Component

O-Phospho-L-serine, free metabolite

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. Human PSAT1 transfers nitrogen from glutamate to phosphohydroxypyruvate, producing O-phosphoserine and 2-oxoglutarate in a reversible PLP-dependent reaction.

    Human phosphoserine aminotransferase / PSAT1 → O-Phospho-L-serine, free metabolite source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text
    experimental_model
    Recombinant human PSAT kinetics and substrate-bound crystal structures.
    limitations
    This is an enzyme reaction, not evidence that dietary glutamate or B6 is limiting in a particular person.
    nutrient_topic
    L-Serine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Serine
    plain_language
    Glutamate supplies nitrogen while active B6 enables the transfer.
    primary_references
    L-serine biosynthesis in the human central nervous system: Structure and function of phosphoserine aminotransferase. · 2023 · https://pubmed.ncbi.nlm.nih.gov/36851825/ · DOI 10.1002/pro.4609

    L-Serine: synthesis, one-carbon metabolism, lipids and cross-nutrient mechanisms (2026-09-19) · lines 30–36

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Recombinant human PSAT kinetics and substrate-bound crystal structures. · source_derived_draft · unverified_draft

    ## l-serine-psat-nitrogen Glutamate supplies nitrogen while active B6 enables the transfer. Human PSAT1 transfers nitrogen from glutamate to phosphohydroxypyruvate, producing O-phosphoserine and 2-oxoglutarate in a reversible PLP-dependent reaction. Model: Recombinant human PSAT kinetics and substrate-bound crystal structures. Limitations: This is an enzyme reaction, not evidence that dietary glutamate or B6 is limiting in a particular person. Evidence access: Primary full text L-serine biosynthesis in the human central nervous system: Structure and function of phosphoserine aminotransferase. · 2023 · https://pubmed.ncbi.nlm.nih.gov/36851825/ · DOI 10.1002/pro.4609
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Human phosphoserine phosphatase catalyzes the final, effectively irreversible dephosphorylation step of the phosphorylated serine synthesis pathway.

    Human phosphoserine phosphatase / PSPH → L-Serine source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Recombinant human PSPH functional analysis.
    limitations
    Free phosphoserine is distinct from a phosphorylated serine residue in a protein.
    nutrient_topic
    L-Serine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Serine
    plain_language
    The last enzyme releases free serine from its phosphorylated precursor.
    primary_references
    Effect of l-serine and magnesium ions on the functional properties of human phosphoserine phosphatase and its pathogenetic variants. · 2024 · https://pubmed.ncbi.nlm.nih.gov/38278334/ · DOI 10.1016/j.bbadis.2024.167034

    L-Serine: synthesis, one-carbon metabolism, lipids and cross-nutrient mechanisms (2026-09-19) · lines 46–52

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Recombinant human PSPH functional analysis. · source_derived_draft · unverified_draft

    ## l-serine-psph-final-step The last enzyme releases free serine from its phosphorylated precursor. Human phosphoserine phosphatase catalyzes the final, effectively irreversible dephosphorylation step of the phosphorylated serine synthesis pathway. Model: Recombinant human PSPH functional analysis. Limitations: Free phosphoserine is distinct from a phosphorylated serine residue in a protein. Evidence access: Primary abstract Effect of l-serine and magnesium ions on the functional properties of human phosphoserine phosphatase and its pathogenetic variants. · 2024 · https://pubmed.ncbi.nlm.nih.gov/38278334/ · DOI 10.1016/j.bbadis.2024.167034
    Complete structured claim and evidence

  2. Human PSPH uses an active-site Mg2+ ion; replacing it with Ca2+ changes coordination of catalytic Asp20 in a way that impedes nucleophilic attack.

    Mg2+ → Human phosphoserine phosphatase / PSPH source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human enzyme crystallography; the calcium-bound structure used 0.7 M CaCl2 crystallization conditions.
    limitations
    The high-calcium structure does not establish inhibition by normal dietary calcium.
    nutrient_topic
    L-Serine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Serine
    plain_language
    Two minerals can bind differently to the same enzyme.
    primary_references
    How calcium inhibits the magnesium-dependent enzyme human phosphoserine phosphatase. · 2004 · https://pubmed.ncbi.nlm.nih.gov/15291819/ · DOI 10.1111/j.0014-2956.2004.04277.x

    L-Serine: synthesis, one-carbon metabolism, lipids and cross-nutrient mechanisms (2026-09-19) · lines 54–60

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human enzyme crystallography; the calcium-bound structure used 0.7 M CaCl2 crystallization conditions. · source_derived_draft · unverified_draft

    ## l-serine-psph-metal Two minerals can bind differently to the same enzyme. Human PSPH uses an active-site Mg2+ ion; replacing it with Ca2+ changes coordination of catalytic Asp20 in a way that impedes nucleophilic attack. Model: Human enzyme crystallography; the calcium-bound structure used 0.7 M CaCl2 crystallization conditions. Limitations: The high-calcium structure does not establish inhibition by normal dietary calcium. Evidence access: Primary abstract How calcium inhibits the magnesium-dependent enzyme human phosphoserine phosphatase. · 2004 · https://pubmed.ncbi.nlm.nih.gov/15291819/ · DOI 10.1111/j.0014-2956.2004.04277.x
    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