Component

Allium sativum alliin lyase / alliinase

Allium sativum alliin lyase / alliinase. Interpret through the linked study species, preparation, exposure and measured endpoint.

3 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. Alliinase localization to garlic bundle-sheath cells qualifies where precursor-enzyme mixing occurs after tissue damage.

    Allium sativum alliin lyase / alliinase → Alliin / (+S)-S-allyl-L-cysteine sulfoxide source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Publisher abstract read through web tool; anatomical localization, not independent full-section microscopy reanalysis.
    experimental_model
    Garlic-clove anatomical staining; primary publisher abstract.
    interpretation_status
    Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.
    limitations
    Spatial localization, not a causal inhibition or universal intracellular arrangement. Precursor is contextual; no human enzyme is implied.
    plain_language
    Alliinase localization to garlic bundle-sheath cells qualifies where precursor-enzyme mixing occurs after tissue damage.
    primary_references
    Alliin lyase localization in bundle sheaths of the garlic clove (Allium sativum) | 1994 | DOI 10.1002/j.1537-2197.1994.tb15413.x | https://bsapubs.onlinelibrary.wiley.com/doi/abs/10.1002/j.1537-2197.1994.tb15413.x
    source_locator
    Reviewed reference lines 13-13; exact primary location described in quoted passage where extracted.

    Allicin: detailed mechanisms of action (reviewed 5 October 2026) · lines 13–13

    Original AI-assisted review of primary studies and, where relevant, official regulatory records. Access level is retained per claim. Corrections, null results and unresolved questions remain explicit. Not publisher full text or independent replication. · supports · Garlic-clove anatomical staining; primary publisher abstract. · source_derived_draft · unverified_draft

    **Plant anatomy.** Alliinase was strongly localized to garlic-clove bundle-sheath cells, particularly around phloem, with little detected in storage mesophyll away from vascular bundles. Tissue disruption permits precursor–enzyme contact, but a uniform arrangement in every garlic cell is an oversimplification. Intact garlic still contains active metabolism and other constituents. [Ellmore and Feldberg 1994](https://bsapubs.onlinelibrary.wiley.com/doi/abs/10.1002/j.1537-2197.1994.tb15413.x)
    Complete structured claim and evidence

What acts on it

  1. Garlic alliinase is a PLP-dependent plant enzyme; its structural cofactor requirement is not a human B6 supplementation experiment.

    PLP → Allium sativum alliin lyase / alliinase source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary indexed abstract reviewed; full methods, exact concentrations or species-specific attribution remain unextracted unless explicitly stated in the abstract or separately verified publisher text.
    experimental_model
    Purified Allium sativum enzyme; X-ray structural study.
    interpretation_status
    Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.
    limitations
    Interpret only within the recorded preparation, exposure and comparator. The complete source passage retains qualifications; unspecified doses/timing have not been extracted here. No clinical efficacy, nutrient deficiency or unique molecular mediation is inferred.
    plain_language
    Garlic alliinase is a PLP-dependent plant enzyme; its structural cofactor requirement is not a human B6 supplementation experiment.
    primary_references
    The active principle of garlic at atomic resolution. | 2002 | DOI 10.1074/jbc.m208669200 | PMID 12235163 | https://pubmed.ncbi.nlm.nih.gov/12235163/ | https://doi.org/10.1074/jbc.m208669200
    source_locator
    Reviewed reference lines 11-11; exact primary location described in quoted passage where extracted.

    Allicin: detailed mechanisms of action (reviewed 5 October 2026) · lines 11–11

    Original AI-assisted review of primary studies and, where relevant, official regulatory records. Access level is retained per claim. Corrections, null results and unresolved questions remain explicit. Not publisher full text or independent replication. · supports · Purified Allium sativum enzyme; X-ray structural study. · source_derived_draft · unverified_draft

    **Alliinase and vitamin B6.** Garlic alliinase is a plant pyridoxal-5′-phosphate (PLP)-dependent enzyme, not a human enzyme. Structural studies resolved its cofactor-containing active site, an apo form, and a PLP-bound aminoacrylate intermediate. Alliin cleavage produces allylsulfenic acid and an aminoacrylate intermediate; the latter yields pyruvate and ammonia. Two allylsulfenic acid molecules condense to allicin with water loss. This links allicin formation to B6 chemistry in the plant. It does not show that taking B6 increases allicin production in a person. [Kuettner 2002](https://pubmed.ncbi.nlm.nih.gov/12235163/) [Shimon 2007](https://pubmed.ncbi.nlm.nih.gov/17174334/)
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. PLP-dependent garlic alliinase cleaves alliin to the sulfenic-acid precursor; aminoacrylate formation leads to pyruvate and ammonia.

    Alliin / (+S)-S-allyl-L-cysteine sulfoxide → Allylsulfenic acid source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary indexed abstract reviewed; full methods, exact concentrations or species-specific attribution remain unextracted unless explicitly stated in the abstract or separately verified publisher text.
    experimental_model
    Plant enzyme and structural intermediate; biochemical reaction.
    interpretation_status
    Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.
    limitations
    Interpret only within the recorded preparation, exposure and comparator. The complete source passage retains qualifications; unspecified doses/timing have not been extracted here. No clinical efficacy, nutrient deficiency or unique molecular mediation is inferred.
    plain_language
    PLP-dependent garlic alliinase cleaves alliin to the sulfenic-acid precursor; aminoacrylate formation leads to pyruvate and ammonia.
    primary_references
    Two structures of alliinase from Alliium sativum L.: apo form and ternary complex with aminoacrylate reaction intermediate covalently bound to the PLP cofactor. | 2007 | DOI 10.1016/j.jmb.2006.11.041 | PMID 17174334 | https://pubmed.ncbi.nlm.nih.gov/17174334/ | https://doi.org/10.1016/j.jmb.2006.11.041
    source_locator
    Reviewed reference lines 11-11; exact primary location described in quoted passage where extracted.

    Allicin: detailed mechanisms of action (reviewed 5 October 2026) · lines 11–11

    Original AI-assisted review of primary studies and, where relevant, official regulatory records. Access level is retained per claim. Corrections, null results and unresolved questions remain explicit. Not publisher full text or independent replication. · supports · Plant enzyme and structural intermediate; biochemical reaction. · source_derived_draft · unverified_draft

    **Alliinase and vitamin B6.** Garlic alliinase is a plant pyridoxal-5′-phosphate (PLP)-dependent enzyme, not a human enzyme. Structural studies resolved its cofactor-containing active site, an apo form, and a PLP-bound aminoacrylate intermediate. Alliin cleavage produces allylsulfenic acid and an aminoacrylate intermediate; the latter yields pyruvate and ammonia. Two allylsulfenic acid molecules condense to allicin with water loss. This links allicin formation to B6 chemistry in the plant. It does not show that taking B6 increases allicin production in a person. [Kuettner 2002](https://pubmed.ncbi.nlm.nih.gov/12235163/) [Shimon 2007](https://pubmed.ncbi.nlm.nih.gov/17174334/)
    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.