Component

Escherichia coli quinate/shikimate dehydrogenase / YdiB

1 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.

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. E. coli YdiB accepts NAD/NADP cofactors for quinate/shikimate dehydrogenase activity.

    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
    Primary enzyme specificity/structure comparison.
    interpretation_status
    Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.
    limitations
    Paralog-specific acceptance is not a universal AroE property or a fixed in-vivo reaction direction.
    plain_language
    E. coli YdiB accepts NAD/NADP cofactors for quinate/shikimate dehydrogenase activity.
    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 · Primary enzyme specificity/structure comparison. · Recorded from source · Recorded from source

    **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

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.