Component

IMPA1 (human inositol monophosphatase 1)

IMPA1 (human inositol monophosphatase 1). Species, exposure and limitations are retained in each linked claim.

7 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 it acts on

  1. Human inositol monophosphatase hydrolyzes inositol monophosphates to regenerate free inositol.

    IMPA1 (human inositol monophosphatase 1) → Inositol monophosphates source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/inositol-research/1332026.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "57cfa39b1fe68149ad3a1ea25ede4c979db0586ef14c905cbe402fe3f70ce9e5", "start_char": 0, "end_char": 1147, "text_sha256": "57cfa39b1fe68149ad3a1ea25ede4c979db0586ef14c905cbe402fe3f70ce9e5"}
    experimental_model
    Human enzyme crystallography and catalytic characterization
    exposure
    Structural analysis of the inositol recycling enzyme
    limitations
    Structure does not show that extra substrate bypasses a genetic enzyme defect in patients.
    nutrient_topic
    Inositol research collection; topical membership is not evidence of a direct dietary effect. · Inositol (stereoisomer family)
    organism
    Homo sapiens
    plain_language
    A recycling step removes the last phosphate so the inositol ring can be reused.
    primary_references
    [ino-p1332026] Structure of inositol monophosphatase, the putative target of lithium therapy. (1992). https://pubmed.ncbi.nlm.nih.gov/1332026/ DOI: 10.1073/pnas.89.21.10031
    tissue_or_cell_type
    Purified inositol monophosphatase

    Inositol: synthesis, signaling, mineral interactions and conditional deficiency (2026-09-17) · lines 236–247

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human enzyme crystallography and catalytic characterization · source_derived_draft · unverified_draft

    ### ino-impa-recycling Human inositol monophosphatase hydrolyzes inositol monophosphates to regenerate free inositol. Condition category: normal nutrient_topic: Inositol research collection; topical membership is not evidence of a direct dietary effect. plain_language: A recycling step removes the last phosphate so the inositol ring can be reused. organism: Homo sapiens tissue_or_cell_type: Purified inositol monophosphatase experimental_model: Human enzyme crystallography and catalytic characterization limitations: Structure does not show that extra substrate bypasses a genetic enzyme defect in patients. exposure: Structural analysis of the inositol recycling enzyme evidence_span: {"source_cache": "artifacts/inositol-research/1332026.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "57cfa39b1fe68149ad3a1ea25ede4c979db0586ef14c905cbe402fe3f70ce9e5", "start_char": 0, "end_char": 1147, "text_sha256": "57cfa39b1fe68149ad3a1ea25ede4c979db0586ef14c905cbe402fe3f70ce9e5"} [ino-p1332026] Structure of inositol monophosphatase, the putative target of lithium therapy. (1992). https://pubmed.ncbi.nlm.nih.gov/1332026/ DOI: 10.1073/pnas.89.21.10031
    Complete structured claim and evidence

  2. IMPA1-deficient patient-derived neuronal progenitors showed impaired proliferation, cell-cycle arrest, apoptosis and reduced neuronal differentiation.

    IMPA1 (human inositol monophosphatase 1) → Neural progenitor survival and neurogenesis source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_span
    {"source_cache": "artifacts/inositol-research/32839513.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "5ca10517672cac78ad8cdb0c593f14f73f1989e55977432d979690eebc3eefed", "start_char": 0, "end_char": 1711, "text_sha256": "5ca10517672cac78ad8cdb0c593f14f73f1989e55977432d979690eebc3eefed"}
    experimental_model
    Patient-derived iPSC differentiation and rescue
    exposure
    Biallelic IMPA1 defect and myo-inositol-supplemented medium
    limitations
    Cellular rescue is not demonstrated neurological benefit in treated patients; effects were lineage-specific.
    nutrient_topic
    Inositol research collection; topical membership is not evidence of a direct dietary effect. · Inositol (stereoisomer family)
    organism
    Homo sapiens
    plain_language
    Failure of the inositol-processing machinery affected developing nerve cells.
    primary_references
    [ino-p32839513] Inositol monophosphatase 1 (IMPA1) mutation in intellectual disability patients impairs neurogenesis but not gliogenesis. (2021). https://pubmed.ncbi.nlm.nih.gov/32839513/ DOI: 10.1038/s41380-020-00862-9
    tissue_or_cell_type
    Hippocampal dentate-gyrus-like neuronal progenitors
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Inositol: synthesis, signaling, mineral interactions and conditional deficiency (2026-09-17) · lines 1263–1274

