Component
Human glutamyl-prolyl-tRNA synthetase / EPRS1
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 it acts on
The prolyl-tRNA synthetase domain of human EPRS attaches proline to its cognate tRNA in an ATP-dependent aminoacylation reaction.
Experimental context and source evidence
- evidence_access
- Primary full text
- experimental_model
- Purified human EPRS/ProRS biochemical assays.
- limitations
- tRNA charging and collagen hydroxylation are separate enzyme steps.
- nutrient_topic
- L-Proline collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Proline
- plain_language
- A protein-building block must first be loaded onto the correct tRNA.
- primary_references
- Halofuginone and other febrifugine derivatives inhibit prolyl-tRNA synthetase. · 2012 · https://pubmed.ncbi.nlm.nih.gov/22327401/ · DOI 10.1038/nchembio.790
L-Proline: synthesis, collagen processing, redox metabolism and cross-nutrient mechanisms (2026-09-19) · lines 222–228
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Purified human EPRS/ProRS biochemical assays. · source_derived_draft · unverified_draft
## l-proline-eprs-charging A protein-building block must first be loaded onto the correct tRNA. The prolyl-tRNA synthetase domain of human EPRS attaches proline to its cognate tRNA in an ATP-dependent aminoacylation reaction. Model: Purified human EPRS/ProRS biochemical assays. Limitations: tRNA charging and collagen hydroxylation are separate enzyme steps. Evidence access: Primary full text Halofuginone and other febrifugine derivatives inhibit prolyl-tRNA synthetase. · 2012 · https://pubmed.ncbi.nlm.nih.gov/22327401/ · DOI 10.1038/nchembio.790
Complete structured claim and evidence
What acts on it
Halofuginone inhibited the prolyl-tRNA synthetase activity of EPRS by competing with proline; added proline or enzyme reversed inhibition in the tested systems.
Experimental context and source evidence
- availability_state
- machinery_impairment Imported condition classification; unverified.
- evidence_access
- Primary full text
- experimental_model
- Biochemical charging assays and mammalian-cell experiments.
- limitations
- This is pharmacological machinery inhibition, not a claim that halofuginone physically removes all cellular proline.
- nutrient_topic
- L-Proline collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Proline
- plain_language
- Blocking the loading enzyme can mimic a shortage even while proline is present.
- primary_references
- Halofuginone and other febrifugine derivatives inhibit prolyl-tRNA synthetase. · 2012 · https://pubmed.ncbi.nlm.nih.gov/22327401/ · DOI 10.1038/nchembio.790
- trigger_kind
- machinery_impairment Imported condition classification; unverified.
L-Proline: synthesis, collagen processing, redox metabolism and cross-nutrient mechanisms (2026-09-19) · lines 230–236
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Biochemical charging assays and mammalian-cell experiments. · source_derived_draft · unverified_draft
## l-proline-eprs-inhibition Blocking the loading enzyme can mimic a shortage even while proline is present. Halofuginone inhibited the prolyl-tRNA synthetase activity of EPRS by competing with proline; added proline or enzyme reversed inhibition in the tested systems. Model: Biochemical charging assays and mammalian-cell experiments. Limitations: This is pharmacological machinery inhibition, not a claim that halofuginone physically removes all cellular proline. Evidence access: Primary full text Halofuginone and other febrifugine derivatives inhibit prolyl-tRNA synthetase. · 2012 · https://pubmed.ncbi.nlm.nih.gov/22327401/ · DOI 10.1038/nchembio.790
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.