Component

DHPS

Independent protein record; interpretation is limited by each linked claim and its study context.

6 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. Purified human DHPS transferred radiolabeled aminobutyl from deoxyhypusine-eIF5A to 1,3-diaminopropane, regenerating spermidine.

    DHPS → Spermidine source_derived_draftungraded
    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 evidence

  2. DHPS transfers spermidine-derived aminobutyl onto eIF5A Lys50 to form deoxyhypusine.

    DHPS → eIF5A1 with unmodified Lys50 source_derived_draftungraded
    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

What acts on it

  1. The human DHPS study measured an apparent spermidine binding KD of about 4 micromolar using the reported FRET assay.

    Spermidine → DHPS source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text
    experimental_model
    Recombinant human DHPS; assay-dependent apparent affinity.
    limitations
    Binding affinity is not a dietary requirement, plasma target or treatment dose.
    nutrient_topic
    Spermidine collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Spermidine
    plain_language
    The first enzyme recognizes spermidine directly.
    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 22–28

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Recombinant human DHPS; assay-dependent apparent affinity. · source_derived_draft · unverified_draft

    ## spermidine-dhps-binding The first enzyme recognizes spermidine directly. The human DHPS study measured an apparent spermidine binding KD of about 4 micromolar using the reported FRET assay. Model: Recombinant human DHPS; assay-dependent apparent affinity. Limitations: Binding affinity is not a dietary requirement, plasma target or treatment dose. 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

  2. Human DHPS binds NAD and spermidine; NAD-dependent chemistry initiates aminobutyl transfer.

    NAD+ → DHPS source_derived_draftungraded
    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

  3. 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

  4. Spermine bound human DHPS and generated a smaller NADH fluorescence response than spermidine.

    Spermine → DHPS source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text
    experimental_model
    Single-turnover fluorescence and structural assays; apparent spermine KD about 81 micromolar.
    limitations
    The assay probes an initial reaction step, not successful cellular replacement of spermidine for complete eIF5A hypusination.
    nutrient_topic
    Spermidine collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Spermidine
    plain_language
    A related polyamine can participate in part of the chemistry.
    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 30–36

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Single-turnover fluorescence and structural assays; apparent spermine KD about 81 micromolar. · source_derived_draft · unverified_draft

    ## spermidine-spermine-first-step A related polyamine can participate in part of the chemistry. Spermine bound human DHPS and generated a smaller NADH fluorescence response than spermidine. Model: Single-turnover fluorescence and structural assays; apparent spermine KD about 81 micromolar. Limitations: The assay probes an initial reaction step, not successful cellular replacement of spermidine for complete eIF5A hypusination. 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

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