Component

Erwinia chrysanthemi shikimate kinase

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 acts on it

  1. The studied Erwinia shikimate kinase requires magnesium for its ATP-dependent reaction.

    Mg2+ → Erwinia chrysanthemi shikimate kinase source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full-text HTML and indexed abstract reviewed for the stated results; archived locally. Primary publisher article introductory text reviewed; precise affinity estimates are contextual, not newly remeasured.
    experimental_model
    Purified Erwinia chrysanthemi enzyme and Mg–ADP structure.
    interpretation_status
    Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.
    limitations
    No human magnesium dose threshold or E. coli-specific quantitative affinity inferred.
    plain_language
    The studied Erwinia shikimate kinase requires magnesium for its ATP-dependent reaction.
    primary_references
    Biochemical and X-ray crystallographic studies on shikimate kinase: the important structural role of the P-loop lysine. | 2001 | DOI 10.1110/ps.52501 | PMID 11369852 | https://pubmed.ncbi.nlm.nih.gov/11369852/ | https://doi.org/10.1110/ps.52501 | https://pmc.ncbi.nlm.nih.gov/articles/PMC2374015/
    primary_references
    Crystal structure of the Escherichia coli shikimate kinase I (AroK) that confers sensitivity to mecillinam. | 2002 | DOI 10.1002/prot.10099 | PMID 12001235 | https://pubmed.ncbi.nlm.nih.gov/12001235/ | https://doi.org/10.1002/prot.10099
    source_locator
    Reviewed reference lines 15-15; exact primary location described in quoted passage where extracted.

    Shikimic acid: detailed mechanisms of action (reviewed 5 October 2026) · lines 15–15

    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 Erwinia chrysanthemi enzyme and Mg–ADP structure. · source_derived_draft · unverified_draft

    **ATP and magnesium at shikimate kinase.** Shikimate kinase transfers a phosphoryl group from ATP to shikimate, yielding shikimate-3-phosphate and ADP. The Erwinia chrysanthemi enzyme study identifies magnesium dependence and a Mg–ADP structural complex; this is a microbial enzyme requirement, not a demonstrated human magnesium-deficiency phenotype. E. coli has AroK and AroL kinase isoenzymes with different substrate affinities. The AroK structural paper discusses approximate shikimate Km values of 20 mM versus 0.2 mM for the two systems; these are organism/assay properties, not plasma targets. Loss of both kinases produces aromatic-amino-acid auxotrophy; environmental nutrient rescue and isoenzyme compensation matter. [Biochemical and X-ray crystallographic studies on shikimate kinase: the important structural role of the P-loop lysine.](https://pubmed.ncbi.nlm.nih.gov/11369852/) [Crystal structure of the Escherichia coli shikimate kinase I (AroK) that confers sensitivity to mecillinam.](https://pubmed.ncbi.nlm.nih.gov/12001235/)
    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.