Component

Mycobacterium tuberculosis EgtD / Rv3701c

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.

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. The 2020 reexamination found that Mycobacterium tuberculosis EgtD was not a PknD substrate under its in vitro conditions.

    Mycobacterium tuberculosis protein kinase PknD → Mycobacterium tuberculosis EgtD / Rv3701c source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    In vitro kinase reassessment; active-site accessibility considered structurally.
    limitations
    A negative in vitro result does not alone exclude every cellular condition; matched protocols are needed.
    nutrient_topic
    Ergothioneine collection; molecular form, preparation, species, exposure and manipulation remain explicit. · L-Ergothioneine
    plain_language
    A later study did not reproduce the proposed kinase reaction.
    primary_references
    Reexamination of the Ergothioneine Biosynthetic Methyltransferase EgtD from Mycobacterium tuberculosis as a Protein Kinase Substrate. · 2020 · https://pubmed.ncbi.nlm.nih.gov/32614492/ · DOI 10.1002/cbic.202000232

    Ergothioneine: transport, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 584–590

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · In vitro kinase reassessment; active-site accessibility considered structurally. · source_derived_draft · unverified_draft

    ## ergothioneine-pknd-negative A later study did not reproduce the proposed kinase reaction. The 2020 reexamination found that Mycobacterium tuberculosis EgtD was not a PknD substrate under its in vitro conditions. Model: In vitro kinase reassessment; active-site accessibility considered structurally. Limitations: A negative in vitro result does not alone exclude every cellular condition; matched protocols are needed. Evidence access: Primary abstract Reexamination of the Ergothioneine Biosynthetic Methyltransferase EgtD from Mycobacterium tuberculosis as a Protein Kinase Substrate. · 2020 · https://pubmed.ncbi.nlm.nih.gov/32614492/ · DOI 10.1002/cbic.202000232
    Complete structured claim and evidence

  2. The 2015 Mycobacterium tuberculosis study reported PknD phosphorylation of EgtD at Thr213 in vitro and in a cell-based system.

    Mycobacterium tuberculosis protein kinase PknD → Mycobacterium tuberculosis EgtD / Rv3701c source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Bacterial kinase assays and cell-based phosphorylation evidence.
    limitations
    The kinase-substrate assignment was directly challenged by the 2020 reexamination; not settled regulation.
    nutrient_topic
    Ergothioneine collection; molecular form, preparation, species, exposure and manipulation remain explicit. · L-Ergothioneine
    plain_language
    One study reported a kinase-controlled synthesis switch.
    primary_references
    Regulation of Ergothioneine Biosynthesis and Its Effect on Mycobacterium tuberculosis Growth and Infectivity. · 2015 · https://pubmed.ncbi.nlm.nih.gov/26229105/ · DOI 10.1074/jbc.M115.648642

    Ergothioneine: transport, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 576–582

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Bacterial kinase assays and cell-based phosphorylation evidence. · source_derived_draft · unverified_draft

    ## ergothioneine-pknd-positive One study reported a kinase-controlled synthesis switch. The 2015 Mycobacterium tuberculosis study reported PknD phosphorylation of EgtD at Thr213 in vitro and in a cell-based system. Model: Bacterial kinase assays and cell-based phosphorylation evidence. Limitations: The kinase-substrate assignment was directly challenged by the 2020 reexamination; not settled regulation. Evidence access: Primary abstract Regulation of Ergothioneine Biosynthesis and Its Effect on Mycobacterium tuberculosis Growth and Infectivity. · 2015 · https://pubmed.ncbi.nlm.nih.gov/26229105/ · DOI 10.1074/jbc.M115.648642
    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