Component

Human pyrroline-5-carboxylate reductase 2 / PYCR2

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. PYCR2 variants in two families were associated with microcephaly and hypomyelination; engineered PYCR2 loss in HEK293FT cells lowered mitochondrial membrane potential and increased oxidative-stress-induced apoptosis.

    Human pyrroline-5-carboxylate reductase 2 / PYCR2 → Mitochondrial stress response in PYCR2-deficient human cells source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary abstract
    experimental_model
    Human families, variant-expression studies and CRISPR-modified human cells.
    limitations
    This does not prove that low circulating proline is the disease mechanism or that extra substrate rescues it.
    nutrient_topic
    L-Proline collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Proline
    plain_language
    A related enzyme has a distinct neurological disease pattern.
    primary_references
    Mutations in PYCR2, Encoding Pyrroline-5-Carboxylate Reductase 2, Cause Microcephaly and Hypomyelination. · 2015 · https://pubmed.ncbi.nlm.nih.gov/25865492/ · DOI 10.1016/j.ajhg.2015.03.003
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    L-Proline: synthesis, collagen processing, redox metabolism and cross-nutrient mechanisms (2026-09-19) · lines 158–164

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human families, variant-expression studies and CRISPR-modified human cells. · source_derived_draft · unverified_draft

    ## l-proline-pycr2-genetic A related enzyme has a distinct neurological disease pattern. PYCR2 variants in two families were associated with microcephaly and hypomyelination; engineered PYCR2 loss in HEK293FT cells lowered mitochondrial membrane potential and increased oxidative-stress-induced apoptosis. Model: Human families, variant-expression studies and CRISPR-modified human cells. Limitations: This does not prove that low circulating proline is the disease mechanism or that extra substrate rescues it. Evidence access: Primary abstract Mutations in PYCR2, Encoding Pyrroline-5-Carboxylate Reductase 2, Cause Microcephaly and Hypomyelination. · 2015 · https://pubmed.ncbi.nlm.nih.gov/25865492/ · DOI 10.1016/j.ajhg.2015.03.003
    Complete structured claim and evidence

  2. Recombinant human PYCR2 reduced P5C to proline and favored NADH over NADPH under the reported comparison conditions.

    Human pyrroline-5-carboxylate reductase 2 / PYCR2 → L-Proline source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text
    experimental_model
    Purified human PYCR2 and human melanoma-cell localization experiments.
    limitations
    PYCR2 has its own identity and disease associations; it is not interchangeable with PYCR1.
    nutrient_topic
    L-Proline collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Proline
    plain_language
    A second mitochondrial enzyme performs the final reduction.
    primary_references
    Functional specialization in proline biosynthesis of melanoma. · 2012 · https://pubmed.ncbi.nlm.nih.gov/23024808/ · DOI 10.1371/journal.pone.0045190

    L-Proline: synthesis, collagen processing, redox metabolism 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 · Purified human PYCR2 and human melanoma-cell localization experiments. · source_derived_draft · unverified_draft

    ## l-proline-pycr2-reduction A second mitochondrial enzyme performs the final reduction. Recombinant human PYCR2 reduced P5C to proline and favored NADH over NADPH under the reported comparison conditions. Model: Purified human PYCR2 and human melanoma-cell localization experiments. Limitations: PYCR2 has its own identity and disease associations; it is not interchangeable with PYCR1. Evidence access: Primary full text Functional specialization in proline biosynthesis of melanoma. · 2012 · https://pubmed.ncbi.nlm.nih.gov/23024808/ · DOI 10.1371/journal.pone.0045190
    Complete structured claim and evidence

What acts on it

  1. Proline inhibited recombinant PYCR2 more strongly than PYCR1 or PYCRL; approximate apparent inhibition constants were 0.1, 0.6 and 8 mM, respectively.

    L-Proline → Human pyrroline-5-carboxylate reductase 2 / PYCR2 source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text
    experimental_model
    Purified human enzymes; product-inhibition assays, with PYCR2 losing about 90% activity at 0.3 mM proline.
    limitations
    These assay concentrations are not blood targets or supplement recommendations.
    nutrient_topic
    L-Proline collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Proline
    plain_language
    Accumulating product can slow further production, with unequal sensitivity among enzymes.
    primary_references
    Functional specialization in proline biosynthesis of melanoma. · 2012 · https://pubmed.ncbi.nlm.nih.gov/23024808/ · DOI 10.1371/journal.pone.0045190

    L-Proline: synthesis, collagen processing, redox metabolism 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 enzymes; product-inhibition assays, with PYCR2 losing about 90% activity at 0.3 mM proline. · source_derived_draft · unverified_draft

    ## l-proline-product-feedback Accumulating product can slow further production, with unequal sensitivity among enzymes. Proline inhibited recombinant PYCR2 more strongly than PYCR1 or PYCRL; approximate apparent inhibition constants were 0.1, 0.6 and 8 mM, respectively. Model: Purified human enzymes; product-inhibition assays, with PYCR2 losing about 90% activity at 0.3 mM proline. Limitations: These assay concentrations are not blood targets or supplement recommendations. Evidence access: Primary full text Functional specialization in proline biosynthesis of melanoma. · 2012 · https://pubmed.ncbi.nlm.nih.gov/23024808/ · DOI 10.1371/journal.pone.0045190
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Isotope tracing with gene silencing linked glutamine/glutamate-derived proline mainly to PYCR1/PYCR2 and ornithine-derived proline mainly to PYCRL in human melanoma cells.

    L-Ornithine → L-Proline source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text
    experimental_model
    Lu1205 cells; 1 mM labeled precursors for eight hours; ornithine labeling required omission of extracellular proline.
    limitations
    The ornithine experiment used conditions the authors regarded as likely nonphysiological; no universal exclusive routing rule is inferred.
    nutrient_topic
    L-Proline collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Proline
    plain_language
    Two precursor routes can feed the same product through differently placed enzymes.
    primary_references
    Functional specialization in proline biosynthesis of melanoma. · 2012 · https://pubmed.ncbi.nlm.nih.gov/23024808/ · DOI 10.1371/journal.pone.0045190

    L-Proline: synthesis, collagen processing, redox metabolism 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 · Lu1205 cells; 1 mM labeled precursors for eight hours; ornithine labeling required omission of extracellular proline. · source_derived_draft · unverified_draft

    ## l-proline-precursor-routing Two precursor routes can feed the same product through differently placed enzymes. Isotope tracing with gene silencing linked glutamine/glutamate-derived proline mainly to PYCR1/PYCR2 and ornithine-derived proline mainly to PYCRL in human melanoma cells. Model: Lu1205 cells; 1 mM labeled precursors for eight hours; ornithine labeling required omission of extracellular proline. Limitations: The ornithine experiment used conditions the authors regarded as likely nonphysiological; no universal exclusive routing rule is inferred. Evidence access: Primary full text Functional specialization in proline biosynthesis of melanoma. · 2012 · https://pubmed.ncbi.nlm.nih.gov/23024808/ · DOI 10.1371/journal.pone.0045190
    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