Component

Dansyl-Tyr-Val-alpha-hydroxyglycine

Fluorescent alpha-hydroxyglycine intermediate used to isolate PAL activity.

1 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.

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

Where it participates (unsigned role)

  1. Under conditions that inactivated hydroxylase-dependent rat PAM amidation, ascorbate did not impair conversion of the pre-hydroxylated dansyl-Tyr-Val-alpha-hydroxyglycine intermediate to its amide.

    Experimental context and source evidence
    cross_nutrient
    Vitamin C chemistry in collagen, modified-lysine/carnitine metabolism or copper-dependent peptide/catecholamine processing.
    experimental_model
    Recombinant rat type-A 75-kDa PAM, purified enzyme assays
    exposure
    Time/concentration series of ascorbate, DHA or H2O2; fluorescent peptide substrate or pre-hydroxylated intermediate.
    limitations
    Distinct-substrate assay localizes the defect; no claim that all PAM domains share the same redox/cofactor dependence.
    nutrient_topic
    Vitamin C research collection; topical membership is not evidence of a direct dietary effect. · Vitamin C
    organism
    Rattus norvegicus (protein)
    plain_language
    Bypassing the damaged hydroxylation step showed that the finishing lyase step still worked.
    primary_references
    [pam1992] Selective inactivation of the hydroxylase activity of bifunctional rat peptidylglycine alpha-amidating enzyme. (1992). https://pubmed.ncbi.nlm.nih.gov/1567215/ DOI: 10.1016/0003-9861(92)90730-k
    tissue_or_cell_type
    Cell-free recombinant rat protein

    Vitamin C: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 924–935

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant rat type-A 75-kDa PAM, purified enzyme assays · source_derived_draft · unverified_draft

    ### vc-enzyme-pam-lyase-spared Under conditions that inactivated hydroxylase-dependent rat PAM amidation, ascorbate did not impair conversion of the pre-hydroxylated dansyl-Tyr-Val-alpha-hydroxyglycine intermediate to its amide. Condition category: normal nutrient_topic: Vitamin C research collection; topical membership is not evidence of a direct dietary effect. plain_language: Bypassing the damaged hydroxylation step showed that the finishing lyase step still worked. organism: Rattus norvegicus (protein) tissue_or_cell_type: Cell-free recombinant rat protein experimental_model: Recombinant rat type-A 75-kDa PAM, purified enzyme assays limitations: Distinct-substrate assay localizes the defect; no claim that all PAM domains share the same redox/cofactor dependence. cross_nutrient: Vitamin C chemistry in collagen, modified-lysine/carnitine metabolism or copper-dependent peptide/catecholamine processing. exposure: Time/concentration series of ascorbate, DHA or H2O2; fluorescent peptide substrate or pre-hydroxylated intermediate. [pam1992] Selective inactivation of the hydroxylase activity of bifunctional rat peptidylglycine alpha-amidating enzyme. (1992). https://pubmed.ncbi.nlm.nih.gov/1567215/ DOI: 10.1016/0003-9861(92)90730-k
    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