Component
Cyclooxygenase-1 with asparagine substituted at position 530
Cyclooxygenase-1 with asparagine substituted at position 530. 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.
Other things that act on it
Enzymes, hormones, genes, and other components with a recorded effect. These are not nutrients, so they do not count toward the arrows above. Each finding names the chapter that recorded it.
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.
What it acts on
The Ala530 mutant of prostaglandin endoperoxide synthase had both cyclooxygenase and hydroperoxidase activity while the Asn530 mutant lacked cyclooxygenase activity but retained hydroperoxidase activity, establishing that the hydroxyl group of Ser530 is not essential for catalysis or substrate binding and suggesting that a bulky group at position 530, such as that introduced by aspirin acetylation, prevents arachidonate binding to the cyclooxygenase active site.
Experimental context and source evidence
- evidence_span
- {"source_cache": "artifacts/aspirin-research/2144687.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0a66f17b41129423ecb73bf520dad47b666792a6477552db04272474fc79be24", "start_char": 0, "end_char": 1595, "text_sha256": "0a66f17b41129423ecb73bf520dad47b666792a6477552db04272474fc79be24"}
- experimental_model
- Sequence comparison and site-directed mutagenesis across sheep, mouse and human prostaglandin endoperoxide synthase
- exposure
- Ser530 replaced with alanine and with asparagine, and tetranitromethane modification with ibuprofen protection
- limitations
- Extends the single mutant to a pair that differ in bulk. Sequence-based assignment of the heme ligands is inference from similarity, not structure.
- 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
- Sheep, mouse and human enzyme
- plain_language
- Swap in a small residue and the enzyme is fine; swap in a bigger one and the cyclooxygenase half stops.
- primary_references
- [asa-p2144687] Structure-function relationships in sheep, mouse, and human prostaglandin endoperoxide G/H synthases. (1990). https://pubmed.ncbi.nlm.nih.gov/2144687/
- tissue_or_cell_type
- Recombinant enzyme
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Sequence comparison and site-directed mutagenesis across sheep, mouse and human prostaglandin endoperoxide synthase · source_derived_draft · unverified_draft
### asa-bulk-not-identity The Ala530 mutant of prostaglandin endoperoxide synthase had both cyclooxygenase and hydroperoxidase activity while the Asn530 mutant lacked cyclooxygenase activity but retained hydroperoxidase activity, establishing that the hydroxyl group of Ser530 is not essential for catalysis or substrate binding and suggesting that a bulky group at position 530, such as that introduced by aspirin acetylation, prevents arachidonate binding to the cyclooxygenase active site. 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: Swap in a small residue and the enzyme is fine; swap in a bigger one and the cyclooxygenase half stops. organism: Sheep, mouse and human enzyme tissue_or_cell_type: Recombinant enzyme experimental_model: Sequence comparison and site-directed mutagenesis across sheep, mouse and human prostaglandin endoperoxide synthase limitations: Extends the single mutant to a pair that differ in bulk. Sequence-based assignment of the heme ligands is inference from similarity, not structure. exposure: Ser530 replaced with alanine and with asparagine, and tetranitromethane modification with ibuprofen protection evidence_span: {"source_cache": "artifacts/aspirin-research/2144687.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0a66f17b41129423ecb73bf520dad47b666792a6477552db04272474fc79be24", "start_char": 0, "end_char": 1595, "text_sha256": "0a66f17b41129423ecb73bf520dad47b666792a6477552db04272474fc79be24"} [asa-p2144687] Structure-function relationships in sheep, mouse, and human prostaglandin endoperoxide G/H synthases. (1990). https://pubmed.ncbi.nlm.nih.gov/2144687/
Complete structured claim and evidence
The events it takes part in
A mechanism often involves more than two components. These are the full events, with every participant and its role.
Situations it appears in
Low-supply and faulty-machinery situations recorded in the chapters where this component plays a part.
In the sources
Preserved passages that mention this component, quoted exactly. Open one to read it in context.
Open hypotheses
Proposed ideas that involve this component. They are labeled as hypotheses and do not change any recorded statement.
This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.