Component

Human pyrroline-5-carboxylate reductase 3 / PYCR3 / PYCRL

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. Human PYCRL/PYCR3 localized predominantly to the cytosol in the tested melanoma cells and was more efficient with NADPH in the biochemical comparison.

    Human pyrroline-5-carboxylate reductase 3 / PYCR3 / PYCRL → L-Proline source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text
    experimental_model
    Lu1205 cell fractionation and recombinant human PYCRL kinetics.
    limitations
    The melanoma routing pattern is not asserted to apply identically in every human tissue.
    nutrient_topic
    L-Proline collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Proline
    plain_language
    The cytosolic version has different preferences from the mitochondrial 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 30–36

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Lu1205 cell fractionation and recombinant human PYCRL kinetics. · source_derived_draft · unverified_draft

    ## l-proline-pycr3-reduction The cytosolic version has different preferences from the mitochondrial enzymes. Human PYCRL/PYCR3 localized predominantly to the cytosol in the tested melanoma cells and was more efficient with NADPH in the biochemical comparison. Model: Lu1205 cell fractionation and recombinant human PYCRL kinetics. Limitations: The melanoma routing pattern is not asserted to apply identically in every human tissue. 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

  2. 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

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