Component

Collagen-bound 5-hydroxylysine residues

Protein-bound site or substrate state, not free dietary L-lysine. Sequence and assay context limit the relationship.

5 recorded relationships. Experimental role, claim status and evidence remain attached to each record.

Read recorded mechanisms Open recursive mind map

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.

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.

Recorded relationships

What acts on it

  1. COLGALT1 transfers galactose from UDP-galactose to collagen hydroxylysine.

    COLGALT1 → Collagen-bound 5-hydroxylysine residues source_derived_draftungraded
    Experimental context and source evidence
    experimental_model
    Recombinant human COLGALT1 with collagen peptides.
    limitations
    This reaction modifies lysine already in a protein. It does not show that extra oral lysine increases the reaction or improves a clinical outcome.
    organism
    Human
    plain_language
    A sugar is attached to a lysine residue that has already been hydroxylated.
    primary_references
    [colgalt1-2025] Molecular structure and enzymatic mechanism of the human collagen hydroxylysine galactosyltransferase GLT25D1/COLGALT1 (2025). https://www.nature.com/articles/s41467-025-59017-5 DOI: 10.1038/s41467-025-59017-5
    tissue_or_cell_type
    Not specified as a whole tissue; see experimental model.

    L-Lysine: mechanism-first literature curation (2026-09-17) · lines 437–445

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human COLGALT1 with collagen peptides. · source_derived_draft · unverified_draft

    ### colgalt1-galactosylation COLGALT1 transfers galactose from UDP-galactose to collagen hydroxylysine. Plain language: A sugar is attached to a lysine residue that has already been hydroxylated. Condition category: normal organism: Human tissue_or_cell_type: Not specified as a whole tissue; see experimental model. experimental_model: Recombinant human COLGALT1 with collagen peptides. limitations: This reaction modifies lysine already in a protein. It does not show that extra oral lysine increases the reaction or improves a clinical outcome. [colgalt1-2025] Molecular structure and enzymatic mechanism of the human collagen hydroxylysine galactosyltransferase GLT25D1/COLGALT1 (2025). https://www.nature.com/articles/s41467-025-59017-5 DOI: 10.1038/s41467-025-59017-5
    Complete structured claim and evidence

  2. Lysyl-oxidase activity can convert collagen hydroxylysine side chains to hydroxyallysine.

    Lysyl oxidase enzyme family → Collagen-bound 5-hydroxylysine residues source_derived_draftungraded
    Experimental context and source evidence
    experimental_model
    LOXL2 assay development with extracellular matrix; family-level reaction context.
    limitations
    This is a reaction-class record; not every hydroxylysine site is an accessible LOX substrate.
    organism
    Mammalian cells/tissues and recombinant LOXL2; see study methods
    plain_language
    Hydroxylated lysines provide a different aldehyde starting point for cross-links.
    primary_references
    [lox-assay-2021] An in situ activity assay for lysyl oxidases (2021). https://pubmed.ncbi.nlm.nih.gov/34226627/
    tissue_or_cell_type
    Not specified as a whole tissue; see experimental model.

    L-Lysine: mechanism-first literature curation (2026-09-17) · lines 477–485

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · LOXL2 assay development with extracellular matrix; family-level reaction context. · source_derived_draft · unverified_draft

    ### lox-hydroxylysine-oxidation Lysyl-oxidase activity can convert collagen hydroxylysine side chains to hydroxyallysine. Plain language: Hydroxylated lysines provide a different aldehyde starting point for cross-links. Condition category: normal organism: Mammalian cells/tissues and recombinant LOXL2; see study methods tissue_or_cell_type: Not specified as a whole tissue; see experimental model. experimental_model: LOXL2 assay development with extracellular matrix; family-level reaction context. limitations: This is a reaction-class record; not every hydroxylysine site is an accessible LOX substrate. [lox-assay-2021] An in situ activity assay for lysyl oxidases (2021). https://pubmed.ncbi.nlm.nih.gov/34226627/
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Mn2+ supports COLGALT1 galactosyltransferase activity; Mg2+ gave lower activity in the reported assay.

    Mn2+ → COLGALT1 source_derived_draftungraded
    Experimental context and source evidence
    experimental_model
    Purified human COLGALT1 metal-substitution assays.
    limitations
    Metal dependence does not establish which nutrient is limiting in a person; magnesium is not claimed universally inactive.
    organism
    Human
    plain_language
    Manganese is a catalytic partner for this collagen-sugar enzyme.
    primary_references
    [colgalt1-2025] Molecular structure and enzymatic mechanism of the human collagen hydroxylysine galactosyltransferase GLT25D1/COLGALT1 (2025). https://www.nature.com/articles/s41467-025-59017-5 DOI: 10.1038/s41467-025-59017-5
    tissue_or_cell_type
    Not specified as a whole tissue; see experimental model.

