Component

Mustard myrosinase, study-resolved enzyme

Mustard myrosinase, study-resolved enzyme. Species, exposure and limitations are retained in each linked claim.

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. Ascorbate accelerated hydrolysis of the glycosyl-enzyme intermediate and occupied a position supporting its role as the catalytic base.

    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/sulforaphane-research/10978344.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "ed373ac9a91fa7b03d25c21c32adaf57dd2f0f9b65e1f99e9da49aab4c22b0aa", "start_char": 0, "end_char": 1511, "text_sha256": "ed373ac9a91fa7b03d25c21c32adaf57dd2f0f9b65e1f99e9da49aab4c22b0aa"}
    experimental_model
    High-resolution crystallography and reactivation kinetics
    exposure
    Ascorbate with substrate analogues and a trapped glycosyl-enzyme intermediate
    limitations
    Plant enzyme chemistry; does not show that vitamin C pills increase systemic sulforaphane in people.
    nutrient_topic
    Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
    organism
    Mustard plant myrosinase
    plain_language
    Vitamin C can help the plant enzyme carry out its reaction.
    primary_references
    [sulforaphane-p10978344] High resolution X-ray crystallography shows that ascorbate is a cofactor for myrosinase and substitutes for the function of the catalytic base. (2000). https://pubmed.ncbi.nlm.nih.gov/10978344/ DOI: 10.1074/jbc.m006796200
    tissue_or_cell_type
    Enzyme active site

    Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 190–201

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · High-resolution crystallography and reactivation kinetics · source_derived_draft · unverified_draft

    ### sulforaphane-ascorbate-myrosinase Ascorbate accelerated hydrolysis of the glycosyl-enzyme intermediate and occupied a position supporting its role as the catalytic base. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: Vitamin C can help the plant enzyme carry out its reaction. organism: Mustard plant myrosinase tissue_or_cell_type: Enzyme active site experimental_model: High-resolution crystallography and reactivation kinetics limitations: Plant enzyme chemistry; does not show that vitamin C pills increase systemic sulforaphane in people. exposure: Ascorbate with substrate analogues and a trapped glycosyl-enzyme intermediate evidence_span: {"source_cache": "artifacts/sulforaphane-research/10978344.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "ed373ac9a91fa7b03d25c21c32adaf57dd2f0f9b65e1f99e9da49aab4c22b0aa", "start_char": 0, "end_char": 1511, "text_sha256": "ed373ac9a91fa7b03d25c21c32adaf57dd2f0f9b65e1f99e9da49aab4c22b0aa"} [sulforaphane-p10978344] High resolution X-ray crystallography shows that ascorbate is a cofactor for myrosinase and substitutes for the function of the catalytic base. (2000). https://pubmed.ncbi.nlm.nih.gov/10978344/ DOI: 10.1074/jbc.m006796200
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Myrosinase increased mean urinary-metabolite-based recovery from 18.6% to 39.8%, and early conversion during the first eight hours from 8.0% to 25.4%.

    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/sulforaphane-research/41692762.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "67e337141c8012ea573d9720d5e4774bfdd1ae098c056b68991752169fbdb32a", "start_char": 0, "end_char": 1248, "text_sha256": "67e337141c8012ea573d9720d5e4774bfdd1ae098c056b68991752169fbdb32a"}
    experimental_model
    Randomized double-blind crossover single-dose study
    exposure
    Broccoli seed glucoraphanin with versus without mustard myrosinase; both arms contained ascorbic acid
    limitations
    Both arms included ascorbic acid, so its independent benefit cannot be inferred; conversion biomarker is not clinical efficacy.
    nutrient_topic
    Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
    organism
    Human, 16 adults, nine women and seven men
    plain_language
    A recent controlled product comparison confirms the importance of enzyme activity.
    primary_references
    [sulforaphane-p41692762] Exogenous myrosinase from mustard seed increases bioavailability of sulforaphane from a glucoraphanin-rich broccoli seed extract in a randomized clinical study. (2026). https://pubmed.ncbi.nlm.nih.gov/41692762/ DOI: 10.1038/s41598-026-39389-4
    tissue_or_cell_type
    Urinary metabolites and fecal microbial genes

    Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 996–1007

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Randomized double-blind crossover single-dose study · source_derived_draft · unverified_draft

    ### sulforaphane-mustard-seed-trial Myrosinase increased mean urinary-metabolite-based recovery from 18.6% to 39.8%, and early conversion during the first eight hours from 8.0% to 25.4%. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: A recent controlled product comparison confirms the importance of enzyme activity. organism: Human, 16 adults, nine women and seven men tissue_or_cell_type: Urinary metabolites and fecal microbial genes experimental_model: Randomized double-blind crossover single-dose study limitations: Both arms included ascorbic acid, so its independent benefit cannot be inferred; conversion biomarker is not clinical efficacy. exposure: Broccoli seed glucoraphanin with versus without mustard myrosinase; both arms contained ascorbic acid evidence_span: {"source_cache": "artifacts/sulforaphane-research/41692762.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "67e337141c8012ea573d9720d5e4774bfdd1ae098c056b68991752169fbdb32a", "start_char": 0, "end_char": 1248, "text_sha256": "67e337141c8012ea573d9720d5e4774bfdd1ae098c056b68991752169fbdb32a"} [sulforaphane-p41692762] Exogenous myrosinase from mustard seed increases bioavailability of sulforaphane from a glucoraphanin-rich broccoli seed extract in a randomized clinical study. (2026). https://pubmed.ncbi.nlm.nih.gov/41692762/ DOI: 10.1038/s41598-026-39389-4
    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