Component
Human hydroxyproline dehydrogenase / PRODH2
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
Quinone acceptors including CoQ1 reacted more efficiently than oxygen during purified human HYPDH turnover, supporting a dehydrogenase mechanism.
Experimental context and source evidence
- evidence_access
- Primary abstract
- experimental_model
- Truncated purified human HYPDH; quinone analogue and oxygen comparisons.
- limitations
- CoQ10 as the physiological acceptor is inferred, not directly measured in intact human tissues; this does not demonstrate benefit from CoQ10 supplements.
- nutrient_topic
- L-Proline collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Proline
- plain_language
- Hydroxyproline breakdown can feed a quinone electron-transfer route.
- 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 286–292
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Truncated purified human HYPDH; quinone analogue and oxygen comparisons. · source_derived_draft · unverified_draft
## l-proline-hypdh-electrons Hydroxyproline breakdown can feed a quinone electron-transfer route. Quinone acceptors including CoQ1 reacted more efficiently than oxygen during purified human HYPDH turnover, supporting a dehydrogenase mechanism. Model: Truncated purified human HYPDH; quinone analogue and oxygen comparisons. Limitations: CoQ10 as the physiological acceptor is inferred, not directly measured in intact human tissues; this does not demonstrate benefit from CoQ10 supplements. 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 evidencePurified truncated human PRODH2/HYPDH contained one FAD and showed approximately twelvefold higher catalytic efficiency for hydroxyproline than proline.
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
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.