The catalytic zinc atom of alcohol dehydrogenase: molecular mechanisms & dependencies

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.

Human evidence only

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)

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.
Zinc → Horse liver alcohol dehydrogenase, the crystallographic model enzyme source_derived_draftungraded
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
In the closed subunits the catalytic zinc holds the substrate oxygen in classical tetrahedral coordination with Cys-43, Cys-153 and His-66, while in the open subunits the zinc takes an inverted coordination that adds the carboxylate of Glu-67, which may be an intermediate in displacing the zinc-bound water with the alcohol substrate.
Zinc → Saccharomyces cerevisiae alcohol dehydrogenase I / ADH1 source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/alcohol-research/25157460.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "c91a7069c53b4af61096bdc09ce952b0277d63d547a94e5d3870d2980aa31e20", "start_char": 0, "end_char": 1560, "text_sha256": "c91a7069c53b4af61096bdc09ce952b0277d63d547a94e5d3870d2980aa31e20"}
experimental_model
X-ray crystallography of yeast ADH1 at 2.4 angstrom with site-directed mutagenesis
exposure
Coenzyme-bound closed and open subunit conformations
limitations
A yeast enzyme, used because its asymmetric tetramer captures two catalytic states. The zinc coordination chemistry is conserved, but kinetic numbers are yeast numbers.
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
Yeast enzyme
plain_language
Three amino acids hold the zinc, and a fourth swings in to hand over the alcohol.
primary_references
[alcohol-p25157460] Yeast alcohol dehydrogenase structure and catalysis. (2014). https://pubmed.ncbi.nlm.nih.gov/25157460/ DOI: 10.1021/bi5006442
tissue_or_cell_type
Purified homotetramer
Alcohol: ethanol clearance, acetaldehyde, the channels it binds, organ injury and nutrient collisions (2026-09-21) · lines 72–83
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · X-ray crystallography of yeast ADH1 at 2.4 angstrom with site-directed mutagenesis · source_derived_draft · unverified_draft
### alcohol-zinc-coordination-chemistry In the closed subunits the catalytic zinc holds the substrate oxygen in classical tetrahedral coordination with Cys-43, Cys-153 and His-66, while in the open subunits the zinc takes an inverted coordination that adds the carboxylate of Glu-67, which may be an intermediate in displacing the zinc-bound water with the alcohol substrate. 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: Three amino acids hold the zinc, and a fourth swings in to hand over the alcohol. organism: Yeast enzyme tissue_or_cell_type: Purified homotetramer experimental_model: X-ray crystallography of yeast ADH1 at 2.4 angstrom with site-directed mutagenesis limitations: A yeast enzyme, used because its asymmetric tetramer captures two catalytic states. The zinc coordination chemistry is conserved, but kinetic numbers are yeast numbers. exposure: Coenzyme-bound closed and open subunit conformations evidence_span: {"source_cache": "artifacts/alcohol-research/25157460.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "c91a7069c53b4af61096bdc09ce952b0277d63d547a94e5d3870d2980aa31e20", "start_char": 0, "end_char": 1560, "text_sha256": "c91a7069c53b4af61096bdc09ce952b0277d63d547a94e5d3870d2980aa31e20"} [alcohol-p25157460] Yeast alcohol dehydrogenase structure and catalysis. (2014). https://pubmed.ncbi.nlm.nih.gov/25157460/ DOI: 10.1021/bi5006442
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.

The catalytic zinc atom of alcohol dehydrogenase