Component

N1-Acetylspermidine

Context-specific entity; species, compartment and exposure are stated on each claim.

3 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 acts on it

  1. Recombinant human PAOX oxidized N1-acetylspermidine with Km 2.1 micromolar and kcat 15 per second.

    Human N1-acetylpolyamine oxidase / PAOX → N1-Acetylspermidine source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Purified human enzyme.
    limitations
    Do not apply these values to unmodified spermidine or a human plasma target.
    nutrient_topic
    Spermidine collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Spermidine
    plain_language
    The acetylated molecule has its own enzyme kinetics.
    primary_references
    Properties of recombinant human N1-acetylpolyamine oxidase (hPAO): potential role in determining drug sensitivity. · 2005 · https://pubmed.ncbi.nlm.nih.gov/15791459/ · DOI 10.1007/s00280-004-0936-5

    Spermidine: biosynthesis, hypusination, transport and cross-nutrient mechanisms (2026-09-19) · lines 94–100

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

    ## spermidine-paox-acetylspermidine The acetylated molecule has its own enzyme kinetics. Recombinant human PAOX oxidized N1-acetylspermidine with Km 2.1 micromolar and kcat 15 per second. Model: Purified human enzyme. Limitations: Do not apply these values to unmodified spermidine or a human plasma target. Evidence access: Primary abstract Properties of recombinant human N1-acetylpolyamine oxidase (hPAO): potential role in determining drug sensitivity. · 2005 · https://pubmed.ncbi.nlm.nih.gov/15791459/ · DOI 10.1007/s00280-004-0936-5
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Human SAT1 kinetics support a random sequential mechanism involving acetyl donor and polyamine in a ternary complex.

    Acetyl-CoA → Human spermidine/spermine N1-acetyltransferase / SAT1 source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human SAT1 initial-velocity, inhibition and pH experiments.
    limitations
    Mechanism does not quantify whole-body acetyl-CoA competition.
    nutrient_topic
    Spermidine collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Spermidine
    plain_language
    Both the donor and the polyamine must reach the enzyme.
    primary_references
    Mechanistic and structural analysis of human spermidine/spermine N1-acetyltransferase. · 2007 · https://pubmed.ncbi.nlm.nih.gov/17516632/ · DOI 10.1021/bi700256z

    Spermidine: biosynthesis, hypusination, transport and cross-nutrient mechanisms (2026-09-19) · lines 86–92

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human SAT1 initial-velocity, inhibition and pH experiments. · source_derived_draft · unverified_draft

    ## spermidine-sat1-cosubstrate Both the donor and the polyamine must reach the enzyme. Human SAT1 kinetics support a random sequential mechanism involving acetyl donor and polyamine in a ternary complex. Model: Human SAT1 initial-velocity, inhibition and pH experiments. Limitations: Mechanism does not quantify whole-body acetyl-CoA competition. Evidence access: Primary abstract Mechanistic and structural analysis of human spermidine/spermine N1-acetyltransferase. · 2007 · https://pubmed.ncbi.nlm.nih.gov/17516632/ · DOI 10.1021/bi700256z
    Complete structured claim and evidence

  2. Human SAT1 catalyzes N1-acetylation of spermidine using acetyl-CoA.

    Human spermidine/spermine N1-acetyltransferase / SAT1 → Spermidine source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Purified recombinant human SAT1 kinetics and structural analysis.
    limitations
    Acetyl-CoA dependence connects to CoA metabolism, not demonstrated pantothenate depletion.
    nutrient_topic
    Spermidine collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Spermidine
    plain_language
    A CoA-dependent step changes how spermidine is recycled.
    primary_references
    Mechanistic and structural analysis of human spermidine/spermine N1-acetyltransferase. · 2007 · https://pubmed.ncbi.nlm.nih.gov/17516632/ · DOI 10.1021/bi700256z

    Spermidine: biosynthesis, hypusination, transport and cross-nutrient mechanisms (2026-09-19) · lines 78–84

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Purified recombinant human SAT1 kinetics and structural analysis. · source_derived_draft · unverified_draft

    ## spermidine-sat1-substrate A CoA-dependent step changes how spermidine is recycled. Human SAT1 catalyzes N1-acetylation of spermidine using acetyl-CoA. Model: Purified recombinant human SAT1 kinetics and structural analysis. Limitations: Acetyl-CoA dependence connects to CoA metabolism, not demonstrated pantothenate depletion. Evidence access: Primary abstract Mechanistic and structural analysis of human spermidine/spermine N1-acetyltransferase. · 2007 · https://pubmed.ncbi.nlm.nih.gov/17516632/ · DOI 10.1021/bi700256z
    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