Component

Human cytosolic nonspecific dipeptidase / CNDP2

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

4 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. Deleting CNDP2 in human RT4 bladder epithelial cells reduced Lac-Phe production; extracellular lactate stimulated production in the control cells.

    Human cytosolic nonspecific dipeptidase / CNDP2 → N-Lactoyl-phenylalanine / Lac-Phe source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract and PMC full-text Figure 2 and CRISPR methods
    experimental_model
    Human RT4 cell knockout and 25 mM lactate treatment for 24 hours; Figure 2.
    limitations
    This is a shared-enzyme connection, not proof that carnosine changes appetite.
    nutrient_topic
    Carnosine collection; isomer, preparation, species, exposure and manipulation remain explicit. · L-Carnosine / beta-alanyl-L-histidine
    plain_language
    The peptide-processing enzyme also participates in another metabolic pathway.
    primary_references
    An exercise-inducible metabolite that suppresses feeding and obesity. · 2022 · https://pubmed.ncbi.nlm.nih.gov/35705806/ · DOI 10.1038/s41586-022-04828-5

    Carnosine: synthesis, transport, carbonyl chemistry and nutrient interactions (2026-09-19) · lines 172–178

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human RT4 cell knockout and 25 mM lactate treatment for 24 hours; Figure 2. · source_derived_draft · unverified_draft

    ## carnosine-cndp2-lacphe The peptide-processing enzyme also participates in another metabolic pathway. Deleting CNDP2 in human RT4 bladder epithelial cells reduced Lac-Phe production; extracellular lactate stimulated production in the control cells. Model: Human RT4 cell knockout and 25 mM lactate treatment for 24 hours; Figure 2. Limitations: This is a shared-enzyme connection, not proof that carnosine changes appetite. Evidence access: Primary abstract and PMC full-text Figure 2 and CRISPR methods An exercise-inducible metabolite that suppresses feeding and obesity. · 2022 · https://pubmed.ncbi.nlm.nih.gov/35705806/ · DOI 10.1038/s41586-022-04828-5
    Complete structured claim and evidence

  2. Human CNDP2 hydrolyzed carnosine only under alkaline assay conditions, with an optimum near pH 9.5.

    Human cytosolic nonspecific dipeptidase / CNDP2 → L-Carnosine / beta-alanyl-L-histidine source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Purified recombinant protein.
    limitations
    Do not assume CNDP2 is an equally active carnosinase at normal cytosolic pH.
    nutrient_topic
    Carnosine collection; isomer, preparation, species, exposure and manipulation remain explicit. · L-Carnosine / beta-alanyl-L-histidine
    plain_language
    The similarly named enzyme behaved differently.
    primary_references
    Sequence identification and characterization of human carnosinase and a closely related non-specific dipeptidase. · 2003 · https://pubmed.ncbi.nlm.nih.gov/12473676/ · DOI 10.1074/jbc.M209764200

    Carnosine: synthesis, transport, carbonyl chemistry and nutrient interactions (2026-09-19) · lines 52–58

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Purified recombinant protein. · source_derived_draft · unverified_draft

    ## carnosine-cndp2-ph The similarly named enzyme behaved differently. Human CNDP2 hydrolyzed carnosine only under alkaline assay conditions, with an optimum near pH 9.5. Model: Purified recombinant protein. Limitations: Do not assume CNDP2 is an equally active carnosinase at normal cytosolic pH. Evidence access: Primary abstract Sequence identification and characterization of human carnosinase and a closely related non-specific dipeptidase. · 2003 · https://pubmed.ncbi.nlm.nih.gov/12473676/ · DOI 10.1074/jbc.M209764200
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Lac-Phe rose after exercise in human cohorts of 36 and 8 participants; in the modality comparison, changes tracked lactate and were greatest after sprint exercise.

    N-Lactoyl-phenylalanine / Lac-Phe → Human exercise-associated circulating Lac-Phe source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text
    experimental_model
    Human metabolomics and endurance/sprint/resistance comparisons.
    limitations
    A biomarker rise is not evidence that taking phenylalanine reproduces exercise benefits.
    nutrient_topic
    L-Phenylalanine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Phenylalanine
    plain_language
    Phenylalanine can join lactate in a metabolite that rises after exercise.
    primary_references
    An exercise-inducible metabolite that suppresses feeding and obesity. · 2022 · https://pubmed.ncbi.nlm.nih.gov/35705806/ · DOI 10.1038/s41586-022-04828-5

    L-Phenylalanine: transport, protein synthesis, cofactor recycling and cross-nutrient mechanisms (2026-09-19) · lines 398–404

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human metabolomics and endurance/sprint/resistance comparisons. · source_derived_draft · unverified_draft

    ## l-phenylalanine-lacphe-exercise Phenylalanine can join lactate in a metabolite that rises after exercise. Lac-Phe rose after exercise in human cohorts of 36 and 8 participants; in the modality comparison, changes tracked lactate and were greatest after sprint exercise. Model: Human metabolomics and endurance/sprint/resistance comparisons. Limitations: A biomarker rise is not evidence that taking phenylalanine reproduces exercise benefits. Evidence access: Primary full text An exercise-inducible metabolite that suppresses feeding and obesity. · 2022 · https://pubmed.ncbi.nlm.nih.gov/35705806/ · DOI 10.1038/s41586-022-04828-5
    Complete structured claim and evidence

  2. Adding Mn2+ was required for full recombinant CNDP2 dipeptidase activity.

    Mn2+ → Human recombinant CNDP2 dipeptidase activity source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Recombinant human CNDP2 characterization.
    limitations
    This does not show that manganese supplements lower carnosine in people.
    nutrient_topic
    Carnosine collection; isomer, preparation, species, exposure and manipulation remain explicit. · L-Carnosine / beta-alanyl-L-histidine
    plain_language
    Manganese supports the enzyme’s measured activity.
    primary_references
    Sequence identification and characterization of human carnosinase and a closely related non-specific dipeptidase. · 2003 · https://pubmed.ncbi.nlm.nih.gov/12473676/ · DOI 10.1074/jbc.M209764200

    Carnosine: synthesis, transport, carbonyl chemistry and nutrient interactions (2026-09-19) · lines 60–66

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Recombinant human CNDP2 characterization. · source_derived_draft · unverified_draft

    ## carnosine-cndp2-manganese Manganese supports the enzyme’s measured activity. Adding Mn2+ was required for full recombinant CNDP2 dipeptidase activity. Model: Recombinant human CNDP2 characterization. Limitations: This does not show that manganese supplements lower carnosine in people. Evidence access: Primary abstract Sequence identification and characterization of human carnosinase and a closely related non-specific dipeptidase. · 2003 · https://pubmed.ncbi.nlm.nih.gov/12473676/ · DOI 10.1074/jbc.M209764200
    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