Component

Human carbonic anhydrase II / CA2

Human cytosolic carbonic anhydrase II, distinct from secreted CA6.

6 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. The leaf oil inhibited human carbonic anhydrase II in vitro, with reported IC50 243.24 micrograms/mL.

    Ceylon leaf oil sample characterized in the 2023 enzyme study → Human carbonic anhydrase II / CA2 source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/ceylon-research/36676085.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "c71e19c572310e80b103949f460ac437e9a564daae423e1de3f17964f2c92291", "start_char": 0, "end_char": 1755, "text_sha256": "c71e19c572310e80b103949f460ac437e9a564daae423e1de3f17964f2c92291"}
    experimental_model
    Composition, chemical redox and cell-free enzyme assays
    exposure
    One leaf oil sample; concentration-response assays in micrograms/mL
    limitations
    This leaf sample is not representative of all leaf oils. Chemical reduction is not mineral absorption; enzyme inhibition is not disease treatment.
    nutrient_topic
    Ceylon cinnamon research collection; topical membership is not evidence of a direct dietary effect. · Ceylon cinnamon / Cinnamomum verum bark preparations
    organism
    C. zeylanicum leaf sample; human CA II and other assay preparations
    plain_language
    The oil slowed a human enzyme in a test tube; clinical effects were not tested.
    primary_references
    [ceylon-p36676085] Comprehensive Metabolite Profiling of Cinnamon (Cinnamomum zeylanicum) Leaf Oil Using LC-HR/MS, GC/MS, and GC-FID: Determination of Antiglaucoma, Antioxidant, Anticholinergic, and Antidiabetic Profiles. (2023). https://pubmed.ncbi.nlm.nih.gov/36676085/ DOI: 10.3390/life13010136
    tissue_or_cell_type
    Leaf essential oil and purified-enzyme assays

    Ceylon cinnamon: metabolism, signaling and nutrient connections (2026-09-17) · lines 129–140

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Composition, chemical redox and cell-free enzyme assays · source_derived_draft · unverified_draft

    ### ceylon-leaf-ca2 The leaf oil inhibited human carbonic anhydrase II in vitro, with reported IC50 243.24 micrograms/mL. Condition category: normal nutrient_topic: Ceylon cinnamon research collection; topical membership is not evidence of a direct dietary effect. plain_language: The oil slowed a human enzyme in a test tube; clinical effects were not tested. organism: C. zeylanicum leaf sample; human CA II and other assay preparations tissue_or_cell_type: Leaf essential oil and purified-enzyme assays experimental_model: Composition, chemical redox and cell-free enzyme assays limitations: This leaf sample is not representative of all leaf oils. Chemical reduction is not mineral absorption; enzyme inhibition is not disease treatment. exposure: One leaf oil sample; concentration-response assays in micrograms/mL evidence_span: {"source_cache": "artifacts/ceylon-research/36676085.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "c71e19c572310e80b103949f460ac437e9a564daae423e1de3f17964f2c92291", "start_char": 0, "end_char": 1755, "text_sha256": "c71e19c572310e80b103949f460ac437e9a564daae423e1de3f17964f2c92291"} [ceylon-p36676085] Comprehensive Metabolite Profiling of Cinnamon (Cinnamomum zeylanicum) Leaf Oil Using LC-HR/MS, GC/MS, and GC-FID: Determination of Antiglaucoma, Antioxidant, Anticholinergic, and Antidiabetic Profiles. (2023). https://pubmed.ncbi.nlm.nih.gov/36676085/ DOI: 10.3390/life13010136
    Complete structured claim and evidence

  2. X-ray absorption analysis of human CA2 supported a zinc site with three histidine nitrogen ligands and most likely one water/hydroxide oxygen ligand in both isolated and reconstituted enzyme.

