Component

Synthesis of 12-oxo-phytodienoic acid and jasmonates in plants

Synthesis of 12-oxo-phytodienoic acid and jasmonates in plants. 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

Where it participates (unsigned role)

  1. Aspirin causes time-dependent inhibition and acetylation of plant allene oxide synthase leading to irreversible inactivation of this cytochrome P450, acetylating three serine residues near the C-terminal region that are highly conserved among allene oxide synthases but not among classical P450s; unlike animal cyclooxygenase, where acetylation of a single serine within the substrate channel causes inactivation, these three serines are not thought to line the putative substrate channel, so inhibition may be by a different mechanism, and aspirin could inhibit other P450s with similar motifs.

    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/aspirin-research/9660772.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "49e5d050a7b1505f537ae535df4e7a51563a72d528973779baf53c963b50c259", "start_char": 0, "end_char": 1662, "text_sha256": "49e5d050a7b1505f537ae535df4e7a51563a72d528973779baf53c963b50c259"}
    experimental_model
    Inhibition and acetylation of plant allene oxide synthase, a cytochrome P450
    exposure
    Aspirin and salicylic acid applied to the plant oxylipin pathway
    limitations
    Recorded because it shows the acetyl group is not specific to cyclooxygenase. The three acetylated serines here are not thought to line the substrate channel, so the mechanism may differ from the one at cyclooxygenase.
    nutrient_topic
    Aspirin research collection; topical membership is not evidence of a direct clinical effect, and aspirin is recorded separately from salicylate, the metabolite it becomes. · Aspirin / acetylsalicylic acid
    organism
    Plant
    plain_language
    Aspirin hands its acetyl group to other enzymes too, including one in plants, and not always at the substrate channel.
    primary_references
    [asa-p9660772] Aspirin inhibition and acetylation of the plant cytochrome P450, allene oxide synthase, resembles that of animal prostaglandin endoperoxide H synthase. (1998). https://pubmed.ncbi.nlm.nih.gov/9660772/ DOI: 10.1074/jbc.273.29.18139
    tissue_or_cell_type
    Allene oxide synthase

    Aspirin: the serine it acetylates, the enzyme that acetylation creates, the dose that separates platelet from vessel wall, and the metabolite that is a different drug (2026-09-22) · lines 195–206

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Inhibition and acetylation of plant allene oxide synthase, a cytochrome P450 · source_derived_draft · unverified_draft

    ### asa-acetylates-other-enzymes Aspirin causes time-dependent inhibition and acetylation of plant allene oxide synthase leading to irreversible inactivation of this cytochrome P450, acetylating three serine residues near the C-terminal region that are highly conserved among allene oxide synthases but not among classical P450s; unlike animal cyclooxygenase, where acetylation of a single serine within the substrate channel causes inactivation, these three serines are not thought to line the putative substrate channel, so inhibition may be by a different mechanism, and aspirin could inhibit other P450s with similar motifs. Condition category: normal nutrient_topic: Aspirin research collection; topical membership is not evidence of a direct clinical effect, and aspirin is recorded separately from salicylate, the metabolite it becomes. plain_language: Aspirin hands its acetyl group to other enzymes too, including one in plants, and not always at the substrate channel. organism: Plant tissue_or_cell_type: Allene oxide synthase experimental_model: Inhibition and acetylation of plant allene oxide synthase, a cytochrome P450 limitations: Recorded because it shows the acetyl group is not specific to cyclooxygenase. The three acetylated serines here are not thought to line the substrate channel, so the mechanism may differ from the one at cyclooxygenase. exposure: Aspirin and salicylic acid applied to the plant oxylipin pathway evidence_span: {"source_cache": "artifacts/aspirin-research/9660772.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "49e5d050a7b1505f537ae535df4e7a51563a72d528973779baf53c963b50c259", "start_char": 0, "end_char": 1662, "text_sha256": "49e5d050a7b1505f537ae535df4e7a51563a72d528973779baf53c963b50c259"} [asa-p9660772] Aspirin inhibition and acetylation of the plant cytochrome P450, allene oxide synthase, resembles that of animal prostaglandin endoperoxide H synthase. (1998). https://pubmed.ncbi.nlm.nih.gov/9660772/ DOI: 10.1074/jbc.273.29.18139
    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