrial matrix
L-Lysine: mechanism-first literature curation (2026-09-17) · lines 136–144
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human GCDH crystallography and substrate-mechanism analysis · source_derived_draft · unverified_draft
### gcdh-crotonyl-coa FAD-containing human GCDH dehydrogenates glutaryl-CoA through glutaconyl-CoA and decarboxylates it to crotonyl-CoA. Plain language: GCDH shortens the lysine-derived carbon chain. Condition category: normal organism: Homo sapiens tissue_or_cell_type: Mitochondrial matrix experimental_model: Human GCDH crystallography and substrate-mechanism analysis limitations: The downstream shared ECHS1/HADH/ACAT1 reactions are separate records; these individual enzyme assays do not measure the full lysine-derived flux in a person. [fu2004] Crystal Structures of Human Glutaryl-CoA Dehydrogenase with and without an Alternate Substrate: Structural Bases of Dehydrogenation and Decarboxylation Reactions (2004). https://pubs.acs.org/doi/10.1021/bi049290c DOI: 10.1021/bi049290c
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.