Component

Hercynylcysteine sulfoxide

Context-specific entity; species, compartment and exposure are stated on each claim.

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 acts on it

  1. Biochemical characterization of Mycobacterium smegmatis EgtE supported sulfoxide substrate processing through a sulfenic-acid intermediate toward ergothioneine.

    Mycobacterium smegmatis EgtE → Hercynylcysteine sulfoxide source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    In vitro enzyme characterization.
    limitations
    Intermediate assignment is mechanistically supported; full intracellular flux was not measured.
    nutrient_topic
    Ergothioneine collection; molecular form, preparation, species, exposure and manipulation remain explicit. · L-Ergothioneine
    plain_language
    Sulfur is retained while the cysteine carbon scaffold is removed.
    primary_references
    Mechanistic studies of a novel C-S lyase in ergothioneine biosynthesis: the involvement of a sulfenic acid intermediate. · 2015 · https://pubmed.ncbi.nlm.nih.gov/26149121/ · DOI 10.1038/srep11870

    Ergothioneine: transport, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 208–214

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · In vitro enzyme characterization. · source_derived_draft · unverified_draft

    ## ergothioneine-egte-sulfenic Sulfur is retained while the cysteine carbon scaffold is removed. Biochemical characterization of Mycobacterium smegmatis EgtE supported sulfoxide substrate processing through a sulfenic-acid intermediate toward ergothioneine. Model: In vitro enzyme characterization. Limitations: Intermediate assignment is mechanistically supported; full intracellular flux was not measured. Evidence access: Primary abstract Mechanistic studies of a novel C-S lyase in ergothioneine biosynthesis: the involvement of a sulfenic acid intermediate. · 2015 · https://pubmed.ncbi.nlm.nih.gov/26149121/ · DOI 10.1038/srep11870
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Mycobacterium smegmatis EgtC removes the glutamyl portion of the ergothioneine-pathway sulfur adduct.

    Mycobacterium smegmatis EgtC → Hercynyl-gamma-glutamylcysteine sulfoxide source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Substrate-bound bacterial EgtC structure.
    limitations
    Not human glutathione breakdown; EgtC homologs can have other functions.
    nutrient_topic
    Ergothioneine collection; molecular form, preparation, species, exposure and manipulation remain explicit. · L-Ergothioneine
    plain_language
    A separate enzyme removes the carrier part of the sulfur donor.
    primary_references
    Structure of the Ergothioneine-Biosynthesis Amidohydrolase EgtC. · 2015 · https://pubmed.ncbi.nlm.nih.gov/26079795/ · DOI 10.1002/cbic.201500168

    Ergothioneine: transport, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 192–198

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Substrate-bound bacterial EgtC structure. · source_derived_draft · unverified_draft

    ## ergothioneine-egtc-amide A separate enzyme removes the carrier part of the sulfur donor. Mycobacterium smegmatis EgtC removes the glutamyl portion of the ergothioneine-pathway sulfur adduct. Model: Substrate-bound bacterial EgtC structure. Limitations: Not human glutathione breakdown; EgtC homologs can have other functions. Evidence access: Primary abstract Structure of the Ergothioneine-Biosynthesis Amidohydrolase EgtC. · 2015 · https://pubmed.ncbi.nlm.nih.gov/26079795/ · DOI 10.1002/cbic.201500168
    Complete structured claim and evidence

  2. Purified Mycobacterium smegmatis EgtE catalyzed a PLP-dependent C-S lyase reaction in ergothioneine biosynthesis.

    PLP → Mycobacterium smegmatis EgtE source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Purified bacterial EgtE with thioether/sulfoxide substrates and reductant comparisons.
    limitations
    No demonstrated B6-dependent synthesis in human cells.
    nutrient_topic
    Ergothioneine collection; molecular form, preparation, species, exposure and manipulation remain explicit. · L-Ergothioneine
    plain_language
    The active vitamin B6 cofactor participates in microbial synthesis.
    primary_references
    Mechanistic studies of a novel C-S lyase in ergothioneine biosynthesis: the involvement of a sulfenic acid intermediate. · 2015 · https://pubmed.ncbi.nlm.nih.gov/26149121/ · DOI 10.1038/srep11870

    Ergothioneine: transport, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 200–206

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Purified bacterial EgtE with thioether/sulfoxide substrates and reductant comparisons. · source_derived_draft · unverified_draft

    ## ergothioneine-egte-plp The active vitamin B6 cofactor participates in microbial synthesis. Purified Mycobacterium smegmatis EgtE catalyzed a PLP-dependent C-S lyase reaction in ergothioneine biosynthesis. Model: Purified bacterial EgtE with thioether/sulfoxide substrates and reductant comparisons. Limitations: No demonstrated B6-dependent synthesis in human cells. Evidence access: Primary abstract Mechanistic studies of a novel C-S lyase in ergothioneine biosynthesis: the involvement of a sulfenic acid intermediate. · 2015 · https://pubmed.ncbi.nlm.nih.gov/26149121/ · DOI 10.1038/srep11870
    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