Results 131 to 140 of about 1,029 (146)
Some of the next articles are maybe not open access.
Nitrogen base inhibition of yeast alcohol dehydrogenase
Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation, 1966Summary The oxidation of ethanol as catalyzed by yeast alcohol dehydrogenase (alcohol: NAD + oxidoreductase, EC 1.1.1.1) is inhibited by a variety of nitrogen bases. Inhibition by 2,9-dimethyl-1,10-phenanthroline, 1,5-phenanthroline, 5,6-benzoquinoline, 7,8-benzoquinoline, quinoline and adenosine was in each case shown to be competitive with respect
B M, Anderson +2 more
openaire +2 more sources
The intrinsic zinc atoms of yeast alcohol dehydrogenase
Biochemical and Biophysical Research Communications, 1975The intrinsic Zn content of yeast alcohol dehydrogenase (YADH) has been determined by three highly sensitive analytical techniques. The enzyme prepared from baker's yeast has a specific activity of 430–460 U/mg and contains 4 intrinsically bound Zn atoms per tetrameric enzyme of molecular weight 150,000.
C, Veillon, A J, Sytkowski
openaire +2 more sources
Hydrophobic interactions of inhibitors with yeast alcohol dehydrogenase
Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation, 1965Summary Eleven N1-alkylnicotinamide chlorides have been prepared and studied as inhibitors in the yeast alcohol dehydrogenase (alcohol :NAD+ oxidoreductase, EC 1.1.1.1) catalyzed oxidation of ethanol. The effectiveness of these inhibitors increased with increasing chain length of the alkyl substituent.
B M, ANDERSON +2 more
openaire +2 more sources
Inactivation of yeast alcohol dehydrogenase by N-alkylmaleimides
Archives of Biochemistry and Biophysics, 1968Abstract Seven N-alkylmaleamic acids were synthesized and converted through heating to the corresponding N-alkylmaleimides. Alkylmaleimides of varying chainlength were shown to effectively inactivate yeast alcohol dehydrogenase at pH 7.0. The effect of pH on the rate of hydrolysis of N-ethylmaleimide was studied in the pH range from 8.6 to 9.4 where ...
J R, Heitz, C D, Anderson, B M, Anderson
openaire +2 more sources
Coenzyme binding capacity of yeast alcohol dehydrogenase
Biochemical and Biophysical Research Communications, 1978Abstract Commercial lyophilized preparations of yeast alcohol dehydrogenase from Boehringer G.m.b.H. (Mannheim, Germany) bind 2 mols of reduced coenzyme/144000 g of enzyme (1). After the purification by a DEAE-Sephadex column chromatography, the coenzyme binding capacity is raised to 4 mols of NADH/mol of enzyme.
V, Leskovac, D, Pericin
openaire +2 more sources
Effect of Rotenone on the Alcohol Dehydrogenase of Yeast Mitochondria
Nature, 1967CHANCE1 applied the crossover theorem to a study of intact yeast cells, and reported an apparent crossover point (or phosphorylation site) between pyridine nucleotide and flavoprotein (site I), between cytochromes b and c (site II) and between eytochrome c and cytochrome oxidase (site III). These observations led to the expectation that intact isolated
W X, Balcavage, J R, Mattoon
openaire +2 more sources
Synthesis of Drosophila melanogaster alcohol dehydrogenase in yeast
Gene, 1990Expression systems for the heterologous expression of Drosophila melanogaster alcohol dehydrogenase (ADH) in Saccharomyces cerevisiae have been designed, analyzed and compared. Four different yeast/Escherichia coli shuttle vectors were constructed and used to transform four different yeast strains.
Atrian S +2 more
openaire +3 more sources
Inhibition of yeast alcohol dehydrogenase by alkylammonium chlorides
Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1965Abstract Five alkylammonium chlorides were shown to be competitive inhibitors with respect to NAD + in the yeast alcohol dehydrogenase (alcohol:NAD + oxidoreductase, EC 1.1.1.1)-catalyzed oxidation of ethanol. This inhibition increases with increasing chain length of the alkyl substituents of these compounds and is consistent with a hydrophobic ...
B M, ANDERSON, M L, REYNOLDS
openaire +2 more sources
Production of yeast alcohol dehydrogenase isoenzymes by selection
Nature, 1976Mutants of yeast alcohol dehydrogenase have been produced that protect the cell against the poisonous aldehyde acrolein by increasing the NADH-NAD ratio. The altered properties include changes both in binding constants and in cooperativity. Such mutants may be useful in exploring the nature of adaptation at the molecular level.
openaire +2 more sources
Regulation of Yeast Alcohol Dehydrogenase Isozymes
1981The two major alcohol dehydrogenases of yeast are coded by separate nuclear genes, and show 95% amino acid homology. Nonetheless, the “constitutive” ADH, ADH-I, preferentially catalyzes the reaction acetaldehyde → ethanol, and the inducible ADH, ADH-II, preferentially catalyzes the reverse reaction.
Christopher Wills +2 more
openaire +1 more source