Component
Cobalt(II) ion
Co2+, used as a replacement divalent ion in biochemical assays.
2 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.
Other things that act on it
Enzymes, hormones, genes, and other components with a recorded effect. These are not nutrients, so they do not count toward the arrows above. Each finding names the chapter that recorded it.
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.
Where it participates (unsigned role)
Reconstituted erythrocyte transketolase activity ranked Co2+ < Mn2+ < Ca2+ < Mg2+ in the tested assay.
Experimental context and source evidence
- cross_nutrient
- Magnesium availability supports vitamin B1 activation or cofactor use in the specified preparation; this does not establish a dietary threshold or universal treatment failure.
- experimental_model
- Human erythrocyte transketolase; sulfur-35 ThDP binding and divalent-ion reconstitution.
- limitations
- Replacement in vitro does not establish physiological substitution during Mg deficiency.
- nutrient_topic
- Magnesium research collection; topical membership is not evidence of a direct dietary effect. · Magnesium
- organism
- Homo sapiens
- plain_language
- Several divalent metals supported this B1-dependent enzyme; magnesium worked best here.
- primary_references
- [jung-1988-tkt] Studies on the nature of thiamine pyrophosphate binding and dependency on divalent cations of transketolase from human erythrocytes (1988). https://pubmed.ncbi.nlm.nih.gov/3248678/ DOI: 10.1016/0020-711x(88)90228-5
- tissue_or_cell_type
- Erythrocyte enzyme
Magnesium: cross-nutrient mechanisms and deficiency (2026-09-17) · lines 565–575
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human erythrocyte transketolase; sulfur-35 ThDP binding and divalent-ion reconstitution. · source_derived_draft · unverified_draft
### mg-tkt-other-divalent-cations Reconstituted erythrocyte transketolase activity ranked Co2+ < Mn2+ < Ca2+ < Mg2+ in the tested assay. Condition category: normal nutrient_topic: Magnesium research collection; topical membership is not evidence of a direct dietary effect. plain_language: Several divalent metals supported this B1-dependent enzyme; magnesium worked best here. organism: Homo sapiens tissue_or_cell_type: Erythrocyte enzyme experimental_model: Human erythrocyte transketolase; sulfur-35 ThDP binding and divalent-ion reconstitution. limitations: Replacement in vitro does not establish physiological substitution during Mg deficiency. cross_nutrient: Magnesium availability supports vitamin B1 activation or cofactor use in the specified preparation; this does not establish a dietary threshold or universal treatment failure. [jung-1988-tkt] Studies on the nature of thiamine pyrophosphate binding and dependency on divalent cations of transketolase from human erythrocytes (1988). https://pubmed.ncbi.nlm.nih.gov/3248678/ DOI: 10.1016/0020-711x(88)90228-5
Complete structured claim and evidenceFor reconstituted human ARG1, turnover and catalytic efficiency ranked Mn(II) > Ni(II) ≈ Co(II) ≫ Zn(II).
Experimental context and source evidence
- cross_nutrient
- Zinc and cobalt substitutions were less effective than Mn; in-vitro substitution does not establish nutritional equivalence.
- experimental_model
- Metal-substitution crystallography and kinetics of purified human ARG1
- exposure
- Non-native metal reconstitution or added zinc
- limitations
- Primary experimental scope only; no human dietary threshold, clinical treatment rule, or universal metal substitution is established.
- nutrient_topic
- Manganese research collection; topical membership is not evidence of a direct dietary effect. · Manganese
- organism
- Homo sapiens protein
- plain_language
- Manganese gave the most efficient ARG1 catalysis in this comparison.
- primary_references
- [mn-enz-23061982] Structure and function of non-native metal clusters in human arginase I. (2012). https://pubmed.ncbi.nlm.nih.gov/23061982/ DOI: 10.1021/bi301145n
- tissue_or_cell_type
- Purified enzyme
Manganese: enzyme cofactors, glycosylation, transport and nutrient interactions (2026-09-17) · lines 546–557
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Metal-substitution crystallography and kinetics of purified human ARG1 · source_derived_draft · unverified_draft
### mn-enz-arg1-manganese-optimum For reconstituted human ARG1, turnover and catalytic efficiency ranked Mn(II) > Ni(II) ≈ Co(II) ≫ Zn(II). Condition category: normal nutrient_topic: Manganese research collection; topical membership is not evidence of a direct dietary effect. plain_language: Manganese gave the most efficient ARG1 catalysis in this comparison. organism: Homo sapiens protein tissue_or_cell_type: Purified enzyme experimental_model: Metal-substitution crystallography and kinetics of purified human ARG1 limitations: Primary experimental scope only; no human dietary threshold, clinical treatment rule, or universal metal substitution is established. exposure: Non-native metal reconstitution or added zinc cross_nutrient: Zinc and cobalt substitutions were less effective than Mn; in-vitro substitution does not establish nutritional equivalence. [mn-enz-23061982] Structure and function of non-native metal clusters in human arginase I. (2012). https://pubmed.ncbi.nlm.nih.gov/23061982/ DOI: 10.1021/bi301145n
Complete structured claim and evidence
The events it takes part in
A mechanism often involves more than two components. These are the full events, with every participant and its role.
Situations it appears in
Low-supply and faulty-machinery situations recorded in the chapters where this component plays a part.
In the sources
Preserved passages that mention this component, quoted exactly. Open one to read it in context.
Open hypotheses
Proposed ideas that involve this component. They are labeled as hypotheses and do not change any recorded statement.
This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.