Component

eIF5A1 with hypusine at residue 50

Protein-bound site or substrate state, not free dietary L-lysine. Sequence and assay context limit the relationship.

5 recorded relationships. Experimental role, claim status and evidence remain attached to each record.

Read recorded mechanisms Open recursive mind map

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.

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.

Recorded relationships

What it acts on

  1. The same reversal assay did not remove the side chain from hypusine-containing eIF5A.

    eIF5A1 with hypusine at residue 50 → DHPS source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Purified human DHPS comparison of deoxyhypusine and hypusine protein substrates.
    limitations
    Assay-specific non-reversal does not establish lifetime stability of the protein.
    nutrient_topic
    Spermidine collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Spermidine
    plain_language
    The second modification step stabilizes the completed product.
    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 46–52

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Purified human DHPS comparison of deoxyhypusine and hypusine protein substrates. · source_derived_draft · unverified_draft

    ## spermidine-hydroxylation-lock The second modification step stabilizes the completed product. The same reversal assay did not remove the side chain from hypusine-containing eIF5A. Model: Purified human DHPS comparison of deoxyhypusine and hypusine protein substrates. Limitations: Assay-specific non-reversal does not establish lifetime stability of the protein. 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 evidence

Where it participates (unsigned role)

  1. Human DOHH structures resolved a peroxo-diiron intermediate involved in hydroxylating deoxyhypusine-eIF5A.

    Molecular oxygen → DOHH source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human enzyme; 1.7-angstrom structures and spectroscopy.
    limitations
    DOHH is not a collagen-type 2-oxoglutarate hydroxylase; do not infer the same vitamin C requirement.
    nutrient_topic
    Spermidine collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Spermidine
    plain_language
    Oxygen chemistry completes the protein modification.
    primary_references
    Crystal Structure of the Peroxo-diiron(III) Intermediate of Deoxyhypusine Hydroxylase, an Oxygenase Involved in Hypusination. · 2015 · https://pubmed.ncbi.nlm.nih.gov/25865244/ · DOI 10.1016/j.str.2015.03.002

    Spermidine: biosynthesis, hypusination, transport and cross-nutrient mechanisms (2026-09-19) · lines 62–68

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human enzyme; 1.7-angstrom structures and spectroscopy. · source_derived_draft · unverified_draft

    ## spermidine-dohh-oxygen Oxygen chemistry completes the protein modification. Human DOHH structures resolved a peroxo-diiron intermediate involved in hydroxylating deoxyhypusine-eIF5A. Model: Human enzyme; 1.7-angstrom structures and spectroscopy. Limitations: DOHH is not a collagen-type 2-oxoglutarate hydroxylase; do not infer the same vitamin C requirement. Evidence access: Primary abstract Crystal Structure of the Peroxo-diiron(III) Intermediate of Deoxyhypusine Hydroxylase, an Oxygenase Involved in Hypusination. · 2015 · https://pubmed.ncbi.nlm.nih.gov/25865244/ · DOI 10.1016/j.str.2015.03.002
    Complete structured claim and evidence

  2. The prostate-cell study linked spermidine-driven eIF5A hypusination to increased NRF2 translation.

    Spermidine → Human Nrf2 / NFE2L2 source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text
    experimental_model
    Human PC3/DU145 cells and hypusination perturbation.
    limitations
    Assay-specific pathway interpretation; does not mean NRF2 is always protective.
    nutrient_topic
    Spermidine collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Spermidine
    plain_language
    A translation response can raise a stress regulator.
    primary_references
    Spermidine inactivates proteasome activity and enhances ferroptosis in prostate cancer. · 2025 · https://pubmed.ncbi.nlm.nih.gov/40486852/ · DOI 10.1016/j.apsb.2025.02.023

    Spermidine: biosynthesis, hypusination, transport and cross-nutrient mechanisms (2026-09-19) · lines 510–516

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human PC3/DU145 cells and hypusination perturbation. · source_derived_draft · unverified_draft

    ## spermidine-nrf2-translation A translation response can raise a stress regulator. The prostate-cell study linked spermidine-driven eIF5A hypusination to increased NRF2 translation. Model: Human PC3/DU145 cells and hypusination perturbation. Limitations: Assay-specific pathway interpretation; does not mean NRF2 is always protective. Evidence access: Primary full text Spermidine inactivates proteasome activity and enhances ferroptosis in prostate cancer. · 2025 · https://pubmed.ncbi.nlm.nih.gov/40486852/ · DOI 10.1016/j.apsb.2025.02.023
    Complete structured claim and evidence

  3. Spermidine restored TFEB protein and eIF5A hypusination in older-donor CD8 cells and in DFMO-treated young-donor cells.

