Component

Human mitochondrial glutamyl-tRNA(Gln)

Context-specific entity; species, compartment and exposure are stated on each claim.

4 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. The glutamate-mischarged tRNA(Gln) intermediate bound mitochondrial EF-Tu weakly, supporting exclusion from translation before correction.

    Human mitochondrial glutamyl-tRNA(Gln) → Human mitochondrial elongation factor Tu / TUFM source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human mitochondrial tRNA binding assays.
    limitations
    Weak affinity supports the proposed quality-control mechanism; it does not prove absolute exclusion under every condition.
    nutrient_topic
    L-Glutamate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Glutamate
    plain_language
    Quality control reduces entry of the unfinished intermediate into protein synthesis.
    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 394–400

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human mitochondrial tRNA binding assays. · source_derived_draft · unverified_draft

    ## glutamate-elongation-quality-control Quality control reduces entry of the unfinished intermediate into protein synthesis. The glutamate-mischarged tRNA(Gln) intermediate bound mitochondrial EF-Tu weakly, supporting exclusion from translation before correction. Model: Human mitochondrial tRNA binding assays. Limitations: Weak affinity supports the proposed quality-control mechanism; it does not prove absolute exclusion under every condition. 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

What acts on it

  1. Human mitochondrial glutamyl-tRNA synthetase attached glutamate to mitochondrial tRNA(Gln), generating the intermediate Glu-tRNA(Gln).

    Human mitochondrial glutamyl-tRNA synthetase / EARS2 → Human mitochondrial glutamyl-tRNA(Gln) source_derived_draftungraded
    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)

  1. Recombinant human mtGluRS and GatCAB reconstituted formation of glutaminyl-tRNA(Gln) through the glutamylated intermediate in vitro.

    Human mitochondrial GatCAB amidotransferase → Human mitochondrial glutaminyl-tRNA(Gln) source_derived_draftungraded
    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

  2. Knocking down any human GatCAB subunit caused accumulation of glutamate-charged tRNA(Gln) and impaired respiration.

    Human mitochondrial GatCAB amidotransferase → Respiration in human GatCAB knockdown cells source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary abstract
    experimental_model
    Human-cell siRNA against GatCAB subunits.
    limitations
    Knockdown establishes a machinery dependency, not dietary glutamate or glutamine deficiency.
    nutrient_topic
    L-Glutamate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Glutamate
    plain_language
    Available amino acid cannot replace the missing processing step.
    primary_references
    Biogenesis of glutaminyl-mt tRNAGln in human mitochondria. · 2009 · https://pubmed.ncbi.nlm.nih.gov/19805282/ · DOI 10.1073/pnas.0907602106
    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 386–392

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human-cell siRNA against GatCAB subunits. · source_derived_draft · unverified_draft

    ## glutamate-gatcab-loss Available amino acid cannot replace the missing processing step. Knocking down any human GatCAB subunit caused accumulation of glutamate-charged tRNA(Gln) and impaired respiration. Model: Human-cell siRNA against GatCAB subunits. Limitations: Knockdown establishes a machinery dependency, not dietary glutamate or glutamine deficiency. 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

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