Component
3-Phosphoglycerate
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.
Where it participates (unsigned role)
Purified NADHX species inhibited recombinant human PHGDH, supporting direct inhibition as an explanation for the serine-synthesis defect in NAXD-deficient cells.
Experimental context and source evidence
- evidence_access
- Primary full text
- experimental_model
- Recombinant enzyme assays, including 40 micromolar 3-phosphoglycerate substrate.
- limitations
- NADHX is chemically damaged NADH, not simply a low NAD+ concentration.
- nutrient_topic
- L-Serine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Serine
- plain_language
- Repair of a niacin-derived cofactor protects a separate amino-acid pathway.
- primary_references
- Failure to repair damaged NAD(P)H blocks de novo serine synthesis in human cells. · 2025 · https://pubmed.ncbi.nlm.nih.gov/39789421/ · DOI 10.1186/s11658-024-00681-8
L-Serine: synthesis, one-carbon metabolism, lipids and cross-nutrient mechanisms (2026-09-19) · lines 126–132
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Recombinant enzyme assays, including 40 micromolar 3-phosphoglycerate substrate. · source_derived_draft · unverified_draft
## l-serine-nadhx-inhibition Repair of a niacin-derived cofactor protects a separate amino-acid pathway. Purified NADHX species inhibited recombinant human PHGDH, supporting direct inhibition as an explanation for the serine-synthesis defect in NAXD-deficient cells. Model: Recombinant enzyme assays, including 40 micromolar 3-phosphoglycerate substrate. Limitations: NADHX is chemically damaged NADH, not simply a low NAD+ concentration. Evidence access: Primary full text Failure to repair damaged NAD(P)H blocks de novo serine synthesis in human cells. · 2025 · https://pubmed.ncbi.nlm.nih.gov/39789421/ · DOI 10.1186/s11658-024-00681-8
Complete structured claim and evidenceHuman PHGDH catalyzes the NAD+-dependent oxidation of 3-phosphoglycerate to phosphohydroxypyruvate, the first step of phosphorylated serine biosynthesis.
Experimental context and source evidence
- evidence_access
- Primary abstract
- experimental_model
- Recombinant human PHGDH catalytic-domain structure and enzyme assays.
- limitations
- The truncated dimeric structure does not define the complete native oligomer.
- nutrient_topic
- L-Serine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Serine
- plain_language
- A glycolysis intermediate can be diverted into serine production.
- primary_references
- Structural insights into the enzymatic activity and potential substrate promiscuity of human 3-phosphoglycerate dehydrogenase (PHGDH). · 2017 · https://pubmed.ncbi.nlm.nih.gov/29262655/ · DOI 10.18632/oncotarget.22327
L-Serine: synthesis, one-carbon metabolism, lipids and cross-nutrient mechanisms (2026-09-19) · lines 14–20
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Recombinant human PHGDH catalytic-domain structure and enzyme assays. · source_derived_draft · unverified_draft
## l-serine-phgdh-reaction A glycolysis intermediate can be diverted into serine production. Human PHGDH catalyzes the NAD+-dependent oxidation of 3-phosphoglycerate to phosphohydroxypyruvate, the first step of phosphorylated serine biosynthesis. Model: Recombinant human PHGDH catalytic-domain structure and enzyme assays. Limitations: The truncated dimeric structure does not define the complete native oligomer. Evidence access: Primary abstract Structural insights into the enzymatic activity and potential substrate promiscuity of human 3-phosphoglycerate dehydrogenase (PHGDH). · 2017 · https://pubmed.ncbi.nlm.nih.gov/29262655/ · DOI 10.18632/oncotarget.22327
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.