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 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.

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

Effects of Pressure on the Kinetics of Capture by Yeast Alcohol Dehydrogenase†

Biochemistry ◽  
1999 ◽  
Vol 38 (23) ◽  
pp. 7470-7475 ◽  
Author(s):  
Yong-Kweon Cho ◽  
Dexter B. Northrop
Keyword(s):  
Alcohol Dehydrogenase ◽  
Yeast Alcohol Dehydrogenase ◽  
Kinetics Of

scholarly journals A study of the pH- and temperature-dependence of the reactions of yeast alcohol dehydrogenase with ethanol, acetaldehyde and butyraldehyde as substrates

1975 ◽  
Vol 147 (2) ◽  
pp. 303-311 ◽  
Author(s):  
C J Dickenson ◽  
F M Dickinson
Keyword(s):  
Alcohol Dehydrogenase ◽  
Temperature Dependence ◽  
Initial Rate ◽  
British Library ◽  
Yeast Alcohol Dehydrogenase ◽  
Wide Range ◽  
Mechanism Of Catalysis ◽  
Ph Range ◽  
Kinetics Of ◽  
Kinetics Of Reduction

The kinetics of ethanol oxidation by NAD+, and acetaldehyde and butyraldehyde reduction by NADH, catalysed by yeast alcohol dehydrogenase, were studied in the pH range 4.9--9.9 at 25 degrees C and in the temperature range 14.8--43.5 degrees C at pH 7.05. The kinetics of reduction of acetaldehyde by [4A-2H]NADH at pH 7.05 and pH 8.9 at 25 degrees C were also studied. The results of the kinetic experiments indicate that the mechanism of catalysis, previously proposed on the basis of studies at pH 7.05 and 25 degrees C (Dickinson & Monger, 1973), applies over the wide range of conditions now tested. Values of some of the initial-rate parameters obtained were used to deduce information about the pH- and temperature-dependence of the specific rates of combination of enzyme and coenzymes and of the dissociation of the enzyme--coenzyme compounds. Primary and secondary plots of initial-rate data are deposited as Supplementary Publication SUP 50043 (20 pages) with the British Library (Lending Division), Boston Spa, Wetherby, Yorks. LS23 7BQ, U.K., from whom copies may be obtained under the terms indicated in Biochem. J. (1975) 145, 5.

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