Component
Human mitochondrial Tyr-tRNA Tyr
Context-specific entity; species, compartment and exposure are stated on each claim.
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 acts on it
Recombinant human YARS2 supported tyrosyl-tRNA aminoacylation; the F52L variant retained activity with abnormal kinetics.
Experimental context and source evidence
- evidence_access
- Primary abstract
- experimental_model
- Wild-type and F52L human enzyme aminoacylation assays.
- limitations
- Retained activity does not mean normal function; this does not establish a tyrosine-rescue dose.
- nutrient_topic
- L-Tyrosine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Tyrosine
- plain_language
- Mitochondria use a separate tyrosine-loading enzyme.
- primary_references
- Mutation of the mitochondrial tyrosyl-tRNA synthetase gene, YARS2, causes myopathy, lactic acidosis, and sideroblastic anemia--MLASA syndrome. · 2010 · https://pubmed.ncbi.nlm.nih.gov/20598274/ · DOI 10.1016/j.ajhg.2010.06.001
L-Tyrosine: catecholamines, thyroid chemistry, pigment, metabolism and cross-nutrient mechanisms (2026-09-19) · lines 76–82
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Wild-type and F52L human enzyme aminoacylation assays. · source_derived_draft · unverified_draft
## l-tyrosine-yars2-charging Mitochondria use a separate tyrosine-loading enzyme. Recombinant human YARS2 supported tyrosyl-tRNA aminoacylation; the F52L variant retained activity with abnormal kinetics. Model: Wild-type and F52L human enzyme aminoacylation assays. Limitations: Retained activity does not mean normal function; this does not establish a tyrosine-rescue dose. Evidence access: Primary abstract Mutation of the mitochondrial tyrosyl-tRNA synthetase gene, YARS2, causes myopathy, lactic acidosis, and sideroblastic anemia--MLASA syndrome. · 2010 · https://pubmed.ncbi.nlm.nih.gov/20598274/ · DOI 10.1016/j.ajhg.2010.06.001
Complete structured claim and evidence
Where it participates (unsigned role)
YARS2 F52L patient-derived myotubes had reduced synthesis of respiratory-chain subunits, with respiratory complex I, III and IV dysfunction in affected tissue.
Experimental context and source evidence
- availability_state
- machinery_impairment Imported condition classification; unverified.
- evidence_access
- Primary abstract
- experimental_model
- Human MLASA families; skeletal muscle, fibroblasts and derived myotubes.
- limitations
- Fibroblasts were relatively spared, so the defect cannot be assigned one universal cellular severity.
- nutrient_topic
- L-Tyrosine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Tyrosine
- plain_language
- A processing defect can cause an energy problem despite an available amino acid.
- primary_references
- Mutation of the mitochondrial tyrosyl-tRNA synthetase gene, YARS2, causes myopathy, lactic acidosis, and sideroblastic anemia--MLASA syndrome. · 2010 · https://pubmed.ncbi.nlm.nih.gov/20598274/ · DOI 10.1016/j.ajhg.2010.06.001
- trigger_kind
- machinery_impairment Imported condition classification; unverified.
L-Tyrosine: catecholamines, thyroid chemistry, pigment, metabolism and cross-nutrient mechanisms (2026-09-19) · lines 84–90
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human MLASA families; skeletal muscle, fibroblasts and derived myotubes. · source_derived_draft · unverified_draft
## l-tyrosine-yars2-defect A processing defect can cause an energy problem despite an available amino acid. YARS2 F52L patient-derived myotubes had reduced synthesis of respiratory-chain subunits, with respiratory complex I, III and IV dysfunction in affected tissue. Model: Human MLASA families; skeletal muscle, fibroblasts and derived myotubes. Limitations: Fibroblasts were relatively spared, so the defect cannot be assigned one universal cellular severity. Evidence access: Primary abstract Mutation of the mitochondrial tyrosyl-tRNA synthetase gene, YARS2, causes myopathy, lactic acidosis, and sideroblastic anemia--MLASA syndrome. · 2010 · https://pubmed.ncbi.nlm.nih.gov/20598274/ · DOI 10.1016/j.ajhg.2010.06.001
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.