Component

Escherichia coli chorismate synthase / AroC

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. An oxidized-FMN/EPSP/enzyme complex formed without productive chorismate-synthase turnover.

    Flavin mononucleotide → Escherichia coli chorismate synthase / AroC source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary indexed abstract reviewed; full results, tables and supplements not independently extracted.
    experimental_model
    E. coli ternary-complex experiment.
    interpretation_status
    Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.
    limitations
    Null denotes no productive turnover in the oxidized complex, not equal activity versus reduced FMN; binding and catalysis are distinct.
    plain_language
    An oxidized-FMN/EPSP/enzyme complex formed without productive chorismate-synthase turnover.
    primary_references
    Evidence for a major structural change in Escherichia coli chorismate synthase induced by flavin and substrate binding. | 1998 | DOI 10.1042/bj3350319 | PMID 9761730 | https://pubmed.ncbi.nlm.nih.gov/9761730/ | https://doi.org/10.1042/bj3350319 | https://pmc.ncbi.nlm.nih.gov/articles/PMC1219785/
    primary_references
    Mechanism of chorismate synthase. Role of the two invariant histidine residues in the active site. | 2004 | DOI 10.1074/jbc.m312471200 | PMID 14668332 | https://pubmed.ncbi.nlm.nih.gov/14668332/ | https://doi.org/10.1074/jbc.m312471200
    source_locator
    Reviewed reference lines 21-21; exact primary location described in quoted passage where extracted.
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Shikimic acid: detailed mechanisms of action (reviewed 5 October 2026) · lines 21–21

    Original AI-assisted review of primary studies and, where relevant, official regulatory records. Access level is retained per claim. Corrections, null results and unresolved questions remain explicit. Not publisher full text or independent replication. · supports · E. coli ternary-complex experiment. · source_derived_draft · unverified_draft

    **Chorismate synthase needs reduced FMN.** E. coli AroC converts EPSP to chorismate with phosphate elimination. Reduced FMN is required although the overall substrate conversion is not a net redox reaction; flavin is a catalytic cofactor rather than a stoichiometrically consumed vitamin. The 1998 study observed a stable oxidized-FMN/EPSP/enzyme complex without productive turnover. Binding, cofactor quantity and cofactor redox state therefore answer different questions. In Neurospora crassa, bifunctional chorismate synthase can use NADPH to reduce its flavin; that reductase capability must not be assigned to every bacterial AroC. [Evidence for a major structural change in Escherichia coli chorismate synthase induced by flavin and substrate binding.](https://pubmed.ncbi.nlm.nih.gov/9761730/) [Mechanism of chorismate synthase. Role of the two invariant histidine residues in the active site.](https://pubmed.ncbi.nlm.nih.gov/14668332/)
    Complete structured claim and evidence

  2. Reduced FMN supports productive E. coli chorismate-synthase catalysis.

    Reduced flavin mononucleotide / FMNH2 → Escherichia coli chorismate synthase / AroC source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary indexed abstract reviewed; full results, tables and supplements not independently extracted.
    experimental_model
    Purified E. coli chorismate synthase.
    interpretation_status
    Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.
    limitations
    Catalytic redox-state requirement; no net stoichiometric consumption of FMN, dietary B2 deficiency or human phenotype inferred.
    plain_language
    Reduced FMN supports productive E. coli chorismate-synthase catalysis.
    primary_references
    Evidence for a major structural change in Escherichia coli chorismate synthase induced by flavin and substrate binding. | 1998 | DOI 10.1042/bj3350319 | PMID 9761730 | https://pubmed.ncbi.nlm.nih.gov/9761730/ | https://doi.org/10.1042/bj3350319 | https://pmc.ncbi.nlm.nih.gov/articles/PMC1219785/
    primary_references
    Mechanism of chorismate synthase. Role of the two invariant histidine residues in the active site. | 2004 | DOI 10.1074/jbc.m312471200 | PMID 14668332 | https://pubmed.ncbi.nlm.nih.gov/14668332/ | https://doi.org/10.1074/jbc.m312471200
    source_locator
    Reviewed reference lines 21-21; exact primary location described in quoted passage where extracted.

