Component

Riboflavin kinase / RFK

Human enzyme phosphorylating riboflavin to FMN.

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.

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. Human RFK phosphorylates riboflavin to FMN using ATP, yielding ADP; this precedes FLAD1-mediated FAD synthesis.

    Riboflavin kinase / RFK → Riboflavin (vitamin B2) source_derived_draftungraded
    Experimental context and source evidence
    evidence_location
    Abstract and product-bound structure
    experimental_model
    Human RFK structural and catalytic mechanism study
    exposure
    Purified RFK with flavin and adenine nucleotide ligands.
    limitations
    Reaction chemistry does not imply RFK controls every tissue flavin pool to the same extent.
    nutrient_topic
    Riboflavin research collection; topical membership is not evidence of a direct dietary effect. · Riboflavin (vitamin B2)
    organism
    Homo sapiens
    plain_language
    RFK performs the first activation step from riboflavin to FMN.
    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 293–304

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human RFK structural and catalytic mechanism study · source_derived_draft · unverified_draft

    ### transport-rfk-phosphorylation Human RFK phosphorylates riboflavin to FMN using ATP, yielding ADP; this precedes FLAD1-mediated FAD synthesis. Condition category: normal nutrient_topic: Riboflavin research collection; topical membership is not evidence of a direct dietary effect. plain_language: RFK performs the first activation step from riboflavin to FMN. organism: Homo sapiens tissue_or_cell_type: Purified protein experimental_model: Human RFK structural and catalytic mechanism study limitations: Reaction chemistry does not imply RFK controls every tissue flavin pool to the same extent. exposure: Purified RFK with flavin and adenine nucleotide ligands. evidence_location: Abstract and product-bound structure [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

What acts on it

  1. 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.

    Evidence, AI assistance and curation standards