Component

Human proline dehydrogenase / PRODH

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

6 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. Mitochondrial PRODH catalyzes the FAD-dependent oxidation of proline to P5C, linking proline breakdown to mitochondrial electron transfer.

    Human proline dehydrogenase / PRODH → Delta-1-pyrroline-5-carboxylate / P5C source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text; background reaction distinguished from new experiments
    experimental_model
    Established reaction described in a primary mitochondrial proline-oxidation study.
    limitations
    The reaction description is biochemical background, distinct from the paper-specific ROS-site experiments.
    nutrient_topic
    L-Proline collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Proline
    plain_language
    Breaking proline down starts with a flavin-dependent mitochondrial enzyme.
    primary_references
    Sources of superoxide/H2O2 during mitochondrial proline oxidation. · 2014 · https://pubmed.ncbi.nlm.nih.gov/25184115/ · DOI 10.1016/j.redox.2014.07.003

    L-Proline: synthesis, collagen processing, redox metabolism 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 · Established reaction described in a primary mitochondrial proline-oxidation study. · source_derived_draft · unverified_draft

    ## l-proline-prodh-oxidation Breaking proline down starts with a flavin-dependent mitochondrial enzyme. Mitochondrial PRODH catalyzes the FAD-dependent oxidation of proline to P5C, linking proline breakdown to mitochondrial electron transfer. Model: Established reaction described in a primary mitochondrial proline-oxidation study. Limitations: The reaction description is biochemical background, distinct from the paper-specific ROS-site experiments. Evidence access: Primary full text; background reaction distinguished from new experiments Sources of superoxide/H2O2 during mitochondrial proline oxidation. · 2014 · https://pubmed.ncbi.nlm.nih.gov/25184115/ · DOI 10.1016/j.redox.2014.07.003
    Complete structured claim and evidence

  2. Blocking proline catabolism in human RPE impaired glucose metabolism and glutathione production.

    Human proline dehydrogenase / PRODH → Glucose metabolism and glutathione production in human RPE source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary abstract
    experimental_model
    Human RPE culture with pharmacological catabolism inhibition and metabolite measurements.
    limitations
    Pharmacological specificity and culture conditions limit inference; no human blood-proline threshold is established.
    nutrient_topic
    L-Proline collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Proline
    plain_language
    A block in proline use can affect antioxidant production indirectly.
    primary_references
    Proline mediates metabolic communication between retinal pigment epithelial cells and the retina. · 2019 · https://pubmed.ncbi.nlm.nih.gov/31110046/ · DOI 10.1074/jbc.RA119.007983
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    L-Proline: synthesis, collagen processing, redox metabolism and cross-nutrient mechanisms (2026-09-19) · lines 318–324

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human RPE culture with pharmacological catabolism inhibition and metabolite measurements. · source_derived_draft · unverified_draft

    ## l-proline-rpe-catabolism-block A block in proline use can affect antioxidant production indirectly. Blocking proline catabolism in human RPE impaired glucose metabolism and glutathione production. Model: Human RPE culture with pharmacological catabolism inhibition and metabolite measurements. Limitations: Pharmacological specificity and culture conditions limit inference; no human blood-proline threshold is established. Evidence access: Primary abstract Proline mediates metabolic communication between retinal pigment epithelial cells and the retina. · 2019 · https://pubmed.ncbi.nlm.nih.gov/31110046/ · DOI 10.1074/jbc.RA119.007983
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Purified truncated human PRODH2/HYPDH contained one FAD and showed approximately twelvefold higher catalytic efficiency for hydroxyproline than proline.

    Human hydroxyproline dehydrogenase / PRODH2 → 4-Hydroxyproline source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human recombinant catalytic core, residues 157–515; substrate kinetics.
    limitations
    PRODH2 is not simply a second interchangeable proline oxidase.
    nutrient_topic
    L-Proline collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Proline
    plain_language
    Hydroxyproline uses a related but distinct breakdown enzyme.
    primary_references
    Proline dehydrogenase 2 (PRODH2) is a hydroxyproline dehydrogenase (HYPDH) and molecular target for treating primary hyperoxaluria. · 2015 · https://pubmed.ncbi.nlm.nih.gov/25697095/ · DOI 10.1042/BJ20141159

    L-Proline: synthesis, collagen processing, redox metabolism and cross-nutrient mechanisms (2026-09-19) · lines 278–284

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human recombinant catalytic core, residues 157–515; substrate kinetics. · source_derived_draft · unverified_draft

    ## l-proline-hypdh-specificity Hydroxyproline uses a related but distinct breakdown enzyme. Purified truncated human PRODH2/HYPDH contained one FAD and showed approximately twelvefold higher catalytic efficiency for hydroxyproline than proline. Model: Human recombinant catalytic core, residues 157–515; substrate kinetics. Limitations: PRODH2 is not simply a second interchangeable proline oxidase. Evidence access: Primary abstract Proline dehydrogenase 2 (PRODH2) is a hydroxyproline dehydrogenase (HYPDH) and molecular target for treating primary hyperoxaluria. · 2015 · https://pubmed.ncbi.nlm.nih.gov/25697095/ · DOI 10.1042/BJ20141159
    Complete structured claim and evidence

  2. Human pancreatic cancer cells took up collagen fragments and used collagen-derived proline in metabolism under nutrient-limited culture conditions.

