scholarly journals Carboxyl groups near the active site zinc contribute to catalysis in yeast alcohol dehydrogenase.

1988 ◽  
Vol 263 (11) ◽  
pp. 5446-5454
Author(s):  
A J Ganzhorn ◽  
B V Plapp
Keyword(s):  
Alcohol Dehydrogenase ◽  
Active Site ◽  
Carboxyl Groups ◽  
Yeast Alcohol Dehydrogenase

Active-site sulfhydryl groups of yeast alcohol dehydrogenase

Biochemistry ◽  
1973 ◽  
Vol 12 (15) ◽  
pp. 2856-2862 ◽  
Author(s):  
Jer-Shung Twu ◽  
Christopher C. Q. Chin ◽  
Finn Wold
Keyword(s):  
Alcohol Dehydrogenase ◽  
Active Site ◽  
Sulfhydryl Groups ◽  
Yeast Alcohol Dehydrogenase

Effect of pH on the reactivity of the active-site sulfhydryl groups in yeast alcohol dehydrogenase

Biochemistry ◽  
1974 ◽  
Vol 13 (16) ◽  
pp. 3418-3420 ◽  
Author(s):  
Carl J. Belke ◽  
Christopher C. Q. Chin ◽  
Finn Wold
Keyword(s):  
Alcohol Dehydrogenase ◽  
Active Site ◽  
Sulfhydryl Groups ◽  
Effect Of Ph ◽  
Yeast Alcohol Dehydrogenase

scholarly journals Subunit conformation of yeast alcohol dehydrogenase.

1978 ◽  
Vol 253 (23) ◽  
pp. 8414-8419
Author(s):  
H. Jörnvall ◽  
H. Eklund ◽  
C.I. Brändén
Keyword(s):  
Alcohol Dehydrogenase ◽  
Yeast Alcohol Dehydrogenase

scholarly journals Isomerization of an enzyme-coenzyme complex in yeast alcohol dehydrogenase-catalysed reactions

2003 ◽  
Vol 68 (2) ◽  
pp. 77-84 ◽  
Author(s):  
Vladimir Leskovac ◽  
Svetlana Trivic ◽  
Draginja Pericin
Keyword(s):  
Alcohol Dehydrogenase ◽  
Rate Constants ◽  
Equilibrium Constants ◽  
Kinetic Mechanism ◽  
Yeast Alcohol Dehydrogenase ◽  
Catalyzed Reactions ◽  
The Individual ◽  
Individual Rate ◽  
Catalyzed Oxidation

In this work, all the rate constants in the kinetic mechanism of the yeast alcohol dehydrogenase-catalyzed oxidation of ethanol by NAD+, at pH 7.0, 25 ?C, have been estimated. The determination of the individual rate constants was achieved by fitting the reaction progress curves to the experimental data, using the procedures of the FITSIM and KINSIM software package of Carl Frieden. This work is the first report in the literature showing the internal equilibrium constants for the isomerization of the enzyme-NAD+ complex in yeast alcohol dehydrogenase-catalyzed reactions.

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