Component

Metal-free human SOD2

Human SOD2 apoprotein; metal loading required for catalytic reconstitution.

1 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.

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. At 30 °C, more than half of human SOD2 purified from expressing yeast mitochondria was apoprotein, and that apoprotein could be fully activated by reconstitution.

    Metal-free human SOD2 → Human SOD2 metallation source_derived_draftungraded
    Experimental context and source evidence
    experimental_model
    Human SOD2 expressed in Saccharomyces cerevisiae and purified from yeast mitochondria
    exposure
    Heterologous expression; metallation and reconstitution
    limitations
    Heterologous yeast expression, not endogenous human tissue. The indexed abstract does not specify a reconstitution dose.
    nutrient_topic
    Manganese research collection; topical membership is not evidence of a direct dietary effect. · Manganese
    organism
    Human protein in Saccharomyces cerevisiae
    plain_language
    Making SOD2 protein does not guarantee that it has loaded its metal.
    primary_references
    [mn-enz-22561997] Metallation state of human manganese superoxide dismutase expressed in Saccharomyces cerevisiae. (2012). https://pubmed.ncbi.nlm.nih.gov/22561997/ DOI: 10.1016/j.abb.2012.04.016
    tissue_or_cell_type
    Yeast mitochondria

    Manganese: enzyme cofactors, glycosylation, transport and nutrient interactions (2026-09-17) · lines 471–481

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human SOD2 expressed in Saccharomyces cerevisiae and purified from yeast mitochondria · source_derived_draft · unverified_draft

    ### mn-enz-sod2-yeast-apo At 30 °C, more than half of human SOD2 purified from expressing yeast mitochondria was apoprotein, and that apoprotein could be fully activated by reconstitution. Condition category: normal nutrient_topic: Manganese research collection; topical membership is not evidence of a direct dietary effect. plain_language: Making SOD2 protein does not guarantee that it has loaded its metal. organism: Human protein in Saccharomyces cerevisiae tissue_or_cell_type: Yeast mitochondria experimental_model: Human SOD2 expressed in Saccharomyces cerevisiae and purified from yeast mitochondria limitations: Heterologous yeast expression, not endogenous human tissue. The indexed abstract does not specify a reconstitution dose. exposure: Heterologous expression; metallation and reconstitution [mn-enz-22561997] Metallation state of human manganese superoxide dismutase expressed in Saccharomyces cerevisiae. (2012). https://pubmed.ncbi.nlm.nih.gov/22561997/ DOI: 10.1016/j.abb.2012.04.016
    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