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Patient-derived iPSC differentiation and rescue · source_derived_draft · unverified_draft

    ### ino-impa1-progenitors IMPA1-deficient patient-derived neuronal progenitors showed impaired proliferation, cell-cycle arrest, apoptosis and reduced neuronal differentiation. Condition category: machinery_impairment nutrient_topic: Inositol research collection; topical membership is not evidence of a direct dietary effect. plain_language: Failure of the inositol-processing machinery affected developing nerve cells. organism: Homo sapiens tissue_or_cell_type: Hippocampal dentate-gyrus-like neuronal progenitors experimental_model: Patient-derived iPSC differentiation and rescue limitations: Cellular rescue is not demonstrated neurological benefit in treated patients; effects were lineage-specific. exposure: Biallelic IMPA1 defect and myo-inositol-supplemented medium evidence_span: {"source_cache": "artifacts/inositol-research/32839513.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "5ca10517672cac78ad8cdb0c593f14f73f1989e55977432d979690eebc3eefed", "start_char": 0, "end_char": 1711, "text_sha256": "5ca10517672cac78ad8cdb0c593f14f73f1989e55977432d979690eebc3eefed"} [ino-p32839513] Inositol monophosphatase 1 (IMPA1) mutation in intellectual disability patients impairs neurogenesis but not gliogenesis. (2021). https://pubmed.ncbi.nlm.nih.gov/32839513/ DOI: 10.1038/s41380-020-00862-9
    Complete structured claim and evidence

What acts on it

  1. The human IMPase study supported lithium binding at the second metal site in its catalytic model.

    Lithium ion (Li+) → IMPA1 (human inositol monophosphatase 1) source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human enzyme kinetics, fluorescence and structural modeling.
    limitations
    Binding-site assignment is model-supported; treatment benefit is not established by enzyme inhibition.
    nutrient_topic
    Lithium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Lithium
    plain_language
    Lithium can interrupt the recycling step.
    primary_references
    Mechanism of inositol monophosphatase, the putative target of lithium therapy. · 1994 · https://pubmed.ncbi.nlm.nih.gov/8016062/ · DOI 10.1073/pnas.91.13.5766

    Lithium: metal-sensitive enzymes, transport and cross-nutrient mechanisms (2026-09-19) · lines 40–46

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human enzyme kinetics, fluorescence and structural modeling. · source_derived_draft · unverified_draft

    ## lithium-impa-lithium Lithium can interrupt the recycling step. The human IMPase study supported lithium binding at the second metal site in its catalytic model. Model: Human enzyme kinetics, fluorescence and structural modeling. Limitations: Binding-site assignment is model-supported; treatment benefit is not established by enzyme inhibition. Evidence access: Primary abstract Mechanism of inositol monophosphatase, the putative target of lithium therapy. · 1994 · https://pubmed.ncbi.nlm.nih.gov/8016062/ · DOI 10.1073/pnas.91.13.5766
    Complete structured claim and evidence

  2. Kinetics, modeling and mutagenesis supported a two-metal catalytic model for human inositol monophosphatase.

    Mg2+ → IMPA1 (human inositol monophosphatase 1) source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human enzyme structural/kinetic study, including Mn, Zn and Mg titrations.
    limitations
    Historical mechanistic model; not a universal count for all conformations or family members.
    nutrient_topic
    Lithium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Lithium
    plain_language
    Inositol recycling uses metal-dependent chemistry.
    primary_references
    Mechanism of inositol monophosphatase, the putative target of lithium therapy. · 1994 · https://pubmed.ncbi.nlm.nih.gov/8016062/ · DOI 10.1073/pnas.91.13.5766

    Lithium: metal-sensitive enzymes, transport and cross-nutrient mechanisms (2026-09-19) · lines 32–38

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human enzyme structural/kinetic study, including Mn, Zn and Mg titrations. · source_derived_draft · unverified_draft

    ## lithium-impa-metal Inositol recycling uses metal-dependent chemistry. Kinetics, modeling and mutagenesis supported a two-metal catalytic model for human inositol monophosphatase. Model: Human enzyme structural/kinetic study, including Mn, Zn and Mg titrations. Limitations: Historical mechanistic model; not a universal count for all conformations or family members. Evidence access: Primary abstract Mechanism of inositol monophosphatase, the putative target of lithium therapy. · 1994 · https://pubmed.ncbi.nlm.nih.gov/8016062/ · DOI 10.1073/pnas.91.13.5766
    Complete structured claim and evidence

