Component
Human mitochondrial glutamyl-tRNA synthetase / EARS2
Context-specific entity; species, compartment and exposure are stated on each claim.
3 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
Human mitochondrial glutamyl-tRNA synthetase attached glutamate to mitochondrial tRNA(Gln), generating the intermediate Glu-tRNA(Gln).
Experimental context and source evidence
- evidence_access
- Primary abstract
- experimental_model
- Recombinant human enzyme and mitochondrial tRNA biochemistry.
- limitations
- This intermediate is not glutamate being correctly incorporated at glutamine codons.
- nutrient_topic
- L-Glutamate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Glutamate
- plain_language
- A deliberately intermediate amino-acid attachment must be processed before translation.
- primary_references
- Biogenesis of glutaminyl-mt tRNAGln in human mitochondria. · 2009 · https://pubmed.ncbi.nlm.nih.gov/19805282/ · DOI 10.1073/pnas.0907602106
L-Glutamate / L-glutamic acid: carbon and nitrogen allocation, signaling and cross-nutrient mechanisms (2026-09-19) · lines 370–376
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Recombinant human enzyme and mitochondrial tRNA biochemistry. · source_derived_draft · unverified_draft
## glutamate-ears2-intermediate A deliberately intermediate amino-acid attachment must be processed before translation. Human mitochondrial glutamyl-tRNA synthetase attached glutamate to mitochondrial tRNA(Gln), generating the intermediate Glu-tRNA(Gln). Model: Recombinant human enzyme and mitochondrial tRNA biochemistry. Limitations: This intermediate is not glutamate being correctly incorporated at glutamine codons. Evidence access: Primary abstract Biogenesis of glutaminyl-mt tRNAGln in human mitochondria. · 2009 · https://pubmed.ncbi.nlm.nih.gov/19805282/ · DOI 10.1073/pnas.0907602106
Complete structured claim and evidence
Where it participates (unsigned role)
Patient fibroblasts with EARS2 p.G317C had broad metabolic abnormalities; reconstitution with wild-type versus disease variants distinguished severity-related TCA and amino-acid signatures.
Experimental context and source evidence
- availability_state
- machinery_impairment Imported condition classification; unverified.
- evidence_access
- Primary full text
- experimental_model
- Human neonatal case, primary fibroblasts and variant reconstitution/metabolomics.
- limitations
- Patient-derived cells and rescue constructs are not dietary supplementation experiments.
- nutrient_topic
- L-Glutamate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Glutamate
- plain_language
- A glutamate-handling translation enzyme can affect many downstream metabolic pools.
- primary_references
- Metabolic impact of pathogenic variants in the mitochondrial glutamyl-tRNA synthetase EARS2. · 2021 · https://pubmed.ncbi.nlm.nih.gov/33855712/ · DOI 10.1002/jimd.12387
- trigger_kind
- machinery_impairment Imported condition classification; unverified.
L-Glutamate / L-glutamic acid: carbon and nitrogen allocation, signaling and cross-nutrient mechanisms (2026-09-19) · lines 402–408
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human neonatal case, primary fibroblasts and variant reconstitution/metabolomics. · source_derived_draft · unverified_draft
## glutamate-ears2-disease-metabolism A glutamate-handling translation enzyme can affect many downstream metabolic pools. Patient fibroblasts with EARS2 p.G317C had broad metabolic abnormalities; reconstitution with wild-type versus disease variants distinguished severity-related TCA and amino-acid signatures. Model: Human neonatal case, primary fibroblasts and variant reconstitution/metabolomics. Limitations: Patient-derived cells and rescue constructs are not dietary supplementation experiments. Evidence access: Primary full text Metabolic impact of pathogenic variants in the mitochondrial glutamyl-tRNA synthetase EARS2. · 2021 · https://pubmed.ncbi.nlm.nih.gov/33855712/ · DOI 10.1002/jimd.12387
Complete structured claim and evidenceRecombinant human mtGluRS and GatCAB reconstituted formation of glutaminyl-tRNA(Gln) through the glutamylated intermediate in vitro.
Experimental context and source evidence
- evidence_access
- Primary abstract
- experimental_model
- Human recombinant mitochondrial tRNA pathway reconstitution.
- limitations
- Each complex subunit is separately modeled; an amino acid supplement was not the tested intervention.
- nutrient_topic
- L-Glutamate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Glutamate
- plain_language
- A second enzyme complex converts the attached amino acid to the required one.
- primary_references
- Biogenesis of glutaminyl-mt tRNAGln in human mitochondria. · 2009 · https://pubmed.ncbi.nlm.nih.gov/19805282/ · DOI 10.1073/pnas.0907602106
L-Glutamate / L-glutamic acid: carbon and nitrogen allocation, signaling and cross-nutrient mechanisms (2026-09-19) · lines 378–384
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human recombinant mitochondrial tRNA pathway reconstitution. · source_derived_draft · unverified_draft
## glutamate-gatcab-conversion A second enzyme complex converts the attached amino acid to the required one. Recombinant human mtGluRS and GatCAB reconstituted formation of glutaminyl-tRNA(Gln) through the glutamylated intermediate in vitro. Model: Human recombinant mitochondrial tRNA pathway reconstitution. Limitations: Each complex subunit is separately modeled; an amino acid supplement was not the tested intervention. Evidence access: Primary abstract Biogenesis of glutaminyl-mt tRNAGln in human mitochondria. · 2009 · https://pubmed.ncbi.nlm.nih.gov/19805282/ · DOI 10.1073/pnas.0907602106
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.