Component
Bacterial and nematode carnitine dehydratases
Bacterial and nematode carnitine dehydratases. 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 acts on it
A complementary DNA clone encoding 2-arylpropionyl-CoA epimerase was isolated from rat liver, expressed in Escherichia coli and confirmed by measuring the rate of inversion of R-ibuprofenoyl-CoA, and significant amino acid sequence similarity was found with carnitine dehydratases from Caenorhabditis elegans at 41% and Escherichia coli at 27%, suggesting that this protein, characterised until then only for its role in drug transformation, has a function in lipid metabolism; the R enantiomer is described as inactive in terms of cyclooxygenase inhibition.
Experimental context and source evidence
- evidence_span
- {"source_cache": "artifacts/ibuprofen-research/9106621.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d2ece633650b8d636b2d0315b6d6486f618f7aae8a585c54558dffe344edf0cf", "start_char": 0, "end_char": 1607, "text_sha256": "d2ece633650b8d636b2d0315b6d6486f618f7aae8a585c54558dffe344edf0cf"}
- experimental_model
- Molecular cloning and bacterial expression of 2-arylpropionyl-CoA epimerase from a rat liver complementary DNA library
- exposure
- Expressed epimerase assayed by rate of inversion of R-ibuprofenoyl-CoA
- limitations
- Identifies the gene and, through its homology, suggests the enzyme is not a drug-metabolising enzyme at all. Sequence homology is an inference about function, not a demonstration.
- 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
- Rat
- plain_language
- The enzyme that activates this drug looks like an enzyme for handling fats, which is probably its real job.
- primary_references
- [ibu-p9106621] Molecular cloning and expression of a 2-arylpropionyl-coenzyme A epimerase: a key enzyme in the inversion metabolism of ibuprofen. (1997). https://pubmed.ncbi.nlm.nih.gov/9106621/ DOI: 10.1124/mol.51.4.576
- tissue_or_cell_type
- Liver
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Molecular cloning and bacterial expression of 2-arylpropionyl-CoA epimerase from a rat liver complementary DNA library · source_derived_draft · unverified_draft
### ibu-the-enzyme-is-a-lipid-enzyme A complementary DNA clone encoding 2-arylpropionyl-CoA epimerase was isolated from rat liver, expressed in Escherichia coli and confirmed by measuring the rate of inversion of R-ibuprofenoyl-CoA, and significant amino acid sequence similarity was found with carnitine dehydratases from Caenorhabditis elegans at 41% and Escherichia coli at 27%, suggesting that this protein, characterised until then only for its role in drug transformation, has a function in lipid metabolism; the R enantiomer is described as inactive in terms of cyclooxygenase inhibition. 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 enzyme that activates this drug looks like an enzyme for handling fats, which is probably its real job. organism: Rat tissue_or_cell_type: Liver experimental_model: Molecular cloning and bacterial expression of 2-arylpropionyl-CoA epimerase from a rat liver complementary DNA library limitations: Identifies the gene and, through its homology, suggests the enzyme is not a drug-metabolising enzyme at all. Sequence homology is an inference about function, not a demonstration. exposure: Expressed epimerase assayed by rate of inversion of R-ibuprofenoyl-CoA evidence_span: {"source_cache": "artifacts/ibuprofen-research/9106621.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d2ece633650b8d636b2d0315b6d6486f618f7aae8a585c54558dffe344edf0cf", "start_char": 0, "end_char": 1607, "text_sha256": "d2ece633650b8d636b2d0315b6d6486f618f7aae8a585c54558dffe344edf0cf"} [ibu-p9106621] Molecular cloning and expression of a 2-arylpropionyl-coenzyme A epimerase: a key enzyme in the inversion metabolism of ibuprofen. (1997). https://pubmed.ncbi.nlm.nih.gov/9106621/ DOI: 10.1124/mol.51.4.576
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.