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The zinc coordination chemistry is conserved, but kinetic numbers are yeast numbers.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes.","comparator":null,"unit":null,"notes":"","entity":{"slug":"ethanol","display_name":"Ethanol","entity_type_key":"drug"}},{"dimension":"organism","value_text":"Yeast enzyme","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"Change that one residue and the enzyme works a hundred times worse.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[alcohol-p25157460] Yeast alcohol dehydrogenase structure and catalysis. 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The zinc coordination chemistry is conserved, but kinetic numbers are yeast numbers.\nexposure: Coenzyme-bound closed and open subunit conformations\nevidence_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\"}\n[alcohol-p25157460] Yeast alcohol dehydrogenase structure and catalysis. (2014). https://pubmed.ncbi.nlm.nih.gov/25157460/ DOI: 10.1021/bi5006442","model_system":"X-ray crystallography of yeast ADH1 at 2.4 angstrom with site-directed mutagenesis","directness":"author_interpretation","verification_status":"source_derived_draft","notes":"Exact curation-document quotation, not publisher quotation. 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