Probing the Active Site of Yeast Alcohol Dehydrogenase through Microscale Yeast-Mediated Reductions of Acetophenone and Acetylpyridines. A Collaborative and Research-Based Advanced Bioorganic Chemistry Laboratory Project

2000 ◽  
Vol 77 (3) ◽  
pp. 363 ◽  
Author(s):  
Michael Carnahan ◽  
Kari Cox ◽  
Joey Espinosa ◽  
Ray Feaster ◽  
Robert Hirsch ◽  
...  
Biochemistry ◽  
1973 ◽  
Vol 12 (15) ◽  
pp. 2856-2862 ◽  
Author(s):  
Jer-Shung Twu ◽  
Christopher C. Q. Chin ◽  
Finn Wold

Biochemistry ◽  
1974 ◽  
Vol 13 (16) ◽  
pp. 3418-3420 ◽  
Author(s):  
Carl J. Belke ◽  
Christopher C. Q. Chin ◽  
Finn Wold

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

2003 ◽  
Vol 68 (2) ◽  
pp. 77-84 ◽  
Author(s):  
Vladimir Leskovac ◽  
Svetlana Trivic ◽  
Draginja Pericin

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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