Component
The Glu-67 carboxylate of yeast alcohol dehydrogenase
The Glu-67 carboxylate of yeast alcohol dehydrogenase. Species, exposure and limitations are retained in each linked claim.
2 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
Substituting Glu-67 with glutamine decreased catalytic efficiency a hundred-fold.
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
- Change that one residue and the enzyme works a hundred times worse.
- 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 85–96
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-glu67-catalytic-efficiency Substituting Glu-67 with glutamine decreased catalytic efficiency a hundred-fold. 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: Change that one residue and the enzyme works a hundred times worse. 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
Where it participates (unsigned role)
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.
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.