Component
Mycobacterium smegmatis EgtD
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
Reconstituted Mycobacterium smegmatis biosynthesis used a methyltransferase to add three methyl groups to the histidine alpha-amino group, producing hercynine.
Experimental context and source evidence
- evidence_access
- Primary abstract
- experimental_model
- Recombinant bacterial enzyme pathway.
- limitations
- Humans have no established equivalent ergothioneine biosynthetic pathway.
- nutrient_topic
- Ergothioneine collection; molecular form, preparation, species, exposure and manipulation remain explicit. · L-Ergothioneine
- plain_language
- Microbes first modify histidine before adding sulfur.
- 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 168–174
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Recombinant bacterial enzyme pathway. · source_derived_draft · unverified_draft
## ergothioneine-histidine-methylation Microbes first modify histidine before adding sulfur. Reconstituted Mycobacterium smegmatis biosynthesis used a methyltransferase to add three methyl groups to the histidine alpha-amino group, producing hercynine. Model: Recombinant bacterial enzyme pathway. Limitations: Humans have no established equivalent ergothioneine biosynthetic pathway. 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
What acts on it
Mycobacterium smegmatis EgtD uses SAM-dependent methyl transfer to convert histidine into hercynine.
Experimental context and source evidence
- evidence_access
- Primary abstract
- experimental_model
- Apo and ligand-bound enzyme structures.
- limitations
- No evidence that human ergothioneine consumption drains SAM; humans lack this established synthesis pathway.
- nutrient_topic
- Ergothioneine collection; molecular form, preparation, species, exposure and manipulation remain explicit. · L-Ergothioneine
- plain_language
- The microbial synthesis branch connects to methyl-donor chemistry.
- primary_references
- Structural insights into the histidine trimethylation activity of EgtD from Mycobacterium smegmatis. · 2014 · https://pubmed.ncbi.nlm.nih.gov/25251321/ · DOI 10.1016/j.bbrc.2014.09.058
Ergothioneine: transport, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 552–558
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Apo and ligand-bound enzyme structures. · source_derived_draft · unverified_draft
## ergothioneine-egtd-sam The microbial synthesis branch connects to methyl-donor chemistry. Mycobacterium smegmatis EgtD uses SAM-dependent methyl transfer to convert histidine into hercynine. Model: Apo and ligand-bound enzyme structures. Limitations: No evidence that human ergothioneine consumption drains SAM; humans lack this established synthesis pathway. Evidence access: Primary abstract Structural insights into the histidine trimethylation activity of EgtD from Mycobacterium smegmatis. · 2014 · https://pubmed.ncbi.nlm.nih.gov/25251321/ · DOI 10.1016/j.bbrc.2014.09.058
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.