Binding of coenzymes to yeast alcohol dehydrogenase
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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 کاملInteractions of substrates, inhibitors, and coenzymes at the active site of horse liver alcohol dehydrogenase.
2,2-Bipyridine chelates 2 zinc ions of horse liver alcohol dehydrogenase with a dissociation constant of 4.0 X low4 M. The complex shows an absorption maximum at 308 rnp with a difference extinction coefficient of 1 .l X lo4 M+ cm-r per zinc ion. Because bipyridine binds the enzyme less tightly than o-phenanthroline, and because the principal absorption maximum of the difference spectrum appear...
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...
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ژورنال
عنوان ژورنال: Journal of the Serbian Chemical Society
سال: 2010
ISSN: 0352-5139,1820-7421
DOI: 10.2298/jsc1002185l