Steering the enzymatic activity of proteins by ionic liquids. A case study of the enzyme kinetics of yeast alcohol dehydrogenase

2012 ◽  
Vol 14 (13) ◽  
pp. 4635 ◽  
Author(s):  
Sebastian Weibels ◽  
Adrian Syguda ◽  
Christian Herrmann ◽  
Hermann Weingärtner
Keyword(s):  
Ionic Liquids ◽  
Alcohol Dehydrogenase ◽  
Enzymatic Activity ◽  
Enzyme Kinetics ◽  
Yeast Alcohol Dehydrogenase ◽  
Kinetics Of

scholarly journals Kinetics of metal extraction in ionic liquids: Eu3+/HNO3//TODGA/[C1C4im][Tf2N] as a case study

RSC Advances ◽  
2013 ◽  
Vol 3 (27) ◽  
pp. 10736 ◽  
Author(s):  
Michal Sypula ◽  
Ali Ouadi ◽  
Clotilde Gaillard ◽  
Isabelle Billard
Keyword(s):  
Ionic Liquids ◽  
Metal Extraction ◽  
Kinetics Of

scholarly journals A study of the oxidation of butan-1-ol and propan-2-ol by nicotinamide-adenine dinucleotide catalysed by yeast alcohol dehydrogenase.

1975 ◽  
Vol 147 (3) ◽  
pp. 541-547 ◽  
Author(s):  
C J Dickenson ◽  
F M Dickinson
Keyword(s):  
Alcohol Dehydrogenase ◽  
Ternary Complexes ◽  
Kinetics Of Oxidation ◽  
Yeast Alcohol Dehydrogenase ◽  
Rate Limiting Step ◽  
Limiting Step ◽  
Ph Range ◽  
Rate Limiting ◽  
Kinetics Of ◽  
Flow Experiments

1. The kinetics of oxidation of butan-1-ol and propan-2-ol by NAD+, catalysed by yeast alcohol dehydrogenase, were studied at 25 degrees C from pH 5.5 to 10, and at pH 7.05 from 14 degrees to 44 degrees C, 2. Under all conditions studied the results are consistent with a mechanism whereby some dissociation of coenzyme from the active enzyme-NAD+-alcohol ternary complexes occurs, and the mechanism is therefore not strictly compulsory order. 3. A primary 2H isotopic effect on the maximum rates of oxidation of [1-2H2]butan-1-ol and [2H7]propan-2-ol was found at 25 degrees C over the pH range 5.5-10. Further, in stopped-flow experiments at pH 7.05 and 25 degrees C, there was no transient formation of NADH in the oxidation of butan-1-ol and propan-2-ol. The principal rate-limiting step in the oxidation of dependence on pH of the maximum rates of oxidation of butan-1-ol and propan-2-ol is consisten with the possibility that histidine and cysteine residues may affect or control catalysis.

scholarly journals A study of the kinetics and mechanism of yeast alcohol dehydrogenase with a variety of substrates

1973 ◽  
Vol 131 (2) ◽  
pp. 261-270 ◽  
Author(s):  
F. M. Dickinson ◽  
G. P. Monger
Keyword(s):  
Alcohol Dehydrogenase ◽  
Ethanol Oxidation ◽  
Ternary Complexes ◽  
Kinetics Of Oxidation ◽  
Yeast Alcohol Dehydrogenase ◽  
Rate Limiting Step ◽  
Limiting Step ◽  
Binary Complexes ◽  
Rate Limiting ◽  
Kinetics Of

1. The kinetics of oxidation of ethanol, propan-1-ol, butan-1-ol and propan-2-ol by NAD+ and of reduction of acetaldehyde and butyraldehyde by NADH catalysed by yeast alcohol dehydrogenase were studied. 2. Results for the aldehyde–NADH reactions are consistent with a compulsory-order mechanism with the rate-limiting step being the dissociation of the product enzyme–NAD+ complex. In contrast the results for the alcohol–NAD+ reactions indicate that some dissociation of coenzyme from the active enzyme–NAD+–alcohol ternary complexes must occur and that the mechanism is not strictly compulsory-order. The rate-limiting step in ethanol oxidation is the dissociation of the product enzyme–NADH complex but with the other alcohols it is probably the catalytic interconversion of ternary complexes. 3. The rate constants describing the combination of NAD+ and NADH with the enzyme and the dissociations of these coenzymes from binary complexes with the enzyme were measured.

Kinetics of Irreversible Inhibition of Yeast Alcohol Dehydrogenase during Modification by o-Phthaldehyde

1994 ◽  
Vol 48 (3) ◽  
pp. 183-190 ◽  
Author(s):  
Wei-Ping Le ◽  
Si-Xu Yan ◽  
Ming-Qian Huang ◽  
Ying-Xia Zhang ◽  
Hai-Meng Zhou
Keyword(s):  
Alcohol Dehydrogenase ◽  
Irreversible Inhibition ◽  
Yeast Alcohol Dehydrogenase ◽  
Kinetics Of

scholarly journals Effects of Pressure on the Kinetics of Capture by Yeast Alcohol Dehydrogenase

Biochemistry ◽  
1999 ◽  
Vol 38 (33) ◽  
pp. 10908-10908
Author(s):  
Yong-Kweon Cho ◽  
Dexter B. Northrop
Keyword(s):  
Alcohol Dehydrogenase ◽  
Yeast Alcohol Dehydrogenase ◽  
Kinetics Of

Alcohol dehydrogenase polymorphism inDrosophila: Enzyme kinetics of product inhibition

1988 ◽  
Vol 28 (1-2) ◽  
pp. 145-150 ◽  
Author(s):  
Pieter W. H. Heinstra ◽  
Willem Scharloo ◽  
George E. W. Thorig
Keyword(s):  
Alcohol Dehydrogenase ◽  
Enzyme Kinetics ◽  
Product Inhibition ◽  
Kinetics Of

scholarly journals Enzyme Kinetics of Native and Recombinant Secondary Alcohol Dehydrogenase originated from Micrococcus leuteus WIUJH20

2011 ◽  
Vol 25 (S1) ◽  
Author(s):  
Jenq‐Kuen Huang ◽  
Nick D Youngblut ◽  
Nicholas J Shoger ◽  
Vamshi Takkalpalli ◽  
Chi‐Tsai Lin ◽  
...  
Keyword(s):  
Alcohol Dehydrogenase ◽  
Enzyme Kinetics ◽  
Secondary Alcohol ◽  
Secondary Alcohol Dehydrogenase ◽  
Kinetics Of
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