Component

Escherichia coli shikimate dehydrogenase / AroE

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. NADPH provides reducing equivalents for the biosynthetic AroE reaction.

    NADPH → Escherichia coli shikimate dehydrogenase / AroE source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary indexed abstract reviewed; full results, tables and supplements not independently extracted. Primary full text retrieved; relevant methods/results/figures reviewed. Selective extraction, not raw-data reanalysis or exhaustive supplemental extraction.
    experimental_model
    E. coli enzyme cofactor specificity.
    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
    NADPH provides reducing equivalents for the biosynthetic AroE reaction.
    primary_references
    Metabolic engineering of Escherichia coli for shikimate pathway derivative production from glucose-xylose co-substrate. | 2020 | DOI 10.1038/s41467-019-14024-1 | PMID 31937786 | https://pubmed.ncbi.nlm.nih.gov/31937786/ | https://doi.org/10.1038/s41467-019-14024-1 | https://pmc.ncbi.nlm.nih.gov/articles/PMC6959354/
    primary_references
    Structures of shikimate dehydrogenase AroE and its Paralog YdiB. A common structural framework for different activities. | 2003 | DOI 10.1074/jbc.m300794200 | PMID 12637497 | https://pubmed.ncbi.nlm.nih.gov/12637497/ | https://doi.org/10.1074/jbc.m300794200
    source_locator
    Reviewed reference lines 13-13; exact primary location described in quoted passage where extracted.

    Shikimic acid: detailed mechanisms of action (reviewed 5 October 2026) · lines 13–13

    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 enzyme cofactor specificity. · source_derived_draft · unverified_draft

    **NADPH supplies reducing equivalents.** E. coli AroE reduces DHS to shikimate using NADPH, producing NADP+. The reaction is reversible; direction depends on conditions. Primary structural/biochemical work distinguishes NADP-specific AroE from paralog YdiB, which accepts NAD or NADP and has quinate/shikimate dehydrogenase activity. Do not give every homolog identical cofactor specificity or infer that human niacin supplementation necessarily increases gut pathway flux. [Structures of shikimate dehydrogenase AroE and its Paralog YdiB. A common structural framework for different activities.](https://pubmed.ncbi.nlm.nih.gov/12637497/) [Metabolic engineering of Escherichia coli for shikimate pathway derivative production from glucose-xylose co-substrate.](https://pubmed.ncbi.nlm.nih.gov/31937786/)
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. AroE reduces DHS to shikimate with NADPH oxidation to NADP+.

    3-Dehydroshikimate / DHS → Shikimate anion source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary indexed abstract reviewed; full results, tables and supplements not independently extracted. Primary full text retrieved; relevant methods/results/figures reviewed. Selective extraction, not raw-data reanalysis or exhaustive supplemental extraction.
    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
    AroE reduces DHS to shikimate with NADPH oxidation to NADP+.
    primary_references
    Metabolic engineering of Escherichia coli for shikimate pathway derivative production from glucose-xylose co-substrate. | 2020 | DOI 10.1038/s41467-019-14024-1 | PMID 31937786 | https://pubmed.ncbi.nlm.nih.gov/31937786/ | https://doi.org/10.1038/s41467-019-14024-1 | https://pmc.ncbi.nlm.nih.gov/articles/PMC6959354/
    primary_references
    Structures of shikimate dehydrogenase AroE and its Paralog YdiB. A common structural framework for different activities. | 2003 | DOI 10.1074/jbc.m300794200 | PMID 12637497 | https://pubmed.ncbi.nlm.nih.gov/12637497/ | https://doi.org/10.1074/jbc.m300794200
    source_locator
    Reviewed reference lines 13-13; exact primary location described in quoted passage where extracted.

    Shikimic acid: detailed mechanisms of action (reviewed 5 October 2026) · lines 13–13

    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

    **NADPH supplies reducing equivalents.** E. coli AroE reduces DHS to shikimate using NADPH, producing NADP+. The reaction is reversible; direction depends on conditions. Primary structural/biochemical work distinguishes NADP-specific AroE from paralog YdiB, which accepts NAD or NADP and has quinate/shikimate dehydrogenase activity. Do not give every homolog identical cofactor specificity or infer that human niacin supplementation necessarily increases gut pathway flux. [Structures of shikimate dehydrogenase AroE and its Paralog YdiB. A common structural framework for different activities.](https://pubmed.ncbi.nlm.nih.gov/12637497/) [Metabolic engineering of Escherichia coli for shikimate pathway derivative production from glucose-xylose co-substrate.](https://pubmed.ncbi.nlm.nih.gov/31937786/)
    Complete structured claim and evidence

  2. The studied E. coli AroE system supported NADP+-dependent DHS oxidation toward gallic acid.

    3-Dehydroshikimate / DHS → Gallic acid source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text retrieved; relevant methods/results/figures reviewed. Selective extraction, not raw-data reanalysis or exhaustive supplemental extraction.
    experimental_model
    Purified enzyme oxidative branch with subsequent spontaneous aromatization proposed in the paper, distinct from NADPH-driven DHS reduction.
    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 studied E. coli AroE system supported NADP+-dependent DHS oxidation toward gallic acid.
    primary_references
    Mechanism of gallic acid biosynthesis in bacteria (Escherichia coli) and walnut (Juglans regia). | 2011 | DOI 10.1007/s11103-011-9739-3 | PMID 21279669 | https://pubmed.ncbi.nlm.nih.gov/21279669/ | https://doi.org/10.1007/s11103-011-9739-3 | https://pmc.ncbi.nlm.nih.gov/articles/PMC3057006/
    source_locator
    Reviewed reference lines 87-87; exact primary location described in quoted passage where extracted.

    Shikimic acid: detailed mechanisms of action (reviewed 5 October 2026) · lines 87–87

    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 enzyme oxidative branch with subsequent spontaneous aromatization proposed in the paper, distinct from NADPH-driven DHS reduction. · source_derived_draft · unverified_draft

    **A plant oxidative branch is not a human metabolic pathway.** Walnut shikimate-dehydrogenase work and E. coli AroE assays support oxidation of DHS toward gallic acid with NADP+ in the studied enzyme systems; expression of walnut JrSDH in tobacco increased gallic-acid accumulation. This branch shows why substrate and redox context matter for enzyme function. It is not evidence that oral shikimic acid is converted into gallic acid by a human shikimate pathway. [Mechanism of gallic acid biosynthesis in bacteria (Escherichia coli) and walnut (Juglans regia).](https://pubmed.ncbi.nlm.nih.gov/21279669/)
    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.