Component

COLGALT1

Independent protein record; interpretation is limited by each linked claim and its study context.

4 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 it acts on

  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

What acts on it

  1. The COLGALT1 GT2 catalytic site contains a Glu-Asp-Asp motif important for manganese binding.

    Mn2+ → COLGALT1 source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    UDP-galactose (donor_substrate)
    evidence_span
    {"source_cache": "artifacts/manganese-glycosylation-sources/colgalt2025.abstract.txt", "locator": "Indexed primary abstract", "file_sha256": "5a42e5928c56f4e312768d79c9a5601b6f9e76a44bcdd9ede4bc8ea0c8985b60", "start_char": 0, "end_char": 1331, "text_sha256": "5a42e5928c56f4e312768d79c9a5601b6f9e76a44bcdd9ede4bc8ea0c8985b60", "text_characters": 1331}
    experimental_model
    Human COLGALT1 structural and biochemical assays
    exposure
    Metal substitution and structural-domain comparisons.
    limitations
    Modification of collagen-bound hydroxylysine does not establish that extra dietary manganese or free lysine improves collagen in a person.
    nutrient_topic
    Manganese research collection; topical membership is not evidence of a direct dietary effect. · Manganese
    organism
    Homo sapiens
    plain_language
    The collagen sugar-transfer reaction has a defined manganese-binding site.
    primary_references
    [mn-gly-colgalt2025] Molecular structure and enzymatic mechanism of the human collagen hydroxylysine galactosyltransferase GLT25D1/COLGALT1. (2025). https://pubmed.ncbi.nlm.nih.gov/40240392/ DOI: 10.1038/s41467-025-59017-5
    tissue_or_cell_type
    Purified protein and collagen peptides

    Manganese: enzyme cofactors, glycosylation, transport and nutrient interactions (2026-09-17) · lines 908–920

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human COLGALT1 structural and biochemical assays · source_derived_draft · unverified_draft

    ### mn-gly-colgalt-gt2-metal The COLGALT1 GT2 catalytic site contains a Glu-Asp-Asp motif important for manganese binding. Condition category: normal nutrient_topic: Manganese research collection; topical membership is not evidence of a direct dietary effect. plain_language: The collagen sugar-transfer reaction has a defined manganese-binding site. organism: Homo sapiens tissue_or_cell_type: Purified protein and collagen peptides experimental_model: Human COLGALT1 structural and biochemical assays limitations: Modification of collagen-bound hydroxylysine does not establish that extra dietary manganese or free lysine improves collagen in a person. exposure: Metal substitution and structural-domain comparisons. cross_nutrient: UDP-galactose (donor_substrate) evidence_span: {"source_cache": "artifacts/manganese-glycosylation-sources/colgalt2025.abstract.txt", "locator": "Indexed primary abstract", "file_sha256": "5a42e5928c56f4e312768d79c9a5601b6f9e76a44bcdd9ede4bc8ea0c8985b60", "start_char": 0, "end_char": 1331, "text_sha256": "5a42e5928c56f4e312768d79c9a5601b6f9e76a44bcdd9ede4bc8ea0c8985b60", "text_characters": 1331} [mn-gly-colgalt2025] Molecular structure and enzymatic mechanism of the human collagen hydroxylysine galactosyltransferase GLT25D1/COLGALT1. (2025). https://pubmed.ncbi.nlm.nih.gov/40240392/ DOI: 10.1038/s41467-025-59017-5
    Complete structured claim and evidence

  2. 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

Where it participates (unsigned role)

  1. Calcium and UDP-galactose bound in COLGALT1’s noncatalytic GT1 domain contribute to folding stability.

    Calcium ion → COLGALT1 folding stability source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    COLGALT1 (affected_protein); UDP-galactose (stabilizing_ligand); Manganese(II) ion (distinct_catalytic_ion)
    evidence_span
    {"source_cache": "artifacts/manganese-glycosylation-sources/colgalt2025.abstract.txt", "locator": "Indexed primary abstract", "file_sha256": "5a42e5928c56f4e312768d79c9a5601b6f9e76a44bcdd9ede4bc8ea0c8985b60", "start_char": 0, "end_char": 1331, "text_sha256": "5a42e5928c56f4e312768d79c9a5601b6f9e76a44bcdd9ede4bc8ea0c8985b60", "text_characters": 1331}
    experimental_model
    Human COLGALT1 structural and biochemical assays
    exposure
    Metal substitution and structural-domain comparisons.
    limitations
    Modification of collagen-bound hydroxylysine does not establish that extra dietary manganese or free lysine improves collagen in a person.
    nutrient_topic
    Manganese research collection; topical membership is not evidence of a direct dietary effect. · Manganese
    organism
    Homo sapiens
    plain_language
    Calcium and the donor sugar also help stabilize a separate part of this manganese enzyme.
    primary_references
    [mn-gly-colgalt2025] Molecular structure and enzymatic mechanism of the human collagen hydroxylysine galactosyltransferase GLT25D1/COLGALT1. (2025). https://pubmed.ncbi.nlm.nih.gov/40240392/ DOI: 10.1038/s41467-025-59017-5
    tissue_or_cell_type
    Purified protein and collagen peptides

    Manganese: enzyme cofactors, glycosylation, transport and nutrient interactions (2026-09-17) · lines 922–934

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human COLGALT1 structural and biochemical assays · source_derived_draft · unverified_draft

    ### mn-gly-colgalt-gt1-stability Calcium and UDP-galactose bound in COLGALT1’s noncatalytic GT1 domain contribute to folding stability. Condition category: normal nutrient_topic: Manganese research collection; topical membership is not evidence of a direct dietary effect. plain_language: Calcium and the donor sugar also help stabilize a separate part of this manganese enzyme. organism: Homo sapiens tissue_or_cell_type: Purified protein and collagen peptides experimental_model: Human COLGALT1 structural and biochemical assays limitations: Modification of collagen-bound hydroxylysine does not establish that extra dietary manganese or free lysine improves collagen in a person. exposure: Metal substitution and structural-domain comparisons. cross_nutrient: COLGALT1 (affected_protein); UDP-galactose (stabilizing_ligand); Manganese(II) ion (distinct_catalytic_ion) evidence_span: {"source_cache": "artifacts/manganese-glycosylation-sources/colgalt2025.abstract.txt", "locator": "Indexed primary abstract", "file_sha256": "5a42e5928c56f4e312768d79c9a5601b6f9e76a44bcdd9ede4bc8ea0c8985b60", "start_char": 0, "end_char": 1331, "text_sha256": "5a42e5928c56f4e312768d79c9a5601b6f9e76a44bcdd9ede4bc8ea0c8985b60", "text_characters": 1331} [mn-gly-colgalt2025] Molecular structure and enzymatic mechanism of the human collagen hydroxylysine galactosyltransferase GLT25D1/COLGALT1. (2025). https://pubmed.ncbi.nlm.nih.gov/40240392/ DOI: 10.1038/s41467-025-59017-5
    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