  3. High Mg2+ concentrations inhibited human inositol monophosphatase uncompetitively with respect to substrate.

    Mg2+ → IMPA1 (human inositol monophosphatase 1) source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/inositol-research/8223565.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "945d1d5166ce6410cd69984d93aebf127b635dcfcebddba31f0e8cc8b1c304a5", "start_char": 0, "end_char": 1621, "text_sha256": "945d1d5166ce6410cd69984d93aebf127b635dcfcebddba31f0e8cc8b1c304a5"}
    experimental_model
    Site-directed mutagenesis and enzyme kinetics
    exposure
    Magnesium and lithium titrations
    limitations
    Biochemical concentration dependence; neither lithium treatment mechanism nor magnesium supplementation response is established by this assay alone.
    nutrient_topic
    Inositol research collection; topical membership is not evidence of a direct dietary effect. · Inositol (stereoisomer family)
    organism
    Human recombinant protein
    plain_language
    An enzyme can need a mineral yet become inhibited when its concentration is too high.
    primary_references
    [ino-p8223565] Probing the role of metal ions in the mechanism of inositol monophosphatase by site-directed mutagenesis. (1993). https://pubmed.ncbi.nlm.nih.gov/8223565/ DOI: 10.1111/j.1432-1033.1993.tb18244.x
    tissue_or_cell_type
    Purified IMPA1

    Inositol: synthesis, signaling, mineral interactions and conditional deficiency (2026-09-17) · lines 262–273

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Site-directed mutagenesis and enzyme kinetics · source_derived_draft · unverified_draft

    ### ino-impa-high-magnesium High Mg2+ concentrations inhibited human inositol monophosphatase uncompetitively with respect to substrate. Condition category: normal nutrient_topic: Inositol research collection; topical membership is not evidence of a direct dietary effect. plain_language: An enzyme can need a mineral yet become inhibited when its concentration is too high. organism: Human recombinant protein tissue_or_cell_type: Purified IMPA1 experimental_model: Site-directed mutagenesis and enzyme kinetics limitations: Biochemical concentration dependence; neither lithium treatment mechanism nor magnesium supplementation response is established by this assay alone. exposure: Magnesium and lithium titrations evidence_span: {"source_cache": "artifacts/inositol-research/8223565.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "945d1d5166ce6410cd69984d93aebf127b635dcfcebddba31f0e8cc8b1c304a5", "start_char": 0, "end_char": 1621, "text_sha256": "945d1d5166ce6410cd69984d93aebf127b635dcfcebddba31f0e8cc8b1c304a5"} [ino-p8223565] Probing the role of metal ions in the mechanism of inositol monophosphatase by site-directed mutagenesis. (1993). https://pubmed.ncbi.nlm.nih.gov/8223565/ DOI: 10.1111/j.1432-1033.1993.tb18244.x
    Complete structured claim and evidence

  4. Li+ inhibited human inositol monophosphatase; parallel changes in Li+ and Mg2+ affinity across mutants supported a shared metal-binding site.

    Lithium ion (Li+) → IMPA1 (human inositol monophosphatase 1) source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_span
    {"source_cache": "artifacts/inositol-research/8223565.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "945d1d5166ce6410cd69984d93aebf127b635dcfcebddba31f0e8cc8b1c304a5", "start_char": 0, "end_char": 1621, "text_sha256": "945d1d5166ce6410cd69984d93aebf127b635dcfcebddba31f0e8cc8b1c304a5"}
    experimental_model
    Site-directed mutagenesis and enzyme kinetics
    exposure
    Magnesium and lithium titrations
    limitations
    Biochemical concentration dependence; neither lithium treatment mechanism nor magnesium supplementation response is established by this assay alone.
    nutrient_topic
    Inositol research collection; topical membership is not evidence of a direct dietary effect. · Inositol (stereoisomer family)
    organism
    Human recombinant protein
    plain_language
    Lithium can interfere with a magnesium-linked step of inositol recycling.
    primary_references
    [ino-p8223565] Probing the role of metal ions in the mechanism of inositol monophosphatase by site-directed mutagenesis. (1993). https://pubmed.ncbi.nlm.nih.gov/8223565/ DOI: 10.1111/j.1432-1033.1993.tb18244.x
    tissue_or_cell_type
    Purified IMPA1
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Inositol: synthesis, signaling, mineral interactions and conditional deficiency (2026-09-17) · lines 275–286

