Component

Magnesium-ADP complex

ADP coordinated to Mg2+, distinct from free ADP.

5 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 2000 experiments interpreted MgADP as a more potent OGDHC activator than free ADP.

    Magnesium-ADP complex → 2-Oxoglutarate dehydrogenase complex source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    Magnesium and thiamine-derived ThDP intersect at mitochondrial carbon metabolism; purified-enzyme responses do not measure whole-body energy supply.
    experimental_model
    Isolated pig-heart enzyme complex plus mitochondrial extracts; extract source not resolved in this curation; nucleotide/phosphate/Mg speciation experiments.
    limitations
    Speciation-based interpretation; later modeling offered independent Mg/ADP effects.
    nutrient_topic
    Magnesium research collection; topical membership is not evidence of a direct dietary effect. · Magnesium
    organism
    Sus scrofa
    plain_language
    The authors assigned enhanced activity to magnesium-bound ADP.
    primary_references
    [rodriguez-2000-ogdh] Modulation of 2-oxoglutarate dehydrogenase complex by inorganic phosphate, Mg(2+), and other effectors (2000). https://pubmed.ncbi.nlm.nih.gov/10864444/ DOI: 10.1006/abbi.2000.1856
    tissue_or_cell_type
    Isolated heart enzyme; additional mitochondrial-extract source not resolved

    Magnesium: cross-nutrient mechanisms and deficiency (2026-09-17) · lines 699–709

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Isolated pig-heart enzyme complex plus mitochondrial extracts; extract source not resolved in this curation; nucleotide/phosphate/Mg speciation experiments. · source_derived_draft · unverified_draft

    ### mg-ogdh-mgadp-interpretation The 2000 experiments interpreted MgADP as a more potent OGDHC activator than free ADP. Condition category: normal nutrient_topic: Magnesium research collection; topical membership is not evidence of a direct dietary effect. plain_language: The authors assigned enhanced activity to magnesium-bound ADP. organism: Sus scrofa tissue_or_cell_type: Isolated heart enzyme; additional mitochondrial-extract source not resolved experimental_model: Isolated pig-heart enzyme complex plus mitochondrial extracts; extract source not resolved in this curation; nucleotide/phosphate/Mg speciation experiments. limitations: Speciation-based interpretation; later modeling offered independent Mg/ADP effects. cross_nutrient: Magnesium and thiamine-derived ThDP intersect at mitochondrial carbon metabolism; purified-enzyme responses do not measure whole-body energy supply. [rodriguez-2000-ogdh] Modulation of 2-oxoglutarate dehydrogenase complex by inorganic phosphate, Mg(2+), and other effectors (2000). https://pubmed.ncbi.nlm.nih.gov/10864444/ DOI: 10.1006/abbi.2000.1856
    Complete structured claim and evidence

  2. MgADP potentiated cloned Kir6.2/SUR1 current through intact SUR1 nucleotide-binding machinery.

    Magnesium-ADP complex → Kir6.2-SUR1 ATP-sensitive potassium channel source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    MgADP supplies a magnesium-dependent regulatory input to potassium conductance.
    experimental_model
    Xenopus oocyte cloned-channel patches.
    limitations
    Heterologous channel biochemistry, not nutritional magnesium depletion.
    nutrient_topic
    Potassium research collection; topical membership is not evidence of a direct dietary effect. · Potassium
    organism
    Xenopus expression system
    plain_language
    Magnesium-bound ADP helps keep this potassium channel active.
    primary_references
    [gribble-1997-sur1] The essential role of the Walker A motifs of SUR1 in K-ATP channel activation by Mg-ADP and diazoxide (1997). https://pmc.ncbi.nlm.nih.gov/articles/PMC1169713/ DOI: 10.1093/emboj/16.6.1145
    tissue_or_cell_type
    Oocyte membrane

