Component

Bovine peptidylglycine alpha-amidating monooxygenase

Bifunctional bovine PAM precursor with PHM and PAL domains.

3 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. Expression of the bovine PHM-only construct in HEK293 cells increased secreted PHM activity, demonstrating a functional hydroxylating domain separable from the PAL portion of PAM.

    Bovine peptidylglycine alpha-amidating monooxygenase → Bovine PAM peptidylglycine alpha-hydroxylating monooxygenase domain source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    Vitamin C chemistry in collagen, modified-lysine/carnitine metabolism or copper-dependent peptide/catecholamine processing.
    experimental_model
    Purified bovine pituitary PAL and bovine-domain expression constructs in HEK293 cells
    exposure
    Purified PAL with N-acetyl-Tyr-Val-alpha-hydroxyglycine; PHM or PAL-containing constructs expressed in HEK293.
    limitations
    Bovine protein expressed in human cells is not a human PAM protein; domain construct activity does not quantify tissue hormone synthesis.
    nutrient_topic
    Vitamin C research collection; topical membership is not evidence of a direct dietary effect. · Vitamin C
    organism
    Bos taurus (protein); Homo sapiens (expression host)
    plain_language
    Peptide amidation begins with a separate vitamin-C-dependent hydroxylation step.
    primary_references
    [pal1991] Peptidyl-alpha-hydroxyglycine alpha-amidating lyase. Purification, characterization, and expression. (1991). https://pubmed.ncbi.nlm.nih.gov/1902227/ DOI: 10.1016/s0021-9258(20)89524-6
    tissue_or_cell_type
    Bovine neurointermediate pituitary; heterologous HEK293

    Vitamin C: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 885–896

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified bovine pituitary PAL and bovine-domain expression constructs in HEK293 cells · source_derived_draft · unverified_draft

    ### vc-enzyme-pam-two-domains Expression of the bovine PHM-only construct in HEK293 cells increased secreted PHM activity, demonstrating a functional hydroxylating domain separable from the PAL portion of PAM. Condition category: normal nutrient_topic: Vitamin C research collection; topical membership is not evidence of a direct dietary effect. plain_language: Peptide amidation begins with a separate vitamin-C-dependent hydroxylation step. organism: Bos taurus (protein); Homo sapiens (expression host) tissue_or_cell_type: Bovine neurointermediate pituitary; heterologous HEK293 experimental_model: Purified bovine pituitary PAL and bovine-domain expression constructs in HEK293 cells limitations: Bovine protein expressed in human cells is not a human PAM protein; domain construct activity does not quantify tissue hormone synthesis. cross_nutrient: Vitamin C chemistry in collagen, modified-lysine/carnitine metabolism or copper-dependent peptide/catecholamine processing. exposure: Purified PAL with N-acetyl-Tyr-Val-alpha-hydroxyglycine; PHM or PAL-containing constructs expressed in HEK293. [pal1991] Peptidyl-alpha-hydroxyglycine alpha-amidating lyase. Purification, characterization, and expression. (1991). https://pubmed.ncbi.nlm.nih.gov/1902227/ DOI: 10.1016/s0021-9258(20)89524-6
    Complete structured claim and evidence

What acts on it

  1. Pituitary peptide-amidating activity inhibited by divalent-metal chelators was restored above control by copper addition; the assayed reaction also required molecular oxygen.

    Copper(II) ion → Bovine peptidylglycine alpha-amidating monooxygenase source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    Vitamin C chemistry in collagen, modified-lysine/carnitine metabolism or copper-dependent peptide/catecholamine processing.
    experimental_model
    Rat pituitary and bovine intermediate-pituitary secretory-granule preparations
    exposure
    Synthetic D-Tyr-Val-Gly amidation with varied ascorbate, oxygen and divalent-metal chelators/copper.
    limitations
    Study included rat and bovine preparations; this cofactor observation is scoped to those preparations rather than a human nutritional copper trial.
    nutrient_topic
    Vitamin C research collection; topical membership is not evidence of a direct dietary effect. · Vitamin C
    organism
    Rattus norvegicus; Bos taurus
    plain_language
    Vitamin C and copper participate together, and removing available metal stops this peptide-processing assay.
    primary_references
    [pam1983] Identification in pituitary tissue of a peptide alpha-amidation activity that acts on glycine-extended peptides and requires molecular oxygen, copper, and ascorbic acid. (1983). https://pubmed.ncbi.nlm.nih.gov/6576381/ DOI: 10.1073/pnas.80.16.5144
    tissue_or_cell_type
    Pituitary secretory granules