    L-Lysine: mechanism-first literature curation (2026-09-17) · lines 447–455

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified human COLGALT1 metal-substitution assays. · source_derived_draft · unverified_draft

    ### manganese-colgalt1 Mn2+ supports COLGALT1 galactosyltransferase activity; Mg2+ gave lower activity in the reported assay. Plain language: Manganese is a catalytic partner for this collagen-sugar enzyme. Condition category: normal organism: Human tissue_or_cell_type: Not specified as a whole tissue; see experimental model. experimental_model: Purified human COLGALT1 metal-substitution assays. limitations: Metal dependence does not establish which nutrient is limiting in a person; magnesium is not claimed universally inactive. [colgalt1-2025] Molecular structure and enzymatic mechanism of the human collagen hydroxylysine galactosyltransferase GLT25D1/COLGALT1 (2025). https://www.nature.com/articles/s41467-025-59017-5 DOI: 10.1038/s41467-025-59017-5
    Complete structured claim and evidence

  2. PLOD1 hydroxylates selected collagen-bound lysine residues to hydroxylysine.

    PLOD1 → Collagen-bound lysine residues source_derived_draftungraded
    Experimental context and source evidence
    experimental_model
    Human lysyl hydroxylase characterization.
    limitations
    This reaction modifies lysine already in a protein. It does not show that extra oral lysine increases the reaction or improves a clinical outcome.
    organism
    Human
    plain_language
    An enzyme adds a hydroxyl group to selected lysines in collagen.
    primary_references
    [plod1-1992] Cloning of human lysyl hydroxylase: complete cDNA-derived amino acid sequence and assignment of the gene (PLOD) to chromosome 1p36.3--p36.2 (1992). https://pubmed.ncbi.nlm.nih.gov/1577494/ DOI: 10.1016/0888-7543(92)90202-4
    tissue_or_cell_type
    Not specified as a whole tissue; see experimental model.

    L-Lysine: mechanism-first literature curation (2026-09-17) · lines 387–395

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human lysyl hydroxylase characterization. · source_derived_draft · unverified_draft

    ### plod1-collagen-hydroxylation PLOD1 hydroxylates selected collagen-bound lysine residues to hydroxylysine. Plain language: An enzyme adds a hydroxyl group to selected lysines in collagen. Condition category: normal organism: Human tissue_or_cell_type: Not specified as a whole tissue; see experimental model. experimental_model: Human lysyl hydroxylase characterization. limitations: This reaction modifies lysine already in a protein. It does not show that extra oral lysine increases the reaction or improves a clinical outcome. [plod1-1992] Cloning of human lysyl hydroxylase: complete cDNA-derived amino acid sequence and assignment of the gene (PLOD) to chromosome 1p36.3--p36.2 (1992). https://pubmed.ncbi.nlm.nih.gov/1577494/ DOI: 10.1016/0888-7543(92)90202-4
    Complete structured claim and evidence

  3. PLOD3 hydroxylates peptidyl lysine using Fe(II), 2-oxoglutarate and oxygen.

    PLOD3 → Collagen-bound lysine residues source_derived_draftungraded
    Experimental context and source evidence
    experimental_model
    Recombinant human PLOD3 structural and biochemical assays.
    limitations
    This reaction modifies lysine already in a protein. It does not show that extra oral lysine increases the reaction or improves a clinical outcome.
    organism
    Human
    plain_language
    The collagen enzyme needs an iron-containing catalytic site and reaction partners.
    primary_references
    [plod3-2018] Molecular architecture of the multifunctional collagen lysyl hydroxylase and glycosyltransferase LH3 (2018). https://www.nature.com/articles/s41467-018-05631-5 DOI: 10.1038/s41467-018-05631-5
    tissue_or_cell_type
    Not specified as a whole tissue; see experimental model.

    L-Lysine: mechanism-first literature curation (2026-09-17) · lines 417–425

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human PLOD3 structural and biochemical assays. · source_derived_draft · unverified_draft

    ### plod3-collagen-hydroxylation PLOD3 hydroxylates peptidyl lysine using Fe(II), 2-oxoglutarate and oxygen. Plain language: The collagen enzyme needs an iron-containing catalytic site and reaction partners. Condition category: normal organism: Human tissue_or_cell_type: Not specified as a whole tissue; see experimental model. experimental_model: Recombinant human PLOD3 structural and biochemical assays. limitations: This reaction modifies lysine already in a protein. It does not show that extra oral lysine increases the reaction or improves a clinical outcome. [plod3-2018] Molecular architecture of the multifunctional collagen lysyl hydroxylase and glycosyltransferase LH3 (2018). https://www.nature.com/articles/s41467-018-05631-5 DOI: 10.1038/s41467-018-05631-5
    Complete structured claim and evidence

In the sources

Preserved passages that mention this component, quoted exactly. Open one to read it in context.

    This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.

    Evidence, AI assistance and curation standards