    Potassium: cross-nutrient mechanisms and deficiency (2026-09-17) · lines 810–820

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Xenopus oocyte cloned-channel patches. · source_derived_draft · unverified_draft

    ### k-mgadp-sur1-activation MgADP potentiated cloned Kir6.2/SUR1 current through intact SUR1 nucleotide-binding machinery. Condition category: normal nutrient_topic: Potassium research collection; topical membership is not evidence of a direct dietary effect. plain_language: Magnesium-bound ADP helps keep this potassium channel active. organism: Xenopus expression system tissue_or_cell_type: Oocyte membrane experimental_model: Xenopus oocyte cloned-channel patches. limitations: Heterologous channel biochemistry, not nutritional magnesium depletion. cross_nutrient: MgADP supplies a magnesium-dependent regulatory input to potassium conductance. [gribble-1997-sur1] The essential role of the Walker A motifs of SUR1 in K-ATP channel activation by Mg-ADP and diazoxide (1997). https://pmc.ncbi.nlm.nih.gov/articles/PMC1169713/ DOI: 10.1093/emboj/16.6.1145
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. A 2011 kinetic reanalysis favored independent Mg and ADP effects rather than requiring MgADP as the activating species.

    Mg2+ → 2-Oxoglutarate dehydrogenase complex source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    Magnesium and thiamine-derived ThDP intersect at mitochondrial carbon metabolism; purified-enzyme responses do not measure whole-body energy supply.
    experimental_model
    Primary kinetic modeling and reanalysis of published mammalian OGDHC datasets.
    limitations
    Computational inference, not a new binding measurement; more complex alternatives were not excluded.
    nutrient_topic
    Magnesium research collection; topical membership is not evidence of a direct dietary effect. · Magnesium
    organism
    Mammalian datasets including Sus scrofa
    plain_language
    One model explains activation using two separate regulators.
    primary_references
    [qi-2011-ogdh] Detailed kinetics and regulation of mammalian 2-oxoglutarate dehydrogenase (2011). https://link.springer.com/article/10.1186/1471-2091-12-53 DOI: 10.1186/1471-2091-12-53
    tissue_or_cell_type
    Published isolated-enzyme datasets

    Magnesium: cross-nutrient mechanisms and deficiency (2026-09-17) · lines 723–733

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Primary kinetic modeling and reanalysis of published mammalian OGDHC datasets. · source_derived_draft · unverified_draft

    ### mg-ogdh-independent-adp-model A 2011 kinetic reanalysis favored independent Mg and ADP effects rather than requiring MgADP as the activating species. Condition category: normal nutrient_topic: Magnesium research collection; topical membership is not evidence of a direct dietary effect. plain_language: One model explains activation using two separate regulators. organism: Mammalian datasets including Sus scrofa tissue_or_cell_type: Published isolated-enzyme datasets experimental_model: Primary kinetic modeling and reanalysis of published mammalian OGDHC datasets. limitations: Computational inference, not a new binding measurement; more complex alternatives were not excluded. cross_nutrient: Magnesium and thiamine-derived ThDP intersect at mitochondrial carbon metabolism; purified-enzyme responses do not measure whole-body energy supply. [qi-2011-ogdh] Detailed kinetics and regulation of mammalian 2-oxoglutarate dehydrogenase (2011). https://link.springer.com/article/10.1186/1471-2091-12-53 DOI: 10.1186/1471-2091-12-53
    Complete structured claim and evidence

