Component
eIF5A1 with unmodified Lys50
Protein-bound site or substrate state, not free dietary L-lysine. Sequence and assay context limit the relationship.
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
DHPS 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
Where it participates (unsigned role)
Human DHPS binds NAD and spermidine; NAD-dependent chemistry initiates aminobutyl transfer.
Experimental context and source evidence
- evidence_access
- Primary full text
- experimental_model
- Purified human DHPS crystallography and single-turnover assays.
- limitations
- NAD is regenerated during the reaction; this does not measure NAD depletion or establish niacin supplementation benefit.
- nutrient_topic
- Spermidine collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Spermidine
- plain_language
- A niacin-derived coenzyme participates in using spermidine.
- primary_references
- Half Way to Hypusine-Structural Basis for Substrate Recognition by Human Deoxyhypusine Synthase. · 2020 · https://pubmed.ncbi.nlm.nih.gov/32235505/ · DOI 10.3390/biom10040522
Spermidine: biosynthesis, hypusination, transport and cross-nutrient mechanisms (2026-09-19) · lines 14–20
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Purified human DHPS crystallography and single-turnover assays. · source_derived_draft · unverified_draft
## spermidine-dhps-nad A niacin-derived coenzyme participates in using spermidine. Human DHPS binds NAD and spermidine; NAD-dependent chemistry initiates aminobutyl transfer. Model: Purified human DHPS crystallography and single-turnover assays. Limitations: NAD is regenerated during the reaction; this does not measure NAD depletion or establish niacin supplementation benefit. Evidence access: Primary full text Half Way to Hypusine-Structural Basis for Substrate Recognition by Human Deoxyhypusine Synthase. · 2020 · https://pubmed.ncbi.nlm.nih.gov/32235505/ · DOI 10.3390/biom10040522
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.