    Vitamin C: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 872–883

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Rat pituitary and bovine intermediate-pituitary secretory-granule preparations · source_derived_draft · unverified_draft

    ### vc-enzyme-amidation-copper-recovery Pituitary peptide-amidating activity inhibited by divalent-metal chelators was restored above control by copper addition; the assayed reaction also required molecular oxygen. Condition category: normal nutrient_topic: Vitamin C research collection; topical membership is not evidence of a direct dietary effect. plain_language: Vitamin C and copper participate together, and removing available metal stops this peptide-processing assay. organism: Rattus norvegicus; Bos taurus tissue_or_cell_type: Pituitary secretory granules experimental_model: Rat pituitary and bovine intermediate-pituitary secretory-granule preparations limitations: Study included rat and bovine preparations; this cofactor observation is scoped to those preparations rather than a human nutritional copper trial. cross_nutrient: Vitamin C chemistry in collagen, modified-lysine/carnitine metabolism or copper-dependent peptide/catecholamine processing. exposure: Synthetic D-Tyr-Val-Gly amidation with varied ascorbate, oxygen and divalent-metal chelators/copper. [pam1983] Identification in pituitary tissue of a peptide alpha-amidation activity that acts on glycine-extended peptides and requires molecular oxygen, copper, and ascorbic acid. (1983). https://pubmed.ncbi.nlm.nih.gov/6576381/ DOI: 10.1073/pnas.80.16.5144
    Complete structured claim and evidence

  2. Bovine intermediate-pituitary granule amidation of D-Tyr-Val-Gly responded to ascorbate, with apparent substrate Km and Vmax changing as the ascorbate concentration changed.

    L-Ascorbate → Bovine peptidylglycine alpha-amidating monooxygenase source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    Vitamin C chemistry in collagen, modified-lysine/carnitine metabolism or copper-dependent peptide/catecholamine processing.
    experimental_model
    Bovine intermediate-pituitary secretory-granule kinetic assay
    exposure
    Synthetic D-Tyr-Val-Gly amidation with varied ascorbate, oxygen and divalent-metal chelators/copper.
    limitations
    The old granule preparation is not a purified modern PAM-domain assay; synthetic substrate kinetics do not quantify all hormone amidation.
    nutrient_topic
    Vitamin C research collection; topical membership is not evidence of a direct dietary effect. · Vitamin C
    organism
    Bos taurus
    plain_language
    Vitamin C helps the pituitary enzyme finish a peptide with an amide group.
    primary_references
    [pam1983] Identification in pituitary tissue of a peptide alpha-amidation activity that acts on glycine-extended peptides and requires molecular oxygen, copper, and ascorbic acid. (1983). https://pubmed.ncbi.nlm.nih.gov/6576381/ DOI: 10.1073/pnas.80.16.5144
    tissue_or_cell_type
    Pituitary secretory granules

    Vitamin C: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 859–870

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Bovine intermediate-pituitary secretory-granule kinetic assay · source_derived_draft · unverified_draft

    ### vc-enzyme-bovine-amidation-ascorbate Bovine intermediate-pituitary granule amidation of D-Tyr-Val-Gly responded to ascorbate, with apparent substrate Km and Vmax changing as the ascorbate concentration changed. Condition category: normal nutrient_topic: Vitamin C research collection; topical membership is not evidence of a direct dietary effect. plain_language: Vitamin C helps the pituitary enzyme finish a peptide with an amide group. organism: Bos taurus tissue_or_cell_type: Pituitary secretory granules experimental_model: Bovine intermediate-pituitary secretory-granule kinetic assay limitations: The old granule preparation is not a purified modern PAM-domain assay; synthetic substrate kinetics do not quantify all hormone amidation. cross_nutrient: Vitamin C chemistry in collagen, modified-lysine/carnitine metabolism or copper-dependent peptide/catecholamine processing. exposure: Synthetic D-Tyr-Val-Gly amidation with varied ascorbate, oxygen and divalent-metal chelators/copper. [pam1983] Identification in pituitary tissue of a peptide alpha-amidation activity that acts on glycine-extended peptides and requires molecular oxygen, copper, and ascorbic acid. (1983). https://pubmed.ncbi.nlm.nih.gov/6576381/ DOI: 10.1073/pnas.80.16.5144
    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.

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