  2. SUR1 K719A or K1384M substitution impaired MgADP potentiation of cloned KATP currents.

    SUR1 K719A variant → Kir6.2-SUR1 ATP-sensitive potassium channel source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    cross_nutrient
    A machinery defect interrupts magnesium-nucleotide regulation without demonstrating ion deficiency.
    experimental_model
    Mutant versus wild-type Xenopus patches.
    limitations
    Engineered substitutions are not evidence of dietary K or Mg deficiency.
    nutrient_topic
    Potassium research collection; topical membership is not evidence of a direct dietary effect. · Potassium
    organism
    Xenopus expression system
    plain_language
    Damaged nucleotide machinery can disrupt potassium-channel regulation.
    primary_references
    [gribble-1997-sur1] The essential role of the Walker A motifs of SUR1 in K-ATP channel activation by Mg-ADP and diazoxide (1997). https://pmc.ncbi.nlm.nih.gov/articles/PMC1169713/ DOI: 10.1093/emboj/16.6.1145
    tissue_or_cell_type
    Oocyte membrane
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Potassium: cross-nutrient mechanisms and deficiency (2026-09-17) · lines 822–832

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Mutant versus wild-type Xenopus patches. · source_derived_draft · unverified_draft

    ### k-sur1-mutations-mgadp SUR1 K719A or K1384M substitution impaired MgADP potentiation of cloned KATP currents. Condition category: machinery_impairment nutrient_topic: Potassium research collection; topical membership is not evidence of a direct dietary effect. plain_language: Damaged nucleotide machinery can disrupt potassium-channel regulation. organism: Xenopus expression system tissue_or_cell_type: Oocyte membrane experimental_model: Mutant versus wild-type Xenopus patches. limitations: Engineered substitutions are not evidence of dietary K or Mg deficiency. cross_nutrient: A machinery defect interrupts magnesium-nucleotide regulation without demonstrating ion deficiency. [gribble-1997-sur1] The essential role of the Walker A motifs of SUR1 in K-ATP channel activation by Mg-ADP and diazoxide (1997). https://pmc.ncbi.nlm.nih.gov/articles/PMC1169713/ DOI: 10.1093/emboj/16.6.1145
    Complete structured claim and evidence

  3. Human RFK crystallized with MgADP and FMN showed magnesium coordination by an FMN phosphate oxygen and Asn36.

    Mg2+ → Riboflavin kinase / RFK source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    Magnesium supports the chemistry used to activate vitamin B2; no blood-magnesium threshold is established.
    evidence_location
    Abstract; metal-coordination structural analysis
    experimental_model
    Product-bound human RFK crystallography
    exposure
    Co-crystallization with MgADP and FMN.
    limitations
    A metal-bound enzyme structure is not a clinical magnesium-deficiency or supplementation experiment.
    nutrient_topic
    Riboflavin research collection; topical membership is not evidence of a direct dietary effect. · Riboflavin (vitamin B2)
    organism
    Homo sapiens
    plain_language
    Magnesium participates directly in the RFK active site.
    primary_references
    [transport-rfk-2003] Ligand binding-induced conformational changes in riboflavin kinase: structural basis for the ordered mechanism. (2003). https://pubmed.ncbi.nlm.nih.gov/14580199/ DOI: 10.1021/bi035450t
    tissue_or_cell_type
    Purified protein

    Riboflavin: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 306–318

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Product-bound human RFK crystallography · source_derived_draft · unverified_draft

    ### transport-rfk-magnesium-coordination Human RFK crystallized with MgADP and FMN showed magnesium coordination by an FMN phosphate oxygen and Asn36. Condition category: normal nutrient_topic: Riboflavin research collection; topical membership is not evidence of a direct dietary effect. plain_language: Magnesium participates directly in the RFK active site. organism: Homo sapiens tissue_or_cell_type: Purified protein experimental_model: Product-bound human RFK crystallography limitations: A metal-bound enzyme structure is not a clinical magnesium-deficiency or supplementation experiment. exposure: Co-crystallization with MgADP and FMN. cross_nutrient: Magnesium supports the chemistry used to activate vitamin B2; no blood-magnesium threshold is established. evidence_location: Abstract; metal-coordination structural analysis [transport-rfk-2003] Ligand binding-induced conformational changes in riboflavin kinase: structural basis for the ordered mechanism. (2003). https://pubmed.ncbi.nlm.nih.gov/14580199/ DOI: 10.1021/bi035450t
    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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