Component
Mycobacterium smegmatis EgtE
Context-specific entity; species, compartment and exposure are stated on each 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.
Other things that act on it
Enzymes, hormones, genes, and other components with a recorded effect. These are not nutrients, so they do not count toward the arrows above. Each finding names the chapter that recorded it.
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.
What it acts on
Biochemical characterization of Mycobacterium smegmatis EgtE supported sulfoxide substrate processing through a sulfenic-acid intermediate toward ergothioneine.
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
What acts on it
Purified Mycobacterium smegmatis EgtE catalyzed a PLP-dependent C-S lyase reaction in ergothioneine biosynthesis.
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
The events it takes part in
A mechanism often involves more than two components. These are the full events, with every participant and its role.
Situations it appears in
Low-supply and faulty-machinery situations recorded in the chapters where this component plays a part.
In the sources
Preserved passages that mention this component, quoted exactly. Open one to read it in context.
Open hypotheses
Proposed ideas that involve this component. They are labeled as hypotheses and do not change any recorded statement.
This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.