    Collagen-bound proline residues → Collagen-derived proline metabolism in human pancreatic cancer cells source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text
    experimental_model
    Human PDAC culture and tracer experiments under limited fuel availability.
    limitations
    Collagen uptake, peptide digestion and proline oxidation are distinct steps; no effect of oral collagen supplements is demonstrated.
    nutrient_topic
    L-Proline collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Proline
    plain_language
    A tissue matrix can become a nutrient reservoir for cells.
    primary_references
    Collagen-derived proline promotes pancreatic ductal adenocarcinoma cell survival under nutrient limited conditions. · 2017 · https://pubmed.ncbi.nlm.nih.gov/28685754/ · DOI 10.1038/ncomms16031

    L-Proline: synthesis, collagen processing, redox metabolism and cross-nutrient mechanisms (2026-09-19) · lines 374–380

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human PDAC culture and tracer experiments under limited fuel availability. · source_derived_draft · unverified_draft

    ## l-proline-pdac-collagen-fuel A tissue matrix can become a nutrient reservoir for cells. Human pancreatic cancer cells took up collagen fragments and used collagen-derived proline in metabolism under nutrient-limited culture conditions. Model: Human PDAC culture and tracer experiments under limited fuel availability. Limitations: Collagen uptake, peptide digestion and proline oxidation are distinct steps; no effect of oral collagen supplements is demonstrated. Evidence access: Primary full text Collagen-derived proline promotes pancreatic ductal adenocarcinoma cell survival under nutrient limited conditions. · 2017 · https://pubmed.ncbi.nlm.nih.gov/28685754/ · DOI 10.1038/ncomms16031
    Complete structured claim and evidence

  3. Isolated mitochondria from human ZR75-30 breast cancer cells consumed oxygen with proline as the sole added substrate.

    L-Proline → Proline-supported respiration in human ZR75-30 mitochondria source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text
    experimental_model
    Isolated human cancer-cell mitochondria.
    limitations
    Fuel use in this model does not quantify whole-body energy contribution or show a supplement benefit.
    nutrient_topic
    L-Proline collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Proline
    plain_language
    In this model, proline can help fuel mitochondrial respiration.
    primary_references
    Sources of superoxide/H2O2 during mitochondrial proline oxidation. · 2014 · https://pubmed.ncbi.nlm.nih.gov/25184115/ · DOI 10.1016/j.redox.2014.07.003

    L-Proline: synthesis, collagen processing, redox metabolism and cross-nutrient mechanisms (2026-09-19) · lines 134–140

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

    ## l-proline-proline-respiration In this model, proline can help fuel mitochondrial respiration. Isolated mitochondria from human ZR75-30 breast cancer cells consumed oxygen with proline as the sole added substrate. Model: Isolated human cancer-cell mitochondria. Limitations: Fuel use in this model does not quantify whole-body energy contribution or show a supplement benefit. Evidence access: Primary full text Sources of superoxide/H2O2 during mitochondrial proline oxidation. · 2014 · https://pubmed.ncbi.nlm.nih.gov/25184115/ · DOI 10.1016/j.redox.2014.07.003
    Complete structured claim and evidence

  4. During proline oxidation in ZR75-30 mitochondria, the main measured ROS sources were complex I and 2-oxoglutarate dehydrogenase, with no significant direct PRODH contribution under the tested substrate/inhibitor conditions.

    L-Proline → Sites of ROS formation during proline oxidation in ZR75-30 mitochondria source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text
    experimental_model
    Isolated human mitochondria; inhibitor combinations used to distinguish ROS-generating sites.
    limitations
    Results in Drosophila instead emphasized complexes I and II; these species-specific observations do not identify a universal source.
    nutrient_topic
    L-Proline collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Proline
    plain_language
    A pathway can increase ROS without its first enzyme being the direct ROS-producing site.
    primary_references
    Sources of superoxide/H2O2 during mitochondrial proline oxidation. · 2014 · https://pubmed.ncbi.nlm.nih.gov/25184115/ · DOI 10.1016/j.redox.2014.07.003

    L-Proline: synthesis, collagen processing, redox metabolism and cross-nutrient mechanisms (2026-09-19) · lines 142–148

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Isolated human mitochondria; inhibitor combinations used to distinguish ROS-generating sites. · source_derived_draft · unverified_draft

    ## l-proline-ros-source-boundary A pathway can increase ROS without its first enzyme being the direct ROS-producing site. During proline oxidation in ZR75-30 mitochondria, the main measured ROS sources were complex I and 2-oxoglutarate dehydrogenase, with no significant direct PRODH contribution under the tested substrate/inhibitor conditions. Model: Isolated human mitochondria; inhibitor combinations used to distinguish ROS-generating sites. Limitations: Results in Drosophila instead emphasized complexes I and II; these species-specific observations do not identify a universal source. Evidence access: Primary full text Sources of superoxide/H2O2 during mitochondrial proline oxidation. · 2014 · https://pubmed.ncbi.nlm.nih.gov/25184115/ · DOI 10.1016/j.redox.2014.07.003
    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.

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