    Shikimic acid: detailed mechanisms of action (reviewed 5 October 2026) · lines 21–21

    Original AI-assisted review of primary studies and, where relevant, official regulatory records. Access level is retained per claim. Corrections, null results and unresolved questions remain explicit. Not publisher full text or independent replication. · supports · Purified E. coli chorismate synthase. · source_derived_draft · unverified_draft

    **Chorismate synthase needs reduced FMN.** E. coli AroC converts EPSP to chorismate with phosphate elimination. Reduced FMN is required although the overall substrate conversion is not a net redox reaction; flavin is a catalytic cofactor rather than a stoichiometrically consumed vitamin. The 1998 study observed a stable oxidized-FMN/EPSP/enzyme complex without productive turnover. Binding, cofactor quantity and cofactor redox state therefore answer different questions. In Neurospora crassa, bifunctional chorismate synthase can use NADPH to reduce its flavin; that reductase capability must not be assigned to every bacterial AroC. [Evidence for a major structural change in Escherichia coli chorismate synthase induced by flavin and substrate binding.](https://pubmed.ncbi.nlm.nih.gov/9761730/) [Mechanism of chorismate synthase. Role of the two invariant histidine residues in the active site.](https://pubmed.ncbi.nlm.nih.gov/14668332/)
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. AroC forms chorismate from EPSP with reduced-FMN dependence and phosphate elimination.

    5-Enolpyruvylshikimate 3-phosphate / EPSP → Chorismate source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary indexed abstract reviewed; full results, tables and supplements not independently extracted.
    experimental_model
    Escherichia coli biochemical pathway; source-specific enzyme evidence recorded in the passage.
    interpretation_status
    Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.
    limitations
    Interpret only within the recorded preparation, exposure and comparator. The complete source passage retains qualifications; unspecified doses/timing have not been extracted here. No clinical efficacy, nutrient deficiency or unique molecular mediation is inferred.
    plain_language
    AroC forms chorismate from EPSP with reduced-FMN dependence and phosphate elimination.
    primary_references
    Evidence for a major structural change in Escherichia coli chorismate synthase induced by flavin and substrate binding. | 1998 | DOI 10.1042/bj3350319 | PMID 9761730 | https://pubmed.ncbi.nlm.nih.gov/9761730/ | https://doi.org/10.1042/bj3350319 | https://pmc.ncbi.nlm.nih.gov/articles/PMC1219785/
    primary_references
    Mechanism of chorismate synthase. Role of the two invariant histidine residues in the active site. | 2004 | DOI 10.1074/jbc.m312471200 | PMID 14668332 | https://pubmed.ncbi.nlm.nih.gov/14668332/ | https://doi.org/10.1074/jbc.m312471200
    source_locator
    Reviewed reference lines 21-21; exact primary location described in quoted passage where extracted.

    Shikimic acid: detailed mechanisms of action (reviewed 5 October 2026) · lines 21–21

    Original AI-assisted review of primary studies and, where relevant, official regulatory records. Access level is retained per claim. Corrections, null results and unresolved questions remain explicit. Not publisher full text or independent replication. · supports · Escherichia coli biochemical pathway; source-specific enzyme evidence recorded in the passage. · source_derived_draft · unverified_draft

    **Chorismate synthase needs reduced FMN.** E. coli AroC converts EPSP to chorismate with phosphate elimination. Reduced FMN is required although the overall substrate conversion is not a net redox reaction; flavin is a catalytic cofactor rather than a stoichiometrically consumed vitamin. The 1998 study observed a stable oxidized-FMN/EPSP/enzyme complex without productive turnover. Binding, cofactor quantity and cofactor redox state therefore answer different questions. In Neurospora crassa, bifunctional chorismate synthase can use NADPH to reduce its flavin; that reductase capability must not be assigned to every bacterial AroC. [Evidence for a major structural change in Escherichia coli chorismate synthase induced by flavin and substrate binding.](https://pubmed.ncbi.nlm.nih.gov/9761730/) [Mechanism of chorismate synthase. Role of the two invariant histidine residues in the active site.](https://pubmed.ncbi.nlm.nih.gov/14668332/)
    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.