Component
Human spermine synthase / SMS
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
The product-bound SMS structure supplied a mechanistic explanation for inhibition by methylthioadenosine.
Experimental context and source evidence
- evidence_access
- Primary abstract
- experimental_model
- Human SMS structural and biochemical study.
- limitations
- Product inhibition is not a measured dietary-arginine effect.
- nutrient_topic
- L-Arginine collection; tissue, species, dose and formulation distinctions retained. · L-Arginine
- plain_language
- A reaction product can slow its own production pathway.
- primary_references
- Crystal structure of human spermine synthase: implications of substrate binding and catalytic mechanism. · 2008 · https://pubmed.ncbi.nlm.nih.gov/18367445/ · DOI 10.1074/jbc.m710323200
L-Arginine: transport, metabolic branches, nutrient interactions, availability and discovery questions (2026-09-18) · lines 166–172
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human SMS structural and biochemical study. · source_derived_draft · unverified_draft
## arg-sms-inhibition A reaction product can slow its own production pathway. The product-bound SMS structure supplied a mechanistic explanation for inhibition by methylthioadenosine. Model: Human SMS structural and biochemical study. Limitations: Product inhibition is not a measured dietary-arginine effect. Evidence access: Primary abstract Crystal structure of human spermine synthase: implications of substrate binding and catalytic mechanism. · 2008 · https://pubmed.ncbi.nlm.nih.gov/18367445/ · DOI 10.1074/jbc.m710323200
Complete structured claim and evidence
Where it participates (unsigned role)
Human spermine-synthase substrate/product structures and mutagenesis support aminopropyl transfer to spermidine.
Experimental context and source evidence
- evidence_access
- Primary abstract
- experimental_model
- Human SMS structures and catalytic assays.
- limitations
- A pathway connection does not mean arginine is always rate limiting.
- nutrient_topic
- L-Arginine collection; tissue, species, dose and formulation distinctions retained. · L-Arginine
- plain_language
- The polyamine pathway extends beyond spermidine.
- primary_references
- Crystal structure of human spermine synthase: implications of substrate binding and catalytic mechanism. · 2008 · https://pubmed.ncbi.nlm.nih.gov/18367445/ · DOI 10.1074/jbc.m710323200
L-Arginine: transport, metabolic branches, nutrient interactions, availability and discovery questions (2026-09-18) · lines 158–164
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human SMS structures and catalytic assays. · source_derived_draft · unverified_draft
## arg-sms The polyamine pathway extends beyond spermidine. Human spermine-synthase substrate/product structures and mutagenesis support aminopropyl transfer to spermidine. Model: Human SMS structures and catalytic assays. Limitations: A pathway connection does not mean arginine is always rate limiting. Evidence access: Primary abstract Crystal structure of human spermine synthase: implications of substrate binding and catalytic mechanism. · 2008 · https://pubmed.ncbi.nlm.nih.gov/18367445/ · DOI 10.1074/jbc.m710323200
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.