Component
Human prolidase / PEPD
Context-specific entity; species, compartment and exposure are stated on each claim.
2 recorded relationships. Experimental role, claim status and evidence remain attached to each record.
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.
Other things that act on it
Enzymes, hormones, genes, and other components with a recorded effect. These are not nutrients, so they do not count toward the arrows above. Each finding names the chapter that recorded it.
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.
What it acts on
Human prolidase hydrolyzes dipeptides with C-terminal proline or hydroxyproline; substrate- and product-bound structures explain its terminal peptide-cleavage reaction.
Experimental context and source evidence
- evidence_access
- Primary abstract
- experimental_model
- Recombinant human wild-type prolidase, high-resolution substrate/product complexes.
- limitations
- This does not mean prolidase by itself cleaves an intact collagen triple helix.
- nutrient_topic
- L-Proline collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Proline
- plain_language
- Recycling a proline-containing peptide requires a suitable peptidase.
- primary_references
- Substrate specificity and reaction mechanism of human prolidase. · 2017 · https://pubmed.ncbi.nlm.nih.gov/28677335/ · DOI 10.1111/febs.14158
L-Proline: synthesis, collagen processing, redox metabolism and cross-nutrient mechanisms (2026-09-19) · lines 262–268
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Recombinant human wild-type prolidase, high-resolution substrate/product complexes. · source_derived_draft · unverified_draft
## l-proline-pepd-recycling Recycling a proline-containing peptide requires a suitable peptidase. Human prolidase hydrolyzes dipeptides with C-terminal proline or hydroxyproline; substrate- and product-bound structures explain its terminal peptide-cleavage reaction. Model: Recombinant human wild-type prolidase, high-resolution substrate/product complexes. Limitations: This does not mean prolidase by itself cleaves an intact collagen triple helix. Evidence access: Primary abstract Substrate specificity and reaction mechanism of human prolidase. · 2017 · https://pubmed.ncbi.nlm.nih.gov/28677335/ · DOI 10.1111/febs.14158
Complete structured claim and evidence
What acts on it
Human prolidase structures contain a binuclear manganese active site associated with the hydrolytic reaction; the study proposes hydroxide as the attacking catalytic species.
Experimental context and source evidence
- evidence_access
- Primary abstract and linked primary deposited structure 5M4G
- experimental_model
- Human enzyme crystal structures, including deposited structure 5M4G at 1.48 angstroms.
- limitations
- Structural metal dependence does not establish that adding manganese improves recycling when manganese is already adequate.
- nutrient_topic
- L-Proline collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Proline
- plain_language
- A mineral is part of the machinery that recycles proline from dipeptides.
- primary_references
- Substrate specificity and reaction mechanism of human prolidase. · 2017 · https://pubmed.ncbi.nlm.nih.gov/28677335/ · DOI 10.1111/febs.14158
L-Proline: synthesis, collagen processing, redox metabolism and cross-nutrient mechanisms (2026-09-19) · lines 270–276
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human enzyme crystal structures, including deposited structure 5M4G at 1.48 angstroms. · source_derived_draft · unverified_draft
## l-proline-pepd-manganese A mineral is part of the machinery that recycles proline from dipeptides. Human prolidase structures contain a binuclear manganese active site associated with the hydrolytic reaction; the study proposes hydroxide as the attacking catalytic species. Model: Human enzyme crystal structures, including deposited structure 5M4G at 1.48 angstroms. Limitations: Structural metal dependence does not establish that adding manganese improves recycling when manganese is already adequate. Evidence access: Primary abstract and linked primary deposited structure 5M4G Substrate specificity and reaction mechanism of human prolidase. · 2017 · https://pubmed.ncbi.nlm.nih.gov/28677335/ · DOI 10.1111/febs.14158
Complete structured claim and evidence
The events it takes part in
A mechanism often involves more than two components. These are the full events, with every participant and its role.
Situations it appears in
Low-supply and faulty-machinery situations recorded in the chapters where this component plays a part.
In the sources
Preserved passages that mention this component, quoted exactly. Open one to read it in context.
Open hypotheses
Proposed ideas that involve this component. They are labeled as hypotheses and do not change any recorded statement.
This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.