Component

D-Proline

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 acts on it

  1. Purified C. difficile proline reductase contained PrdA and selenocysteine-containing PrdB and used D-proline; its stereospecific activity is distinct from human L-proline oxidation.

    Clostridioides difficile D-proline reductase complex → D-Proline source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Purified bacterial reductase and substrate tests.
    limitations
    L-proline-linked fermentation requires stereochemical processing; this enzyme is not a human PRODH isoform.
    nutrient_topic
    L-Proline collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Proline
    plain_language
    Gut bacteria can use a different form of proline with different machinery.
    primary_references
    Analysis of proline reduction in the nosocomial pathogen Clostridium difficile. · 2006 · https://pubmed.ncbi.nlm.nih.gov/17041035/ · DOI 10.1128/JB.01370-06

    L-Proline: synthesis, collagen processing, redox metabolism and cross-nutrient mechanisms (2026-09-19) · lines 406–412

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Purified bacterial reductase and substrate tests. · source_derived_draft · unverified_draft

    ## l-proline-microbial-stereospecificity Gut bacteria can use a different form of proline with different machinery. Purified C. difficile proline reductase contained PrdA and selenocysteine-containing PrdB and used D-proline; its stereospecific activity is distinct from human L-proline oxidation. Model: Purified bacterial reductase and substrate tests. Limitations: L-proline-linked fermentation requires stereochemical processing; this enzyme is not a human PRODH isoform. Evidence access: Primary abstract Analysis of proline reduction in the nosocomial pathogen Clostridium difficile. · 2006 · https://pubmed.ncbi.nlm.nih.gov/17041035/ · DOI 10.1128/JB.01370-06
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Selenium supplementation was required for the increased bacterial growth yield seen with the tested Stickland amino-acid pairs; proline-related acceptors induced selenoenzyme expression.

    Selenium → C. difficile growth during selenium-dependent Stickland fermentation source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Anaerobic C. difficile culture in limiting medium; selenite supplementation and radiolabeled selenium protein analysis.
    limitations
    This bacterial growth mechanism does not establish that dietary selenium causes or prevents infection.
    nutrient_topic
    L-Proline collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Proline
    plain_language
    Selenium also supports some microbial amino-acid fermentation pathways.
    primary_references
    Analysis of proline reduction in the nosocomial pathogen Clostridium difficile. · 2006 · https://pubmed.ncbi.nlm.nih.gov/17041035/ · DOI 10.1128/JB.01370-06

    L-Proline: synthesis, collagen processing, redox metabolism and cross-nutrient mechanisms (2026-09-19) · lines 414–420

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Anaerobic C. difficile culture in limiting medium; selenite supplementation and radiolabeled selenium protein analysis. · source_derived_draft · unverified_draft

    ## l-proline-microbial-selenium Selenium also supports some microbial amino-acid fermentation pathways. Selenium supplementation was required for the increased bacterial growth yield seen with the tested Stickland amino-acid pairs; proline-related acceptors induced selenoenzyme expression. Model: Anaerobic C. difficile culture in limiting medium; selenite supplementation and radiolabeled selenium protein analysis. Limitations: This bacterial growth mechanism does not establish that dietary selenium causes or prevents infection. Evidence access: Primary abstract Analysis of proline reduction in the nosocomial pathogen Clostridium difficile. · 2006 · https://pubmed.ncbi.nlm.nih.gov/17041035/ · DOI 10.1128/JB.01370-06
    Complete structured claim and evidence

  2. Zinc strongly inhibited purified C. difficile D-proline reductase, which did not require added divalent cations for its measured activity.

    Zinc(II) ion → Clostridioides difficile D-proline reductase complex source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Purified bacterial-enzyme assays.
    limitations
    No safe or effective intestinal zinc intervention is established by the enzyme experiment.
    nutrient_topic
    L-Proline collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Proline
    plain_language
    A mineral can inhibit this microbial enzyme rather than serve as its cofactor.
    primary_references
    Analysis of proline reduction in the nosocomial pathogen Clostridium difficile. · 2006 · https://pubmed.ncbi.nlm.nih.gov/17041035/ · DOI 10.1128/JB.01370-06

    L-Proline: synthesis, collagen processing, redox metabolism and cross-nutrient mechanisms (2026-09-19) · lines 422–428

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

    ## l-proline-microbial-zinc A mineral can inhibit this microbial enzyme rather than serve as its cofactor. Zinc strongly inhibited purified C. difficile D-proline reductase, which did not require added divalent cations for its measured activity. Model: Purified bacterial-enzyme assays. Limitations: No safe or effective intestinal zinc intervention is established by the enzyme experiment. Evidence access: Primary abstract Analysis of proline reduction in the nosocomial pathogen Clostridium difficile. · 2006 · https://pubmed.ncbi.nlm.nih.gov/17041035/ · DOI 10.1128/JB.01370-06
    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