Component
1,3-Diaminopropane
Independent small molecule record; interpretation is limited by each linked claim and its study context.
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.
Where it participates (unsigned role)
Purified human DHPS transferred radiolabeled aminobutyl from deoxyhypusine-eIF5A to 1,3-diaminopropane, regenerating spermidine.
Experimental context and source evidence
- evidence_access
- Primary abstract
- experimental_model
- Human enzyme, NAD, labeled protein and diamine substrate.
- limitations
- No in-vivo flux or dominant recycling contribution established.
- nutrient_topic
- Spermidine collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Spermidine
- plain_language
- An unfinished protein modification can be reversed in vitro.
- primary_references
- Reversal of the deoxyhypusine synthesis reaction. Generation of spermidine or homospermidine from deoxyhypusine by deoxyhypusine synthase. · 2003 · https://pubmed.ncbi.nlm.nih.gov/12788913/ · DOI 10.1074/jbc.M304247200
Spermidine: biosynthesis, hypusination, transport and cross-nutrient mechanisms (2026-09-19) · lines 38–44
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human enzyme, NAD, labeled protein and diamine substrate. · source_derived_draft · unverified_draft
## spermidine-dhps-reversal An unfinished protein modification can be reversed in vitro. Purified human DHPS transferred radiolabeled aminobutyl from deoxyhypusine-eIF5A to 1,3-diaminopropane, regenerating spermidine. Model: Human enzyme, NAD, labeled protein and diamine substrate. Limitations: No in-vivo flux or dominant recycling contribution established. Evidence access: Primary abstract Reversal of the deoxyhypusine synthesis reaction. Generation of spermidine or homospermidine from deoxyhypusine by deoxyhypusine synthase. · 2003 · https://pubmed.ncbi.nlm.nih.gov/12788913/ · DOI 10.1074/jbc.M304247200
Complete structured claim and evidenceDHPS transfers spermidine-derived aminobutyl onto eIF5A Lys50 to form deoxyhypusine.
Experimental context and source evidence
- experimental_model
- Human DHPS structural biochemistry.
- limitations
- NAD cycles during catalysis; it is not represented as a net consumed substrate here. This reaction modifies lysine already in a protein. It does not show that extra oral lysine increases the reaction or improves a clinical outcome.
- organism
- Human
- plain_language
- A particular protein lysine becomes a specialized translation-factor residue.
- primary_references
- [dhps-2020] Half Way to Hypusine-Structural Basis for Substrate Recognition by Human Deoxyhypusine Synthase (2020). https://pubmed.ncbi.nlm.nih.gov/32235505/
- tissue_or_cell_type
- Not specified as a whole tissue; see experimental model.
L-Lysine: mechanism-first literature curation (2026-09-17) · lines 578–586
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human DHPS structural biochemistry. · source_derived_draft · unverified_draft
### dhps-eif5a-deoxyhypusine DHPS transfers spermidine-derived aminobutyl onto eIF5A Lys50 to form deoxyhypusine. Plain language: A particular protein lysine becomes a specialized translation-factor residue. Condition category: normal organism: Human tissue_or_cell_type: Not specified as a whole tissue; see experimental model. experimental_model: Human DHPS structural biochemistry. limitations: NAD cycles during catalysis; it is not represented as a net consumed substrate here. This reaction modifies lysine already in a protein. It does not show that extra oral lysine increases the reaction or improves a clinical outcome. [dhps-2020] Half Way to Hypusine-Structural Basis for Substrate Recognition by Human Deoxyhypusine Synthase (2020). https://pubmed.ncbi.nlm.nih.gov/32235505/
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.