Subunit conformation of yeast alcohol dehydrogenase.
نویسندگان
چکیده
منابع مشابه
Yeast Alcohol Dehydrogenase : Molecular Weight
The alcohol dehydrogenases (ADH) crystallized from yeast (1, 2) and from horse liver (3) differ in many of their properties. The mammalian enzyme forms a complex with reduced diphosphopyridine nucleotide in which the absorption band of the coenzyme at 340 rnp is shifted to 325 rnh (4). This permitted the direct study by Theorell and Chance (5) of the stoichiometry and dissociation constant of t...
متن کاملYeast Alcohol Dehydrogenase Structure and Catalysis
Yeast (Saccharomyces cerevisiae) alcohol dehydrogenase I (ADH1) is the constitutive enzyme that reduces acetaldehyde to ethanol during the fermentation of glucose. ADH1 is a homotetramer of subunits with 347 amino acid residues. A structure for ADH1 was determined by X-ray crystallography at 2.4 Å resolution. The asymmetric unit contains four different subunits, arranged as similar dimers named...
متن کاملAromatic aldehydes as substrates for yeast and yeast alcohol dehydrogenase.
The conversion of benzaldehyde to optically active L-phenylacetyl carbinol by yeast fermentation is a key step in the manufacture of L-ephedrine. ’ Typical fermentation raw materials are molasses, which provides a source of hexoses for glycolysis, and benzaldehyde. L-phenylacetyl carbinol formation is catalyzed by the pyruvate decarboxylase complex.’ In the carboligase reaction, pyruvate is dec...
متن کاملRole of the essential thiol groups of yeast alcohol dehydrogenase.
1. Yeast alcohol dehydrogenase inactivated by reaction with iodoacetamide retains 85% of the original NADH-binding capacity as measured under conditions of saturating coenzyme concentration. 2. The dissociation constant of the enzyme-NADH complex is unaffected by inactivation of the enzyme with iodoacetamide, and the affinity of the enzyme for NAD(+) and pyridine-3-aldehyde-adenine dinucleotide...
متن کاملEffects of silver and mercurials on yeast alcohol dehydrogenase.
Two specific chemical oci have been implicated in the catalytic action of yeast alcohol dehydrogenase: sulfhydryl groups (2-5) and zinc (6, 7). The activity of this enzyme is inhibited by agents considered to interact with SH groups, e.g. iodoacetate (3)) iodosobenzoate (5)) iodoacetamide (5), trivalent arsenicals (4,5), N’-ethyhnaleimide,’ ultraviolet irradiation (8)) and certain metal ions: A...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1978
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)34307-7