Component

Hercynyl-gamma-glutamylcysteine 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. 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

Where it participates (unsigned role)

  1. Reconstituted Mycobacterium smegmatis biosynthesis required an iron(II)-dependent oxidative sulfurization step.

    Mycobacterium smegmatis EgtB → Hercynine / N-alpha-trimethylhistidine source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Purified bacterial pathway.
    limitations
    Does not mean iron supplements increase human synthesis.
    nutrient_topic
    Ergothioneine collection; molecular form, preparation, species, exposure and manipulation remain explicit. · L-Ergothioneine
    plain_language
    Iron supports a microbial synthesis enzyme.
    primary_references
    In vitro reconstitution of Mycobacterial ergothioneine biosynthesis. · 2010 · https://pubmed.ncbi.nlm.nih.gov/20420449/ · DOI 10.1021/ja101721e

    Ergothioneine: transport, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 176–182

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

    ## ergothioneine-bacterial-iron-step Iron supports a microbial synthesis enzyme. Reconstituted Mycobacterium smegmatis biosynthesis required an iron(II)-dependent oxidative sulfurization step. Model: Purified bacterial pathway. Limitations: Does not mean iron supplements increase human synthesis. Evidence access: Primary abstract In vitro reconstitution of Mycobacterial ergothioneine biosynthesis. · 2010 · https://pubmed.ncbi.nlm.nih.gov/20420449/ · DOI 10.1021/ja101721e
    Complete structured claim and evidence

  2. Mycobacterium thermoresistibile EgtB coupled gamma-glutamylcysteine to hercynine through an oxygen-dependent C-S bond-forming reaction.

    Mycobacterium thermoresistibile EgtB → Gamma-glutamylcysteine source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Crystal structure and enzyme mechanism study.
    limitations
    Non-heme iron coordination supports a proposed radical mechanism, not direct observation of every intermediate.
    nutrient_topic
    Ergothioneine collection; molecular form, preparation, species, exposure and manipulation remain explicit. · L-Ergothioneine
    plain_language
    A cysteine-containing precursor supplies sulfur.
    primary_references
    Structure of the sulfoxide synthase EgtB from the ergothioneine biosynthetic pathway. · 2015 · https://pubmed.ncbi.nlm.nih.gov/25597398/ · DOI 10.1002/anie.201410045

    Ergothioneine: transport, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 184–190

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Crystal structure and enzyme mechanism study. · source_derived_draft · unverified_draft

    ## ergothioneine-egtb-sulfur-donor A cysteine-containing precursor supplies sulfur. Mycobacterium thermoresistibile EgtB coupled gamma-glutamylcysteine to hercynine through an oxygen-dependent C-S bond-forming reaction. Model: Crystal structure and enzyme mechanism study. Limitations: Non-heme iron coordination supports a proposed radical mechanism, not direct observation of every intermediate. Evidence access: Primary abstract Structure of the sulfoxide synthase EgtB from the ergothioneine biosynthetic pathway. · 2015 · https://pubmed.ncbi.nlm.nih.gov/25597398/ · DOI 10.1002/anie.201410045
    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