Comparative study of yeast alcohol Dehydrogenase Isozyme properties: Theoretical data and experimental results

1993 ◽  
Keyword(s):  
Alcohol Dehydrogenase ◽  
Comparative Study ◽  
Theoretical Data ◽  
Experimental Results ◽  
Yeast Alcohol Dehydrogenase ◽  
Dehydrogenase Isozyme

Comparative Study Between Geant4, MCNP6 and Experimental Results Against Gamma Radiation Comes from a Cobalt-60 Source

2020 ◽  
Vol 75 (5) ◽  
pp. 507-511
Author(s):  
Y. El-Ouardi ◽  
A. Dadouch ◽  
A. Aknouch ◽  
M. Mouhib ◽  
A. Maghnouj ◽  
...  
Keyword(s):  
Comparative Study ◽  
Gamma Radiation ◽  
Experimental Results

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

Reptilian alcohol dehydrogenase: Isozyme divergence among submammalian vertebrates

1992 ◽  
Vol 11 (4) ◽  
pp. 412-412
Author(s):  
Lars Hjelmqvist ◽  
Jawed Shafqat ◽  
Hans Jörnvall
Keyword(s):  
Alcohol Dehydrogenase ◽  
Dehydrogenase Isozyme

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.

scholarly journals Binding of coenzymes to yeast alcohol dehydrogenase

2010 ◽  
Vol 75 (2) ◽  
pp. 185-194 ◽  
Author(s):  
Vladimir Leskovac ◽  
Svetlana Trivic ◽  
Draginja Pericin ◽  
Mira Popovic ◽  
Julijan Kandrac
Keyword(s):  
Alcohol Dehydrogenase ◽  
Equilibrium Constants ◽  
Point Mutations ◽  
Free Energies ◽  
Wild Type ◽  
Wild Type Enzyme ◽  
Mutant Type ◽  
Yeast Alcohol Dehydrogenase ◽  
Internal Equilibrium ◽  
Individual Reaction

In this work, the binding of coenzymes to yeast alcohol dehydrogenase (EC 1.1.1.1) were investigated. The main criterions were the change in the standard free energies for individual reaction steps, the internal equilibrium constants and the overall changes in the reaction free energies. The calculations were performed for the wild type enzyme at pH 6-9 and for 15 different mutant type enzymes, with single or double point mutations, at pH 7.3. The abundance of theoretical and experimental data enabled the binding of coenzymes to enzyme to be assessed in depth.

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