Component
Horse liver alcohol dehydrogenase, the crystallographic model enzyme
Horse liver alcohol dehydrogenase, the crystallographic model enzyme. 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
Each subunit of the dimeric enzyme is organised into two unequal parts separated by a wide deep active-site cleft, with the catalytic zinc atoms bound at the bottom of the clefts about 20 angstrom from the molecular surface, and the adenosine moiety of the coenzyme bound within the smaller region.
Experimental context and source evidence
- evidence_span
- {"source_cache": "artifacts/alcohol-research/4365379.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "857dc9a65cac403f6591e0f33ea1bd3295f4a997274a26c362a3f392dbe9c987", "start_char": 0, "end_char": 912, "text_sha256": "857dc9a65cac403f6591e0f33ea1bd3295f4a997274a26c362a3f392dbe9c987"}
- experimental_model
- X-ray crystallography of horse liver alcohol dehydrogenase at 2.9 angstrom
- exposure
- Inhibitor-bound and coenzyme-bound states
- limitations
- The founding structure of the enzyme family, in horse liver enzyme. It establishes where the zinc and the coenzyme sit; it is not a human kinetic measurement.
- nutrient_topic
- Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. · Ethanol
- organism
- Horse enzyme
- plain_language
- The zinc that does the chemistry sits at the bottom of a deep slot, far from the surface.
- primary_references
- [alcohol-p4365379] Structure of liver alcohol dehydrogenase at 2.9-angstrom resolution. (1973). https://pubmed.ncbi.nlm.nih.gov/4365379/ DOI: 10.1073/pnas.70.8.2439
- tissue_or_cell_type
- Purified dimeric enzyme
Alcohol: ethanol clearance, acetaldehyde, the channels it binds, organ injury and nutrient collisions (2026-09-21) · lines 59–70
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · X-ray crystallography of horse liver alcohol dehydrogenase at 2.9 angstrom · source_derived_draft · unverified_draft
### alcohol-adh-catalytic-zinc-position Each subunit of the dimeric enzyme is organised into two unequal parts separated by a wide deep active-site cleft, with the catalytic zinc atoms bound at the bottom of the clefts about 20 angstrom from the molecular surface, and the adenosine moiety of the coenzyme bound within the smaller region. Condition category: normal nutrient_topic: Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. plain_language: The zinc that does the chemistry sits at the bottom of a deep slot, far from the surface. organism: Horse enzyme tissue_or_cell_type: Purified dimeric enzyme experimental_model: X-ray crystallography of horse liver alcohol dehydrogenase at 2.9 angstrom limitations: The founding structure of the enzyme family, in horse liver enzyme. It establishes where the zinc and the coenzyme sit; it is not a human kinetic measurement. exposure: Inhibitor-bound and coenzyme-bound states evidence_span: {"source_cache": "artifacts/alcohol-research/4365379.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "857dc9a65cac403f6591e0f33ea1bd3295f4a997274a26c362a3f392dbe9c987", "start_char": 0, "end_char": 912, "text_sha256": "857dc9a65cac403f6591e0f33ea1bd3295f4a997274a26c362a3f392dbe9c987"} [alcohol-p4365379] Structure of liver alcohol dehydrogenase at 2.9-angstrom resolution. (1973). https://pubmed.ncbi.nlm.nih.gov/4365379/ DOI: 10.1073/pnas.70.8.2439
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.