    Zinc(II) ion → Human carbonic anhydrase II / CA2 source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    false
    experimental_model
    Purified recombinant human CA2; metal reconstitution, ITC and X-ray absorption spectroscopy
    exposure
    Zn K-edge XANES and EXAFS on isolated and zinc-reconstituted recombinant CA2.
    limitations
    Coordination assignment is spectroscopic; the oxygen ligand is most likely solvent-derived, not an independently measured dietary effect.
    nutrient_topic
    Zinc research collection; topical membership is not evidence of a direct dietary effect. · Zinc
    organism
    Homo sapiens
    plain_language
    CA2 holds zinc with three histidines and a water-derived ligand at its active site.
    primary_references
    [zinc-enz-ca2-coordination2012] Revisiting zinc coordination in human carbonic anhydrase II. (2012). https://pubmed.ncbi.nlm.nih.gov/23030313/ DOI: 10.1021/ic301645j
    tissue_or_cell_type
    Purified protein; cell-free assay

    Zinc: transport, enzyme loading, deficiency and nutrient interactions (2026-09-17) · lines 651–662

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified recombinant human CA2; metal reconstitution, ITC and X-ray absorption spectroscopy · source_derived_draft · unverified_draft

    ### zinc-enz-ca2-coordination X-ray absorption analysis of human CA2 supported a zinc site with three histidine nitrogen ligands and most likely one water/hydroxide oxygen ligand in both isolated and reconstituted enzyme. Condition category: normal nutrient_topic: Zinc research collection; topical membership is not evidence of a direct dietary effect. plain_language: CA2 holds zinc with three histidines and a water-derived ligand at its active site. organism: Homo sapiens tissue_or_cell_type: Purified protein; cell-free assay experimental_model: Purified recombinant human CA2; metal reconstitution, ITC and X-ray absorption spectroscopy limitations: Coordination assignment is spectroscopic; the oxygen ligand is most likely solvent-derived, not an independently measured dietary effect. exposure: Zn K-edge XANES and EXAFS on isolated and zinc-reconstituted recombinant CA2. cross_nutrient: false [zinc-enz-ca2-coordination2012] Revisiting zinc coordination in human carbonic anhydrase II. (2012). https://pubmed.ncbi.nlm.nih.gov/23030313/ DOI: 10.1021/ic301645j
    Complete structured claim and evidence

  3. Chelating zinc from recombinant human CA2 reduced catalytic activity; the apo preparation retained about 10% residual zinc.

    Zinc-depleted human CA2 prepared by chelation → Human carbonic anhydrase II / CA2 source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    false
    experimental_model
    Purified recombinant human CA2 expressed in E. coli; chelation, crystallography, DSC and H/D exchange
    exposure
    100 mM pyridine-2,6-dicarboxylic acid, 25 mM MOPS pH 7.0, 20°C for 8 h; chelator removed by buffer exchange.
    limitations
    Purified recombinant protein; chelation is not dietary deficiency. Approximately 10% zinc remained in the nominal apo preparation.
    nutrient_topic
    Zinc research collection; topical membership is not evidence of a direct dietary effect. · Zinc
    organism
    Homo sapiens
    plain_language
    Removing the bound zinc largely disables CA2, even though the protein is still present.
    primary_references
    [zinc-enz-ca2-apo2009] Apo-human carbonic anhydrase II revisited: implications of the loss of a metal in protein structure, stability, and solvent network. (2009). https://pubmed.ncbi.nlm.nih.gov/19583303/ DOI: 10.1021/bi9007512
    tissue_or_cell_type
    Purified protein; cell-free assay

    Zinc: transport, enzyme loading, deficiency and nutrient interactions (2026-09-17) · lines 599–610

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified recombinant human CA2 expressed in E. coli; chelation, crystallography, DSC and H/D exchange · source_derived_draft · unverified_draft

