Component

Zinc-depleted human CA2 prepared by chelation

Recombinant CA2 after pyridine-2,6-dicarboxylic acid treatment; the 2009 preparation retained approximately 10% zinc occupancy.

4 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. 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. 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

What acts on it

  1. 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

Where it participates (unsigned role)

  1. 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.

    Evidence, AI assistance and curation standards