Component
Human S-adenosylmethionine decarboxylase / AMD1
Study-scoped entity; inspect species, exposure and experimental limitations on each claim.
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
Putrescine stimulated human AMD1 autoprocessing and decarboxylation through a binding pocket separate from the active site.
Experimental context and source evidence
- evidence_access
- Primary abstract
- experimental_model
- Human AMD1 structures, binding measurements and targeted mutants.
- limitations
- Feedback demonstrated at enzyme level; not a measured systemic methyl-donor drain.
- nutrient_topic
- L-Arginine collection; tissue, species, dose and formulation distinctions retained. · L-Arginine
- plain_language
- A pathway product helps activate production of the next branch’s donor.
- primary_references
- Structural basis for putrescine activation of human S-adenosylmethionine decarboxylase. · 2008 · https://pubmed.ncbi.nlm.nih.gov/19053272/ · DOI 10.1021/bi801732m
L-Arginine: transport, metabolic branches, nutrient interactions, availability and discovery questions (2026-09-18) · lines 142–148
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human AMD1 structures, binding measurements and targeted mutants. · source_derived_draft · unverified_draft
## arg-amd-feedback A pathway product helps activate production of the next branch’s donor. Putrescine stimulated human AMD1 autoprocessing and decarboxylation through a binding pocket separate from the active site. Model: Human AMD1 structures, binding measurements and targeted mutants. Limitations: Feedback demonstrated at enzyme level; not a measured systemic methyl-donor drain. Evidence access: Primary abstract Structural basis for putrescine activation of human S-adenosylmethionine decarboxylase. · 2008 · https://pubmed.ncbi.nlm.nih.gov/19053272/ · DOI 10.1021/bi801732m
Complete structured claim and evidence
Where it participates (unsigned role)
AMD1 decarboxylation generates the aminopropyl donor used in polyamine synthesis.
Experimental context and source evidence
- evidence_access
- Primary abstract
- experimental_model
- Human S-adenosylmethionine decarboxylase biochemical study.
- limitations
- Do not confuse aminopropyl donation with GAMT methyl transfer.
- nutrient_topic
- L-Arginine collection; tissue, species, dose and formulation distinctions retained. · L-Arginine
- plain_language
- SAM must be chemically changed before this branch uses it.
- primary_references
- Structural basis for putrescine activation of human S-adenosylmethionine decarboxylase. · 2008 · https://pubmed.ncbi.nlm.nih.gov/19053272/ · DOI 10.1021/bi801732m
L-Arginine: transport, metabolic branches, nutrient interactions, availability and discovery questions (2026-09-18) · lines 150–156
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human S-adenosylmethionine decarboxylase biochemical study. · source_derived_draft · unverified_draft
## arg-amd-reaction SAM must be chemically changed before this branch uses it. AMD1 decarboxylation generates the aminopropyl donor used in polyamine synthesis. Model: Human S-adenosylmethionine decarboxylase biochemical study. Limitations: Do not confuse aminopropyl donation with GAMT methyl transfer. Evidence access: Primary abstract Structural basis for putrescine activation of human S-adenosylmethionine decarboxylase. · 2008 · https://pubmed.ncbi.nlm.nih.gov/19053272/ · DOI 10.1021/bi801732m
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.