    ### zinc-enz-ca2-removal Chelating zinc from recombinant human CA2 reduced catalytic activity; the apo preparation retained about 10% residual zinc. Condition category: normal nutrient_topic: Zinc research collection; topical membership is not evidence of a direct dietary effect. plain_language: Removing the bound zinc largely disables CA2, even though the protein is still present. organism: Homo sapiens tissue_or_cell_type: Purified protein; cell-free assay experimental_model: Purified recombinant human CA2 expressed in E. coli; chelation, crystallography, DSC and H/D exchange limitations: Purified recombinant protein; chelation is not dietary deficiency. Approximately 10% zinc remained in the nominal apo preparation. exposure: 100 mM pyridine-2,6-dicarboxylic acid, 25 mM MOPS pH 7.0, 20°C for 8 h; chelator removed by buffer exchange. cross_nutrient: false [zinc-enz-ca2-apo2009] Apo-human carbonic anhydrase II revisited: implications of the loss of a metal in protein structure, stability, and solvent network. (2009). https://pubmed.ncbi.nlm.nih.gov/19583303/ DOI: 10.1021/bi9007512
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. The chelated human CA2 structure retained the overall protein fold relative to zinc-containing CA2.

    Zinc-depleted human CA2 prepared by chelation → Human CA2 overall protein fold source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    false
    experimental_model
    Purified recombinant human CA2 expressed in E. coli; chelation, crystallography, DSC and H/D exchange
    exposure
    Chelated CA2 crystallography at 1.26 Å resolution.
    limitations
    Purified recombinant protein; chelation is not dietary deficiency. Approximately 10% zinc remained in the nominal apo preparation.
    nutrient_topic
    Zinc research collection; topical membership is not evidence of a direct dietary effect. · Zinc
    organism
    Homo sapiens
    plain_language
    An enzyme can lose activity before its entire shape collapses.
    primary_references
    [zinc-enz-ca2-apo2009] Apo-human carbonic anhydrase II revisited: implications of the loss of a metal in protein structure, stability, and solvent network. (2009). https://pubmed.ncbi.nlm.nih.gov/19583303/ DOI: 10.1021/bi9007512
    tissue_or_cell_type
    Purified protein; cell-free assay

    Zinc: transport, enzyme loading, deficiency and nutrient interactions (2026-09-17) · lines 638–649

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified recombinant human CA2 expressed in E. coli; chelation, crystallography, DSC and H/D exchange · source_derived_draft · unverified_draft

    ### zinc-enz-ca2-fold-preserved The chelated human CA2 structure retained the overall protein fold relative to zinc-containing CA2. Condition category: normal nutrient_topic: Zinc research collection; topical membership is not evidence of a direct dietary effect. plain_language: An enzyme can lose activity before its entire shape collapses. organism: Homo sapiens tissue_or_cell_type: Purified protein; cell-free assay experimental_model: Purified recombinant human CA2 expressed in E. coli; chelation, crystallography, DSC and H/D exchange limitations: Purified recombinant protein; chelation is not dietary deficiency. Approximately 10% zinc remained in the nominal apo preparation. exposure: Chelated CA2 crystallography at 1.26 Å resolution. cross_nutrient: false [zinc-enz-ca2-apo2009] Apo-human carbonic anhydrase II revisited: implications of the loss of a metal in protein structure, stability, and solvent network. (2009). https://pubmed.ncbi.nlm.nih.gov/19583303/ DOI: 10.1021/bi9007512
    Complete structured claim and evidence

  2. Adding 1 mM ZnCl2 revived the activity of chelated recombinant human CA2.

    Zinc(II) ion → Zinc-depleted human CA2 prepared by chelation source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    false
    experimental_model
    Purified recombinant human CA2 expressed in E. coli; chelation, crystallography, DSC and H/D exchange
    exposure
    1 mM ZnCl2 added in vitro after chelation and buffer exchange.
    limitations
    Purified recombinant protein; chelation is not dietary deficiency. Approximately 10% zinc remained in the nominal apo preparation. The assay addition is not a supplement dose.
    nutrient_topic
    Zinc research collection; topical membership is not evidence of a direct dietary effect. · Zinc
    organism
    Homo sapiens
    plain_language
    Returning zinc to the depleted enzyme restored activity.
    primary_references
    [zinc-enz-ca2-apo2009] Apo-human carbonic anhydrase II revisited: implications of the loss of a metal in protein structure, stability, and solvent network. (2009). https://pubmed.ncbi.nlm.nih.gov/19583303/ DOI: 10.1021/bi9007512
    tissue_or_cell_type
    Purified protein; cell-free assay

