Component

Oseltamivir

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. Human CES1 hydrolyzes oseltamivir to its carboxylate metabolite.

    Oseltamivir → Oseltamivir carboxylate source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary indexed abstract reviewed; full results, tables and supplements not independently extracted.
    experimental_model
    Human liver microsomes and recombinant human CES1; not human conversion of shikimic acid into oseltamivir.
    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
    Human CES1 hydrolyzes oseltamivir to its carboxylate metabolite.
    primary_references
    Anti-influenza prodrug oseltamivir is activated by carboxylesterase human carboxylesterase 1, and the activation is inhibited by antiplatelet agent clopidogrel. | 2006 | DOI 10.1124/jpet.106.111807 | PMID 16966469 | https://pubmed.ncbi.nlm.nih.gov/16966469/ | https://doi.org/10.1124/jpet.106.111807
    source_locator
    Reviewed reference lines 45-45; exact primary location described in quoted passage where extracted.

    Shikimic acid: detailed mechanisms of action (reviewed 5 October 2026) · lines 45–45

    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 · Human liver microsomes and recombinant human CES1; not human conversion of shikimic acid into oseltamivir. · source_derived_draft · unverified_draft

    **The prodrug has its own activation mechanism.** The oseltamivir prodrug is hydrolyzed to oseltamivir carboxylate by human CES1 in the studied human-liver/recombinant systems. CES2, intestinal microsomes and plasma did not show comparable activation in those assays. An in-vitro clopidogrel inhibition observation does not by itself establish loss of antiviral treatment efficacy; subsequent correspondence concerns that translation. These records belong to oseltamivir and CES1, not to a fictitious human shikimate-to-drug reaction. [Anti-influenza prodrug oseltamivir is activated by carboxylesterase human carboxylesterase 1, and the activation is inhibited by antiplatelet agent clopidogrel.](https://pubmed.ncbi.nlm.nih.gov/16966469/)
    Complete structured claim and evidence

What acts on it

  1. The oseltamivir record is a distinct-compound or preparation comparison; its biological effects are not assigned to isolated shikimic acid.

    Shikimic acid → Oseltamivir source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary indexed abstract reviewed; full results, tables and supplements not independently extracted. Bibliographic manufacturing context retained from draft; publisher full text unavailable in this review. No synthesis instructions or newly verified experimental quantities extracted. Review article, manufacturing background only; not affirmative primary experimental support.
    experimental_model
    Editorial identity/scope connection, not experimental causation.
    interpretation_status
    Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.
    limitations
    Unsigned navigation, not a human metabolic conversion or automatic ingredient attribution.
    plain_language
    The oseltamivir record is a distinct-compound or preparation comparison; its biological effects are not assigned to isolated shikimic acid.
    primary_references
    Influenza neuraminidase inhibitors possessing a novel hydrophobic interaction in the enzyme active site: design, synthesis, and structural analysis of carbocyclic sialic acid analogues with potent anti-influenza activity. | 1997 | DOI 10.1021/ja963036t | PMID 16526129 | https://pubmed.ncbi.nlm.nih.gov/16526129/ | https://doi.org/10.1021/ja963036t
    primary_references
    Metabolic engineering for microbial production of shikimic acid. | 2003 | DOI 10.1016/j.ymben.2003.09.001 | PMID 14642355 | https://pubmed.ncbi.nlm.nih.gov/14642355/ | https://doi.org/10.1016/j.ymben.2003.09.001
    primary_references
    Practical total synthesis of the anti-influenza drug GS-4104 | 1998 | DOI 10.1021/jo980330q | https://doi.org/10.1021/jo980330q
    source_locator
    Reviewed reference lines 43-43; exact primary location described in quoted passage where extracted.

    Shikimic acid: detailed mechanisms of action (reviewed 5 October 2026) · lines 43–43

    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 · Editorial identity/scope connection, not experimental causation. · source_derived_draft · unverified_draft

    **A manufacturing precursor is not the finished drug.** Shikimic acid has served as a starting scaffold for chemical manufacture of oseltamivir. Adding the drug’s other functional groups requires chemical synthesis; humans do not turn ingested shikimic acid into oseltamivir. Manufacturing and fermentation routes are industrial context, not antiviral evidence for shikimic acid. The 1997 neuraminidase-inhibitor chemistry paper and the 1998 practical synthesis report concern synthesized drug structures. [Influenza neuraminidase inhibitors possessing a novel hydrophobic interaction in the enzyme active site: design, synthesis, and structural analysis of carbocyclic sialic acid analogues with potent anti-influenza activity.](https://pubmed.ncbi.nlm.nih.gov/16526129/) [Practical total synthesis of the anti-influenza drug GS-4104](https://doi.org/10.1021/jo980330q) [Metabolic engineering for microbial production of shikimic acid.](https://pubmed.ncbi.nlm.nih.gov/14642355/)
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. CES2 did not show comparable oseltamivir activation in the tested assays.

    Human carboxylesterase 2 / CES2 → Oseltamivir carboxylate source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary indexed abstract reviewed; full results, tables and supplements not independently extracted.
    experimental_model
    Recombinant human esterase comparison.
    interpretation_status
    Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.
    limitations
    Assay-specific lack of conversion; not a general lack of CES2 activity.
    plain_language
    CES2 did not show comparable oseltamivir activation in the tested assays.
    primary_references
    Anti-influenza prodrug oseltamivir is activated by carboxylesterase human carboxylesterase 1, and the activation is inhibited by antiplatelet agent clopidogrel. | 2006 | DOI 10.1124/jpet.106.111807 | PMID 16966469 | https://pubmed.ncbi.nlm.nih.gov/16966469/ | https://doi.org/10.1124/jpet.106.111807
    source_locator
    Reviewed reference lines 45-45; exact primary location described in quoted passage where extracted.

    Shikimic acid: detailed mechanisms of action (reviewed 5 October 2026) · lines 45–45

    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 · Recombinant human esterase comparison. · source_derived_draft · unverified_draft

    **The prodrug has its own activation mechanism.** The oseltamivir prodrug is hydrolyzed to oseltamivir carboxylate by human CES1 in the studied human-liver/recombinant systems. CES2, intestinal microsomes and plasma did not show comparable activation in those assays. An in-vitro clopidogrel inhibition observation does not by itself establish loss of antiviral treatment efficacy; subsequent correspondence concerns that translation. These records belong to oseltamivir and CES1, not to a fictitious human shikimate-to-drug reaction. [Anti-influenza prodrug oseltamivir is activated by carboxylesterase human carboxylesterase 1, and the activation is inhibited by antiplatelet agent clopidogrel.](https://pubmed.ncbi.nlm.nih.gov/16966469/)
    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.