Component
Recombinant rat type-A 75-kDa peptidylglycine amidating enzyme
Rat bifunctional recombinant construct used in the 1992 inactivation experiments.
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
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 evidenceIn time- and concentration-dependent purified-protein experiments, ascorbate inactivated the full amidation activity of recombinant rat 75-kDa PAM measured with dansyl-Tyr-Val-Gly.
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
- Assay redox damage, not evidence that dietary vitamin C suppresses hormone amidation in vivo; accessible abstract does not specify full concentration range.
- nutrient_topic
- Vitamin C research collection; topical membership is not evidence of a direct dietary effect. · Vitamin C
- organism
- Rattus norvegicus (protein)
- plain_language
- The same vitamin that supports the enzyme can damage its hydroxylating activity under particular cell-free redox conditions.
- 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 911–922
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-oxidative-inactivation In time- and concentration-dependent purified-protein experiments, ascorbate inactivated the full amidation activity of recombinant rat 75-kDa PAM measured with dansyl-Tyr-Val-Gly. Condition category: normal nutrient_topic: Vitamin C research collection; topical membership is not evidence of a direct dietary effect. plain_language: The same vitamin that supports the enzyme can damage its hydroxylating activity under particular cell-free redox conditions. 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: Assay redox damage, not evidence that dietary vitamin C suppresses hormone amidation in vivo; accessible abstract does not specify full concentration range. 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
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.