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Site-directed mutagenesis and enzyme kinetics · source_derived_draft · unverified_draft

    ### ino-impa-lithium Li+ inhibited human inositol monophosphatase; parallel changes in Li+ and Mg2+ affinity across mutants supported a shared metal-binding site. Condition category: machinery_impairment nutrient_topic: Inositol research collection; topical membership is not evidence of a direct dietary effect. plain_language: Lithium can interfere with a magnesium-linked step of inositol recycling. organism: Human recombinant protein tissue_or_cell_type: Purified IMPA1 experimental_model: Site-directed mutagenesis and enzyme kinetics limitations: Biochemical concentration dependence; neither lithium treatment mechanism nor magnesium supplementation response is established by this assay alone. exposure: Magnesium and lithium titrations evidence_span: {"source_cache": "artifacts/inositol-research/8223565.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "945d1d5166ce6410cd69984d93aebf127b635dcfcebddba31f0e8cc8b1c304a5", "start_char": 0, "end_char": 1621, "text_sha256": "945d1d5166ce6410cd69984d93aebf127b635dcfcebddba31f0e8cc8b1c304a5"} [ino-p8223565] Probing the role of metal ions in the mechanism of inositol monophosphatase by site-directed mutagenesis. (1993). https://pubmed.ncbi.nlm.nih.gov/8223565/ DOI: 10.1111/j.1432-1033.1993.tb18244.x
    Complete structured claim and evidence

  5. Mg2+ was essential for human inositol monophosphatase activity.

    Mg2+ → IMPA1 (human inositol monophosphatase 1) source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/inositol-research/8223565.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "945d1d5166ce6410cd69984d93aebf127b635dcfcebddba31f0e8cc8b1c304a5", "start_char": 0, "end_char": 1621, "text_sha256": "945d1d5166ce6410cd69984d93aebf127b635dcfcebddba31f0e8cc8b1c304a5"}
    experimental_model
    Site-directed mutagenesis and enzyme kinetics
    exposure
    Magnesium and lithium titrations
    limitations
    Biochemical concentration dependence; neither lithium treatment mechanism nor magnesium supplementation response is established by this assay alone.
    nutrient_topic
    Inositol research collection; topical membership is not evidence of a direct dietary effect. · Inositol (stereoisomer family)
    organism
    Human recombinant protein
    plain_language
    Inositol recycling needs magnesium at the enzyme level.
    primary_references
    [ino-p8223565] Probing the role of metal ions in the mechanism of inositol monophosphatase by site-directed mutagenesis. (1993). https://pubmed.ncbi.nlm.nih.gov/8223565/ DOI: 10.1111/j.1432-1033.1993.tb18244.x
    tissue_or_cell_type
    Purified IMPA1

    Inositol: synthesis, signaling, mineral interactions and conditional deficiency (2026-09-17) · lines 249–260

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Site-directed mutagenesis and enzyme kinetics · source_derived_draft · unverified_draft

    ### ino-impa-magnesium Mg2+ was essential for human inositol monophosphatase activity. Condition category: normal nutrient_topic: Inositol research collection; topical membership is not evidence of a direct dietary effect. plain_language: Inositol recycling needs magnesium at the enzyme level. organism: Human recombinant protein tissue_or_cell_type: Purified IMPA1 experimental_model: Site-directed mutagenesis and enzyme kinetics limitations: Biochemical concentration dependence; neither lithium treatment mechanism nor magnesium supplementation response is established by this assay alone. exposure: Magnesium and lithium titrations evidence_span: {"source_cache": "artifacts/inositol-research/8223565.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "945d1d5166ce6410cd69984d93aebf127b635dcfcebddba31f0e8cc8b1c304a5", "start_char": 0, "end_char": 1621, "text_sha256": "945d1d5166ce6410cd69984d93aebf127b635dcfcebddba31f0e8cc8b1c304a5"} [ino-p8223565] Probing the role of metal ions in the mechanism of inositol monophosphatase by site-directed mutagenesis. (1993). https://pubmed.ncbi.nlm.nih.gov/8223565/ DOI: 10.1111/j.1432-1033.1993.tb18244.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