Component
LOX
Independent protein record; interpretation is limited by each linked claim and its study context.
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
Expressed LOX Ser280Arg and Ser348Arg variants had lower catalytic activity than wild-type LOX.
Experimental context and source evidence
- availability_state
- machinery_impairment Imported condition classification; unverified.
- experimental_model
- Human-family genetic study with expressed mutant-enzyme assays.
- limitations
- Variant-specific activity measurements; free lysine was not shown to rescue the defect.
- organism
- Human
- plain_language
- Some inherited enzyme changes reduce activity despite the presence of lysine substrates.
- primary_references
- [lox-variants-2016] LOX Mutations Predispose to Thoracic Aortic Aneurysms and Dissections (2016). https://pubmed.ncbi.nlm.nih.gov/26838787/ DOI: 10.1161/CIRCRESAHA.115.307130
- tissue_or_cell_type
- Not specified as a whole tissue; see experimental model.
- trigger_kind
- machinery_impairment Imported condition classification; unverified.
L-Lysine: mechanism-first literature curation (2026-09-17) · lines 517–525
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human-family genetic study with expressed mutant-enzyme assays. · source_derived_draft · unverified_draft
### lox-variants-enzyme-activity Expressed LOX Ser280Arg and Ser348Arg variants had lower catalytic activity than wild-type LOX. Plain language: Some inherited enzyme changes reduce activity despite the presence of lysine substrates. Condition category: machinery_impairment organism: Human tissue_or_cell_type: Not specified as a whole tissue; see experimental model. experimental_model: Human-family genetic study with expressed mutant-enzyme assays. limitations: Variant-specific activity measurements; free lysine was not shown to rescue the defect. [lox-variants-2016] LOX Mutations Predispose to Thoracic Aortic Aneurysms and Dissections (2016). https://pubmed.ncbi.nlm.nih.gov/26838787/ DOI: 10.1161/CIRCRESAHA.115.307130
Complete structured claim and evidence
What acts on it
A protein-derived lysine-tyrosylquinone cofactor was identified in bovine aortic lysyl oxidase.
Experimental context and source evidence
- experimental_model
- Bovine aortic enzyme sequencing, mass spectrometry and spectroscopy.
- limitations
- This protein-bound cofactor is neither a vitamin nor free lysine, and the experiment did not test dietary supplementation.
- organism
- Cattle
- plain_language
- Two amino-acid side chains in the enzyme form part of its catalytic machinery.
- primary_references
- [lox-ltq-1996] A crosslinked cofactor in lysyl oxidase: redox function for amino acid side chains (1996). https://pubmed.ncbi.nlm.nih.gov/8688089/ DOI: 10.1126/science.273.5278.1078
- tissue_or_cell_type
- Not specified as a whole tissue; see experimental model.
L-Lysine: mechanism-first literature curation (2026-09-17) · lines 487–495
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Bovine aortic enzyme sequencing, mass spectrometry and spectroscopy. · source_derived_draft · unverified_draft
### lox-ltq-cofactor A protein-derived lysine-tyrosylquinone cofactor was identified in bovine aortic lysyl oxidase. Plain language: Two amino-acid side chains in the enzyme form part of its catalytic machinery. Condition category: normal organism: Cattle tissue_or_cell_type: Not specified as a whole tissue; see experimental model. experimental_model: Bovine aortic enzyme sequencing, mass spectrometry and spectroscopy. limitations: This protein-bound cofactor is neither a vitamin nor free lysine, and the experiment did not test dietary supplementation. [lox-ltq-1996] A crosslinked cofactor in lysyl oxidase: redox function for amino acid side chains (1996). https://pubmed.ncbi.nlm.nih.gov/8688089/ DOI: 10.1126/science.273.5278.1078
Complete structured claim and evidence
Where it participates (unsigned role)
Dietary copper availability altered tendon lysyl-oxidase activation in the chick experiments.
Experimental context and source evidence
- availability_state
- nutrient_deficiency Imported condition classification; unverified.
- experimental_model
- Chicks receiving diets differing in copper; tendon enzyme assays.
- limitations
- Copper manipulation in chicks, not evidence of dietary lysine deficiency or a human copper/lysine dose recommendation.
- organism
- Chicken
- plain_language
- Insufficient copper can limit a lysine-processing enzyme even when its substrate is present.
- primary_references
- [lox-copper-1999] Activation of chick tendon lysyl oxidase in response to dietary copper (1999). https://pubmed.ncbi.nlm.nih.gov/10573541/
- tissue_or_cell_type
- Tendon
- trigger_kind
- nutrient_deficiency Imported condition classification; unverified.
L-Lysine: mechanism-first literature curation (2026-09-17) · lines 497–505
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Chicks receiving diets differing in copper; tendon enzyme assays. · source_derived_draft · unverified_draft
### copper-insufficiency-lox Dietary copper availability altered tendon lysyl-oxidase activation in the chick experiments. Plain language: Insufficient copper can limit a lysine-processing enzyme even when its substrate is present. Condition category: nutrient_deficiency organism: Chicken tissue_or_cell_type: Tendon experimental_model: Chicks receiving diets differing in copper; tendon enzyme assays. limitations: Copper manipulation in chicks, not evidence of dietary lysine deficiency or a human copper/lysine dose recommendation. [lox-copper-1999] Activation of chick tendon lysyl oxidase in response to dietary copper (1999). https://pubmed.ncbi.nlm.nih.gov/10573541/
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.