Component
Collagen lysyl hydroxylase family
Independent protein family 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.
What acts on it
Ascorbate supports sustained lysyl-hydroxylase activity; the enzyme can initially turn over without ascorbate.
Experimental context and source evidence
- experimental_model
- Purified chick-embryo enzyme kinetics.
- limitations
- Family-level enzyme preparation, not a human PLOD isoform comparison or lysine-supplement trial.
- organism
- Chicken
- plain_language
- Vitamin C supports the reaction, but is not consumed in every coupled turnover.
- primary_references
- [plod-cofactor-1980] Studies on the lysyl hydroxylase reaction. I. Initial velocity kinetics and related aspects. (1980). https://pubmed.ncbi.nlm.nih.gov/6766066/ DOI: 10.1016/0005-2744(80)90040-6
- tissue_or_cell_type
- Not specified as a whole tissue; see experimental model.
L-Lysine: mechanism-first literature curation (2026-09-17) · lines 427–435
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified chick-embryo enzyme kinetics. · source_derived_draft · unverified_draft
### ascorbate-lysyl-hydroxylase Ascorbate supports sustained lysyl-hydroxylase activity; the enzyme can initially turn over without ascorbate. Plain language: Vitamin C supports the reaction, but is not consumed in every coupled turnover. Condition category: normal organism: Chicken tissue_or_cell_type: Not specified as a whole tissue; see experimental model. experimental_model: Purified chick-embryo enzyme kinetics. limitations: Family-level enzyme preparation, not a human PLOD isoform comparison or lysine-supplement trial. [plod-cofactor-1980] Studies on the lysyl hydroxylase reaction. I. Initial velocity kinetics and related aspects. (1980). https://pubmed.ncbi.nlm.nih.gov/6766066/ DOI: 10.1016/0005-2744(80)90040-6
Complete structured claim and evidence
Where it participates (unsigned role)
Human skin fibroblast lysyl hydroxylase activity increased approximately threefold after the study ascorbate treatment.
Experimental context and source evidence
- cross_nutrient
- Vitamin C chemistry in collagen, modified-lysine/carnitine metabolism or copper-dependent peptide/catecholamine processing.
- experimental_model
- Cultured human skin fibroblasts
- exposure
- Prolonged ascorbate exposure versus no added ascorbate; exact culture concentration not verified in accessible abstract.
- limitations
- Activity assay does not resolve human PLOD isoforms or distinguish all possible expression/stability effects.
- nutrient_topic
- Vitamin C research collection; topical membership is not evidence of a direct dietary effect. · Vitamin C
- organism
- Homo sapiens
- plain_language
- Vitamin C also changed the amount of lysyl hydroxylase activity measured in these cells.
- primary_references
- [collagen1981] Regulation of collagen synthesis by ascorbic acid. (1981). https://pubmed.ncbi.nlm.nih.gov/6265920/ DOI: 10.1073/pnas.78.5.2879
- tissue_or_cell_type
- Skin fibroblasts
Vitamin C: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 663–674
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Cultured human skin fibroblasts · source_derived_draft · unverified_draft
### vc-enzyme-fibroblast-lysyl-activity Human skin fibroblast lysyl hydroxylase activity increased approximately threefold after the study ascorbate treatment. Condition category: normal nutrient_topic: Vitamin C research collection; topical membership is not evidence of a direct dietary effect. plain_language: Vitamin C also changed the amount of lysyl hydroxylase activity measured in these cells. organism: Homo sapiens tissue_or_cell_type: Skin fibroblasts experimental_model: Cultured human skin fibroblasts limitations: Activity assay does not resolve human PLOD isoforms or distinguish all possible expression/stability effects. cross_nutrient: Vitamin C chemistry in collagen, modified-lysine/carnitine metabolism or copper-dependent peptide/catecholamine processing. exposure: Prolonged ascorbate exposure versus no added ascorbate; exact culture concentration not verified in accessible abstract. [collagen1981] Regulation of collagen synthesis by ascorbic acid. (1981). https://pubmed.ncbi.nlm.nih.gov/6265920/ DOI: 10.1073/pnas.78.5.2879
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.