Component

The profile of prostaglandin G2 and monohydroxy acid products of cyclooxygenase

The profile of prostaglandin G2 and monohydroxy acid products of cyclooxygenase. Species, exposure and limitations are retained in each linked claim.

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. Native ovine cyclooxygenase-1 produced primarily prostaglandin G2 along with 11R-, 15S- and 15R-hydroxyeicosatetraenoic acids with different Km values for each product, establishing that arachidonate can assume at least three catalytically productive arrangements within the site, and half-maximal inhibitory concentrations for the competitive inhibitor ibuprofen were the same for every product of a given enzyme form, 175 micromolar for the native enzyme and 15 micromolar for the V349L mutant, most simply rationalised by a model in which arachidonate forms its various arrangements only after entering the cyclooxygenase active site.

    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/ibuprofen-research/10722687.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "8e9ebedd8a4d791246c951376fa2f6f07a5ca8af828bafd15836bec26c090348", "start_char": 0, "end_char": 2063, "text_sha256": "8e9ebedd8a4d791246c951376fa2f6f07a5ca8af828bafd15836bec26c090348"}
    experimental_model
    Product analysis and kinetics for solubilised, membrane-associated and active-site-mutant ovine cyclooxygenase-1
    exposure
    Arachidonate product profiling with ibuprofen as a competitive inhibitor
    limitations
    The identical inhibitory concentration across three different products is the informative result. The concentrations are high and the enzyme is ovine.
    nutrient_topic
    Ibuprofen research collection; topical membership is not evidence of a direct clinical effect, and the racemate is recorded separately from each of its two enantiomers. · Ibuprofen
    organism
    Sheep enzyme
    plain_language
    The drug blocks the door rather than any one position inside, which is why it stops every product equally.
    primary_references
    [ibu-p10722687] Different catalytically competent arrangements of arachidonic acid within the cyclooxygenase active site of prostaglandin endoperoxide H synthase-1 lead to the formation of different oxygenated products. (2000). https://pubmed.ncbi.nlm.nih.gov/10722687/ DOI: 10.1074/jbc.275.12.8501
    tissue_or_cell_type
    Cyclooxygenase-1

    Ibuprofen: the enantiomer that works, the one that was called inactive, the one-way chemistry that turns one into the other, and the targets that are not cyclooxygenase (2026-09-22) · lines 305–316

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Product analysis and kinetics for solubilised, membrane-associated and active-site-mutant ovine cyclooxygenase-1 · source_derived_draft · unverified_draft

    ### ibu-blocks-entry-not-orientation Native ovine cyclooxygenase-1 produced primarily prostaglandin G2 along with 11R-, 15S- and 15R-hydroxyeicosatetraenoic acids with different Km values for each product, establishing that arachidonate can assume at least three catalytically productive arrangements within the site, and half-maximal inhibitory concentrations for the competitive inhibitor ibuprofen were the same for every product of a given enzyme form, 175 micromolar for the native enzyme and 15 micromolar for the V349L mutant, most simply rationalised by a model in which arachidonate forms its various arrangements only after entering the cyclooxygenase active site. Condition category: normal nutrient_topic: Ibuprofen research collection; topical membership is not evidence of a direct clinical effect, and the racemate is recorded separately from each of its two enantiomers. plain_language: The drug blocks the door rather than any one position inside, which is why it stops every product equally. organism: Sheep enzyme tissue_or_cell_type: Cyclooxygenase-1 experimental_model: Product analysis and kinetics for solubilised, membrane-associated and active-site-mutant ovine cyclooxygenase-1 limitations: The identical inhibitory concentration across three different products is the informative result. The concentrations are high and the enzyme is ovine. exposure: Arachidonate product profiling with ibuprofen as a competitive inhibitor evidence_span: {"source_cache": "artifacts/ibuprofen-research/10722687.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "8e9ebedd8a4d791246c951376fa2f6f07a5ca8af828bafd15836bec26c090348", "start_char": 0, "end_char": 2063, "text_sha256": "8e9ebedd8a4d791246c951376fa2f6f07a5ca8af828bafd15836bec26c090348"} [ibu-p10722687] Different catalytically competent arrangements of arachidonic acid within the cyclooxygenase active site of prostaglandin endoperoxide H synthase-1 lead to the formation of different oxygenated products. (2000). https://pubmed.ncbi.nlm.nih.gov/10722687/ DOI: 10.1074/jbc.275.12.8501
    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.

    Evidence, AI assistance and curation standards