Component

Escherichia coli chorismate pyruvate-lyase / UbiC

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 it acts on

  1. The ubiC mutant produced little ubiquinone without exogenous 4-hydroxybenzoate.

    Escherichia coli chorismate pyruvate-lyase / UbiC → E. coli ubiquinone biosynthesis Recorded from sourceungraded
    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_contrast
    {"intervention": "ubiC-defective strain without external 4-hydroxybenzoate", "comparator": "UbiC-functional or precursor-rescued background", "endpoint": "The ubiC mutant produced little ubiquinone without exogenous 4-hydroxybenzoate.", "effect_direction": "decrease", "combination": "single", "conditions": []} Explicit extracted experimental comparison; source-derived draft.
    experimental_model
    E. coli K12 mutant characterization.
    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
    The ubiC mutant produced little ubiquinone without exogenous 4-hydroxybenzoate.
    primary_references
    Biosynthesis of ubiquinone in Escherichia coli K-12: biochemical and genetic characterization of a mutant unable to convert chorismate into 4-hydroxybenzoate. | 1974 | DOI 10.1128/jb.118.1.41-45.1974 | PMID 4595202 | https://pubmed.ncbi.nlm.nih.gov/4595202/ | https://doi.org/10.1128/jb.118.1.41-45.1974 | https://pmc.ncbi.nlm.nih.gov/articles/PMC246637/
    primary_references
    The role of shikimic acid in the biosynthesis of vitamin K2. | 1966 | DOI 10.1042/bj1000001 | PMID 5337721 | https://pubmed.ncbi.nlm.nih.gov/5337721/ | https://doi.org/10.1042/bj1000001 | https://pmc.ncbi.nlm.nih.gov/articles/PMC1265084/
    source_locator
    Reviewed reference lines 27-27; 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 27–27

    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 K12 mutant characterization. · Recorded from source · Recorded from source

    **The K and Q branches are organism-specific.** Isotope experiments in E. coli traced shikimate carbon into the benzene ring of menaquinone-8 (MK-8), and methionine-derived methyl carbon into that product. This does not establish increased human MK-7, vitamin-K function or an oral shikimate dose response. Separately, an E. coli ubiC mutant failed to convert chorismate to 4-hydroxybenzoate and produced little ubiquinone unless supplied with 4-hydroxybenzoate. UbiC therefore identifies a branch-specific supply bottleneck; bacterial ubiquinone production is not synonymous with human mitochondrial CoQ10 synthesis. [The role of shikimic acid in the biosynthesis of vitamin K2.](https://pubmed.ncbi.nlm.nih.gov/5337721/) [Biosynthesis of ubiquinone in Escherichia coli K-12: biochemical and genetic characterization of a mutant unable to convert chorismate into 4-hydroxybenzoate.](https://pubmed.ncbi.nlm.nih.gov/4595202/)
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. E. coli UbiC converts chorismate toward the 4-hydroxybenzoate precursor of bacterial ubiquinone.

    Chorismate → 4-Hydroxybenzoate Recorded from sourceungraded
    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
    E. coli UbiC converts chorismate toward the 4-hydroxybenzoate precursor of bacterial ubiquinone.
    primary_references
    Biosynthesis of ubiquinone in Escherichia coli K-12: biochemical and genetic characterization of a mutant unable to convert chorismate into 4-hydroxybenzoate. | 1974 | DOI 10.1128/jb.118.1.41-45.1974 | PMID 4595202 | https://pubmed.ncbi.nlm.nih.gov/4595202/ | https://doi.org/10.1128/jb.118.1.41-45.1974 | https://pmc.ncbi.nlm.nih.gov/articles/PMC246637/
    primary_references
    The role of shikimic acid in the biosynthesis of vitamin K2. | 1966 | DOI 10.1042/bj1000001 | PMID 5337721 | https://pubmed.ncbi.nlm.nih.gov/5337721/ | https://doi.org/10.1042/bj1000001 | https://pmc.ncbi.nlm.nih.gov/articles/PMC1265084/
    source_locator
    Reviewed reference lines 27-27; exact primary location described in quoted passage where extracted.