    Zinc: transport, enzyme loading, deficiency and nutrient interactions (2026-09-17) · lines 612–623

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified recombinant human CA2 expressed in E. coli; chelation, crystallography, DSC and H/D exchange · source_derived_draft · unverified_draft

    ### zinc-enz-ca2-reconstitution Adding 1 mM ZnCl2 revived the activity of chelated recombinant human CA2. Condition category: normal nutrient_topic: Zinc research collection; topical membership is not evidence of a direct dietary effect. plain_language: Returning zinc to the depleted enzyme restored activity. organism: Homo sapiens tissue_or_cell_type: Purified protein; cell-free assay experimental_model: Purified recombinant human CA2 expressed in E. coli; chelation, crystallography, DSC and H/D exchange limitations: Purified recombinant protein; chelation is not dietary deficiency. Approximately 10% zinc remained in the nominal apo preparation. The assay addition is not a supplement dose. exposure: 1 mM ZnCl2 added in vitro after chelation and buffer exchange. cross_nutrient: false [zinc-enz-ca2-apo2009] Apo-human carbonic anhydrase II revisited: implications of the loss of a metal in protein structure, stability, and solvent network. (2009). https://pubmed.ncbi.nlm.nih.gov/19583303/ DOI: 10.1021/bi9007512
    Complete structured claim and evidence

  3. Zinc-containing CA2 unfolded at 59±0.5°C versus 51±0.5°C for the chelated preparation in differential scanning calorimetry.

    Zinc(II) ion → Thermal stability of human CA2 source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    false
    experimental_model
    Purified recombinant human CA2 expressed in E. coli; chelation, crystallography, DSC and H/D exchange
    exposure
    Purified apo and holo proteins; DSC in 50 mM Tris-HCl pH 7.0.
    limitations
    Purified recombinant protein; chelation is not dietary deficiency. Approximately 10% zinc remained in the nominal apo preparation. Thermal unfolding temperature is not a body-temperature requirement.
    nutrient_topic
    Zinc research collection; topical membership is not evidence of a direct dietary effect. · Zinc
    organism
    Homo sapiens
    plain_language
    Bound zinc also helps CA2 resist thermal unfolding.
    primary_references
    [zinc-enz-ca2-apo2009] Apo-human carbonic anhydrase II revisited: implications of the loss of a metal in protein structure, stability, and solvent network. (2009). https://pubmed.ncbi.nlm.nih.gov/19583303/ DOI: 10.1021/bi9007512
    tissue_or_cell_type
    Purified protein; cell-free assay

    Zinc: transport, enzyme loading, deficiency and nutrient interactions (2026-09-17) · lines 625–636

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified recombinant human CA2 expressed in E. coli; chelation, crystallography, DSC and H/D exchange · source_derived_draft · unverified_draft

    ### zinc-enz-ca2-stability Zinc-containing CA2 unfolded at 59±0.5°C versus 51±0.5°C for the chelated preparation in differential scanning calorimetry. Condition category: normal nutrient_topic: Zinc research collection; topical membership is not evidence of a direct dietary effect. plain_language: Bound zinc also helps CA2 resist thermal unfolding. organism: Homo sapiens tissue_or_cell_type: Purified protein; cell-free assay experimental_model: Purified recombinant human CA2 expressed in E. coli; chelation, crystallography, DSC and H/D exchange limitations: Purified recombinant protein; chelation is not dietary deficiency. Approximately 10% zinc remained in the nominal apo preparation. Thermal unfolding temperature is not a body-temperature requirement. exposure: Purified apo and holo proteins; DSC in 50 mM Tris-HCl pH 7.0. cross_nutrient: false [zinc-enz-ca2-apo2009] Apo-human carbonic anhydrase II revisited: implications of the loss of a metal in protein structure, stability, and solvent network. (2009). https://pubmed.ncbi.nlm.nih.gov/19583303/ DOI: 10.1021/bi9007512
    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.

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