Component
Lysyl-tRNA synthetase / KARS1
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.
Where it participates (unsigned role)
KARS1 activates lysine with ATP, forming enzyme-bound lysyl-adenylate and releasing pyrophosphate.
Experimental context and source evidence
- experimental_model
- Human LysRS cryo-EM and aminoacylation assays
- limitations
- The structural experiment used tRNA-Lys3; KARS1 is not the leucyl-tRNA synthetase LARS1.
- organism
- Homo sapiens
- plain_language
- ATP activates lysine before it is attached to its carrier RNA.
- primary_references
- [devarkar2025] Structural basis for aminoacylation of cellular modified tRNALys3 by human lysyl-tRNA synthetase (2025). https://pubmed.ncbi.nlm.nih.gov/40036503/ DOI: 10.1093/nar/gkaf114
- tissue_or_cell_type
- Cytosolic tRNA charging
L-Lysine: mechanism-first literature curation (2026-09-17) · lines 54–62
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human LysRS cryo-EM and aminoacylation assays · source_derived_draft · unverified_draft
### lysine-adenylation KARS1 activates lysine with ATP, forming enzyme-bound lysyl-adenylate and releasing pyrophosphate. Plain language: ATP activates lysine before it is attached to its carrier RNA. Condition category: normal organism: Homo sapiens tissue_or_cell_type: Cytosolic tRNA charging experimental_model: Human LysRS cryo-EM and aminoacylation assays limitations: The structural experiment used tRNA-Lys3; KARS1 is not the leucyl-tRNA synthetase LARS1. [devarkar2025] Structural basis for aminoacylation of cellular modified tRNALys3 by human lysyl-tRNA synthetase (2025). https://pubmed.ncbi.nlm.nih.gov/40036503/ DOI: 10.1093/nar/gkaf114
Complete structured claim and evidenceAfter pyrophosphate release, KARS1 transfers activated lysine to the tRNA-Lys 3-prime end, forming lysyl-tRNA and AMP.
Experimental context and source evidence
- experimental_model
- Human LysRS-tRNA-Lys3 structural and enzyme assays
- limitations
- This is tRNA charging; subsequent ribosomal peptide-bond formation is a distinct step.
- organism
- Homo sapiens
- plain_language
- Charged tRNA supplies lysine for protein synthesis.
- primary_references
- [devarkar2025] Structural basis for aminoacylation of cellular modified tRNALys3 by human lysyl-tRNA synthetase (2025). https://pubmed.ncbi.nlm.nih.gov/40036503/ DOI: 10.1093/nar/gkaf114
- tissue_or_cell_type
- Cytosolic translation machinery
L-Lysine: mechanism-first literature curation (2026-09-17) · lines 64–72
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human LysRS-tRNA-Lys3 structural and enzyme assays · source_derived_draft · unverified_draft
### lysyl-trna-formation After pyrophosphate release, KARS1 transfers activated lysine to the tRNA-Lys 3-prime end, forming lysyl-tRNA and AMP. Plain language: Charged tRNA supplies lysine for protein synthesis. Condition category: normal organism: Homo sapiens tissue_or_cell_type: Cytosolic translation machinery experimental_model: Human LysRS-tRNA-Lys3 structural and enzyme assays limitations: This is tRNA charging; subsequent ribosomal peptide-bond formation is a distinct step. [devarkar2025] Structural basis for aminoacylation of cellular modified tRNALys3 by human lysyl-tRNA synthetase (2025). https://pubmed.ncbi.nlm.nih.gov/40036503/ DOI: 10.1093/nar/gkaf114
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.