    Shikimic acid: detailed mechanisms of action (reviewed 5 October 2026) · lines 27–27

    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. · Recorded from source · Recorded from source

    **The K and Q branches are organism-specific.** Isotope experiments in E. coli traced shikimate carbon into the benzene ring of menaquinone-8 (MK-8), and methionine-derived methyl carbon into that product. This does not establish increased human MK-7, vitamin-K function or an oral shikimate dose response. Separately, an E. coli ubiC mutant failed to convert chorismate to 4-hydroxybenzoate and produced little ubiquinone unless supplied with 4-hydroxybenzoate. UbiC therefore identifies a branch-specific supply bottleneck; bacterial ubiquinone production is not synonymous with human mitochondrial CoQ10 synthesis. [The role of shikimic acid in the biosynthesis of vitamin K2.](https://pubmed.ncbi.nlm.nih.gov/5337721/) [Biosynthesis of ubiquinone in Escherichia coli K-12: biochemical and genetic characterization of a mutant unable to convert chorismate into 4-hydroxybenzoate.](https://pubmed.ncbi.nlm.nih.gov/4595202/)
    Complete structured claim and evidence

  2. External 4-hydroxybenzoate restored the precursor supply supporting ubiquinone production in ubiC-defective E. coli.

    4-Hydroxybenzoate → E. coli ubiquinone biosynthesis Recorded from sourceungraded
    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_condition
    Same mutant without supplied precursor supplied · 4-Hydroxybenzoate Condition belongs to the full experimental contrast; do not separate a joint intervention.
    experimental_condition
    Same mutant without supplied precursor defective · Escherichia coli chorismate pyruvate-lyase / UbiC Condition belongs to the full experimental contrast; do not separate a joint intervention.
    experimental_contrast
    {"intervention": "4-Hydroxybenzoate supplied to ubiC mutant", "comparator": "Same mutant without supplied precursor", "endpoint": "External 4-hydroxybenzoate restored the precursor supply supporting ubiquinone production in ubiC-defective E. coli.", "effect_direction": "increase", "combination": "joint", "conditions": [{"entity_slug": "ecoli-ubic", "state": "defective"}, {"entity_slug": "4-hydroxybenzoate", "state": "supplied"}]} Explicit extracted experimental comparison; source-derived draft.
    experimental_model
    E. coli K12 precursor-rescue experiment.
    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
    External 4-hydroxybenzoate restored the precursor supply supporting ubiquinone production in ubiC-defective E. coli.
    primary_references
    Biosynthesis of ubiquinone in Escherichia coli K-12: biochemical and genetic characterization of a mutant unable to convert chorismate into 4-hydroxybenzoate. | 1974 | DOI 10.1128/jb.118.1.41-45.1974 | PMID 4595202 | https://pubmed.ncbi.nlm.nih.gov/4595202/ | https://doi.org/10.1128/jb.118.1.41-45.1974 | https://pmc.ncbi.nlm.nih.gov/articles/PMC246637/
    primary_references
    The role of shikimic acid in the biosynthesis of vitamin K2. | 1966 | DOI 10.1042/bj1000001 | PMID 5337721 | https://pubmed.ncbi.nlm.nih.gov/5337721/ | https://doi.org/10.1042/bj1000001 | https://pmc.ncbi.nlm.nih.gov/articles/PMC1265084/
    source_locator
    Reviewed reference lines 27-27; 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 27–27

    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 K12 precursor-rescue experiment. · Recorded from source · Recorded from source

    **The K and Q branches are organism-specific.** Isotope experiments in E. coli traced shikimate carbon into the benzene ring of menaquinone-8 (MK-8), and methionine-derived methyl carbon into that product. This does not establish increased human MK-7, vitamin-K function or an oral shikimate dose response. Separately, an E. coli ubiC mutant failed to convert chorismate to 4-hydroxybenzoate and produced little ubiquinone unless supplied with 4-hydroxybenzoate. UbiC therefore identifies a branch-specific supply bottleneck; bacterial ubiquinone production is not synonymous with human mitochondrial CoQ10 synthesis. [The role of shikimic acid in the biosynthesis of vitamin K2.](https://pubmed.ncbi.nlm.nih.gov/5337721/) [Biosynthesis of ubiquinone in Escherichia coli K-12: biochemical and genetic characterization of a mutant unable to convert chorismate into 4-hydroxybenzoate.](https://pubmed.ncbi.nlm.nih.gov/4595202/)
    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.