    Spermidine → Human transcription factor EB / TFEB source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    biomarker_context Imported condition classification; unverified.
    evidence_access
    Primary full text
    experimental_model
    Primary human T-cell cultures.
    limitations
    Total eIF5A and its modified fraction are different measurements.
    nutrient_topic
    Spermidine collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Spermidine
    plain_language
    A measured protein response links the pathway to autophagy.
    primary_references
    Autophagy in T cells from aged donors is maintained by spermidine and correlates with function and vaccine responses. · 2020 · https://pubmed.ncbi.nlm.nih.gov/33317695/ · DOI 10.7554/eLife.57950
    trigger_kind
    biomarker_context Imported condition classification; unverified.

    Spermidine: biosynthesis, hypusination, transport and cross-nutrient mechanisms (2026-09-19) · lines 246–252

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Primary human T-cell cultures. · source_derived_draft · unverified_draft

    ## spermidine-tcell-tfeb A measured protein response links the pathway to autophagy. Spermidine restored TFEB protein and eIF5A hypusination in older-donor CD8 cells and in DFMO-treated young-donor cells. Model: Primary human T-cell cultures. Limitations: Total eIF5A and its modified fraction are different measurements. Evidence access: Primary full text Autophagy in T cells from aged donors is maintained by spermidine and correlates with function and vaccine responses. · 2020 · https://pubmed.ncbi.nlm.nih.gov/33317695/ · DOI 10.7554/eLife.57950
    Complete structured claim and evidence

  4. DOHH hydroxylates deoxyhypusine-eIF5A to hypusine-eIF5A using its oxygen-activating diiron center.

    DOHH → eIF5A1 with deoxyhypusine at residue 50 source_derived_draftungraded
    Experimental context and source evidence
    experimental_model
    Human DOHH structures and spectroscopy.
    limitations
    DOHH is a diiron enzyme, not a 2-oxoglutarate-dependent hydroxylase. 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 second enzyme completes the special modification.
    primary_references
    [dohh-2015] Crystal Structure of the Peroxo-diiron(III) Intermediate of Deoxyhypusine Hydroxylase, an Oxygenase Involved in Hypusination (2015). https://pubmed.ncbi.nlm.nih.gov/25865244/ DOI: 10.1016/j.str.2015.03.002
    tissue_or_cell_type
    Not specified as a whole tissue; see experimental model.

    L-Lysine: mechanism-first literature curation (2026-09-17) · lines 588–596

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human DOHH structures and spectroscopy. · source_derived_draft · unverified_draft

    ### dohh-eif5a-hypusine DOHH hydroxylates deoxyhypusine-eIF5A to hypusine-eIF5A using its oxygen-activating diiron center. Plain language: A second enzyme completes the special modification. Condition category: normal organism: Human tissue_or_cell_type: Not specified as a whole tissue; see experimental model. experimental_model: Human DOHH structures and spectroscopy. limitations: DOHH is a diiron enzyme, not a 2-oxoglutarate-dependent hydroxylase. This reaction modifies lysine already in a protein. It does not show that extra oral lysine increases the reaction or improves a clinical outcome. [dohh-2015] Crystal Structure of the Peroxo-diiron(III) Intermediate of Deoxyhypusine Hydroxylase, an Oxygenase Involved in Hypusination (2015). https://pubmed.ncbi.nlm.nih.gov/25865244/ DOI: 10.1016/j.str.2015.03.002
    Complete structured claim and evidence

In the sources

Preserved passages that mention this component, quoted exactly. Open one to read it in context.

    This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.

    Evidence, AI assistance and curation standards