Component

Alpha-L-aspartyl-L-phenylalanine

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 it acts on

  1. Brush-border and cytosolic preparations hydrolyzed Asp-Phe; cytosolic fractionation identified one activity peak distinct from seven previously described peptidases.

    Alpha-L-aspartyl-L-phenylalanine → Human intestinal Asp-Phe dipeptide hydrolysis source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human intestinal mucosa and red-cell lysate fractionation.
    limitations
    Intact dipeptide transport was proposed; the cytosolic enzyme was not molecularly identified.
    nutrient_topic
    Aspartame collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Aspartame
    plain_language
    The amino-acid pair can be processed after reaching a different cell compartment.
    primary_references
    Intestinal hydrolysis of aspartylphenylalanine--the metabolic product of aspartame. · 1986 · https://pubmed.ncbi.nlm.nih.gov/3743970/ · DOI 10.1016/0016-5085(86)90697-9

    Aspartame: digestion, taste, metabolite dependencies and experimental signaling (2026-09-20) · lines 26–32

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human intestinal mucosa and red-cell lysate fractionation. · source_derived_draft · unverified_draft

    ## aspartame-dipeptide-cleavage The amino-acid pair can be processed after reaching a different cell compartment. Brush-border and cytosolic preparations hydrolyzed Asp-Phe; cytosolic fractionation identified one activity peak distinct from seven previously described peptidases. Model: Human intestinal mucosa and red-cell lysate fractionation. Limitations: Intact dipeptide transport was proposed; the cytosolic enzyme was not molecularly identified. Evidence access: Primary abstract Intestinal hydrolysis of aspartylphenylalanine--the metabolic product of aspartame. · 1986 · https://pubmed.ncbi.nlm.nih.gov/3743970/ · DOI 10.1016/0016-5085(86)90697-9
    Complete structured claim and evidence

What acts on it

  1. The intestinal study describes ester-bond hydrolysis of aspartame to Asp-Phe before further dipeptide digestion.

    Aspartame → Alpha-L-aspartyl-L-phenylalanine source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Reaction background and human intestinal mucosal enzyme experiments.
    limitations
    This record does not assign the initial esterase to an unverified gene.
    nutrient_topic
    Aspartame collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Aspartame
    plain_language
    Removing the methyl ester is separate from splitting the peptide.
    primary_references
    Intestinal hydrolysis of aspartylphenylalanine--the metabolic product of aspartame. · 1986 · https://pubmed.ncbi.nlm.nih.gov/3743970/ · DOI 10.1016/0016-5085(86)90697-9

    Aspartame: digestion, taste, metabolite dependencies and experimental signaling (2026-09-20) · lines 18–24

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

    ## aspartame-ester-cleavage Removing the methyl ester is separate from splitting the peptide. The intestinal study describes ester-bond hydrolysis of aspartame to Asp-Phe before further dipeptide digestion. Model: Reaction background and human intestinal mucosal enzyme experiments. Limitations: This record does not assign the initial esterase to an unverified gene. Evidence access: Primary abstract Intestinal hydrolysis of aspartylphenylalanine--the metabolic product of aspartame. · 1986 · https://pubmed.ncbi.nlm.nih.gov/3743970/ · DOI 10.1016/0016-5085(86)90697-9
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Diseased intestinal mucosa showed reduced brush-border and cytosolic Asp-Phe hydrolase activity alongside reductions in other enzymes.

    Asp-Phe hydrolase activity in diseased human intestinal mucosa → Human intestinal microvillar aspartame hydrolysis source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary abstract
    experimental_model
    Human mucosal enzyme comparison.
    limitations
    No demonstrated aspartame-sensitivity syndrome or successful enzyme repletion was established.
    nutrient_topic
    Aspartame collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Aspartame
    plain_language
    General mucosal disease can change digestive capacity.
    primary_references
    Intestinal hydrolysis of aspartylphenylalanine--the metabolic product of aspartame. · 1986 · https://pubmed.ncbi.nlm.nih.gov/3743970/ · DOI 10.1016/0016-5085(86)90697-9
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Aspartame: digestion, taste, metabolite dependencies and experimental signaling (2026-09-20) · lines 34–40

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

    ## aspartame-mucosal-loss General mucosal disease can change digestive capacity. Diseased intestinal mucosa showed reduced brush-border and cytosolic Asp-Phe hydrolase activity alongside reductions in other enzymes. Model: Human mucosal enzyme comparison. Limitations: No demonstrated aspartame-sensitivity syndrome or successful enzyme repletion was established. Evidence access: Primary abstract Intestinal hydrolysis of aspartylphenylalanine--the metabolic product of aspartame. · 1986 · https://pubmed.ncbi.nlm.nih.gov/3743970/ · DOI 10.1016/0016-5085(86)90697-9
    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