Component

Rabbit skeletal-muscle glycogen phosphorylase

Rabbit skeletal-muscle glycogen phosphorylase

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 acts on it

  1. A labeled cofactor-analogue experiment supported direct participation of the PLP phosphate group in glycogen phosphorylase glucosyl transfer.

    PLP → Rabbit skeletal-muscle glycogen phosphorylase source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    PLP-phosphate chemistry supports glycogen metabolism.
    experimental_model
    Rabbit muscle phosphorylase reconstituted with synthetic cofactor analogue
    exposure
    Synthetic pyridoxal-diphospho-glucose analogue reconstitution
    limitations
    Mechanistic analogue evidence; not a demonstration of muscle glycogen failure in human B6 deficiency.
    nutrient_topic
    Vitamin B6 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin B6
    organism
    Oryctolagus cuniculus
    plain_language
    The phosphate portion of active B6 helps this carbohydrate reaction.
    primary_references
    [b6-phosphorylase-1982] Catalytic mechanism of glycogen phosphorylase: pyridoxal(5')diphospho(1)-alpha-D-glucose as a transition-state analogue. (1982). https://pmc.ncbi.nlm.nih.gov/articles/PMC346497/ DOI: 10.1073/pnas.79.12.3716
    tissue_or_cell_type
    Rabbit skeletal-muscle protein

    Vitamin B6: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 860–871

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Rabbit muscle phosphorylase reconstituted with synthetic cofactor analogue · source_derived_draft · unverified_draft

    ### b6-met-rabbit-phosphorylase-phosphate A labeled cofactor-analogue experiment supported direct participation of the PLP phosphate group in glycogen phosphorylase glucosyl transfer. Condition category: normal nutrient_topic: Vitamin B6 research collection; topical membership is not evidence of a direct dietary effect. plain_language: The phosphate portion of active B6 helps this carbohydrate reaction. organism: Oryctolagus cuniculus tissue_or_cell_type: Rabbit skeletal-muscle protein experimental_model: Rabbit muscle phosphorylase reconstituted with synthetic cofactor analogue limitations: Mechanistic analogue evidence; not a demonstration of muscle glycogen failure in human B6 deficiency. cross_nutrient: PLP-phosphate chemistry supports glycogen metabolism. exposure: Synthetic pyridoxal-diphospho-glucose analogue reconstitution [b6-phosphorylase-1982] Catalytic mechanism of glycogen phosphorylase: pyridoxal(5')diphospho(1)-alpha-D-glucose as a transition-state analogue. (1982). https://pmc.ncbi.nlm.nih.gov/articles/PMC346497/ DOI: 10.1073/pnas.79.12.3716
    Complete structured claim and evidence
  2. Rabbit muscle phosphorylase crystallography located PLP buried next to the catalytic glucose-binding site.

    PLP → Rabbit skeletal-muscle glycogen phosphorylase source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    B6-linked glycogen chemistry involves phosphate-containing substrates.
    experimental_model
    Rabbit skeletal muscle glycogen phosphorylase crystallography
    limitations
    Rabbit structure; the spatial relationship alone does not establish every catalytic step.
    nutrient_topic
    Vitamin B6 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin B6
    organism
    Oryctolagus cuniculus
    plain_language
    B6 also participates in glycogen metabolism.
    primary_references
    [b6-phosphorylase-1977] Location of pyridoxal phosphate in glycogen phosphorylase a. (1977). https://pmc.ncbi.nlm.nih.gov/articles/PMC432034/ DOI: 10.1073/pnas.74.11.4757
    tissue_or_cell_type
    Rabbit skeletal-muscle protein

    Vitamin B6: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 848–858

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Rabbit skeletal muscle glycogen phosphorylase crystallography · source_derived_draft · unverified_draft

    ### b6-met-rabbit-phosphorylase-plp Rabbit muscle phosphorylase crystallography located PLP buried next to the catalytic glucose-binding site. Condition category: normal nutrient_topic: Vitamin B6 research collection; topical membership is not evidence of a direct dietary effect. plain_language: B6 also participates in glycogen metabolism. organism: Oryctolagus cuniculus tissue_or_cell_type: Rabbit skeletal-muscle protein experimental_model: Rabbit skeletal muscle glycogen phosphorylase crystallography limitations: Rabbit structure; the spatial relationship alone does not establish every catalytic step. cross_nutrient: B6-linked glycogen chemistry involves phosphate-containing substrates. [b6-phosphorylase-1977] Location of pyridoxal phosphate in glycogen phosphorylase a. (1977). https://pmc.ncbi.nlm.nih.gov/articles/PMC432034/ DOI: 10.1073/pnas.74.11.4757
    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