Component
The deacylating water molecule of the fatty acid amide hydrolase mechanism
The deacylating water molecule of the fatty acid amide hydrolase mechanism. 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.
Where it participates (unsigned role)
The crystal structure of fatty acid amide hydrolase bound to URB597 revealed a deacylating water molecule and gave insight into how the enzyme is inactivated by carbamate inhibitors.
Experimental context and source evidence
- evidence_span
- {"source_cache": "artifacts/thc-research/20493882.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "c5acef9899dc5e90f996fb08c58b547c167bdbb2c879e1bd669a531fd10c3368", "start_char": 0, "end_char": 1382, "text_sha256": "c5acef9899dc5e90f996fb08c58b547c167bdbb2c879e1bd669a531fd10c3368"}
- experimental_model
- Crystal structure of fatty acid amide hydrolase bound to the carbamate inhibitor URB597
- exposure
- Inhibitor-bound structure
- limitations
- Identifies the water molecule that explains why the inhibitor is slowly reversible. Rat enzyme structure.
- nutrient_topic
- THC research collection; topical membership is not evidence of a direct clinical effect, and THC is recorded separately from the endocannabinoids it imitates. · Delta-9-tetrahydrocannabinol / THC
- organism
- Rat enzyme
- plain_language
- The structure shows exactly how the enzyme is jammed, down to a single water molecule.
- primary_references
- [thc-p20493882] Crystal structure of fatty acid amide hydrolase bound to the carbamate inhibitor URB597: discovery of a deacylating water molecule and insight into enzyme inactivation. (2010). https://pubmed.ncbi.nlm.nih.gov/20493882/ DOI: 10.1016/j.jmb.2010.05.034
- tissue_or_cell_type
- Purified enzyme
THC: the cannabinoid receptors, the endocannabinoid system it occupies, what the drug does, and the dietary fat it is built from (2026-09-21) · lines 374–385
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Crystal structure of fatty acid amide hydrolase bound to the carbamate inhibitor URB597 · source_derived_draft · unverified_draft
### thc-faah-mechanism The crystal structure of fatty acid amide hydrolase bound to URB597 revealed a deacylating water molecule and gave insight into how the enzyme is inactivated by carbamate inhibitors. Condition category: normal nutrient_topic: THC research collection; topical membership is not evidence of a direct clinical effect, and THC is recorded separately from the endocannabinoids it imitates. plain_language: The structure shows exactly how the enzyme is jammed, down to a single water molecule. organism: Rat enzyme tissue_or_cell_type: Purified enzyme experimental_model: Crystal structure of fatty acid amide hydrolase bound to the carbamate inhibitor URB597 limitations: Identifies the water molecule that explains why the inhibitor is slowly reversible. Rat enzyme structure. exposure: Inhibitor-bound structure evidence_span: {"source_cache": "artifacts/thc-research/20493882.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "c5acef9899dc5e90f996fb08c58b547c167bdbb2c879e1bd669a531fd10c3368", "start_char": 0, "end_char": 1382, "text_sha256": "c5acef9899dc5e90f996fb08c58b547c167bdbb2c879e1bd669a531fd10c3368"} [thc-p20493882] Crystal structure of fatty acid amide hydrolase bound to the carbamate inhibitor URB597: discovery of a deacylating water molecule and insight into enzyme inactivation. (2010). https://pubmed.ncbi.nlm.nih.gov/20493882/ DOI: 10.1016/j.jmb.2010.05.034
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.