scholarly journals The thiol groups of yeast alcohol dehydrogenase

1964 ◽  
Vol 90 (3) ◽  
pp. 532-539 ◽  
Author(s):  
EP Whitehead ◽  
BR Rabin
Keyword(s):  
Alcohol Dehydrogenase ◽  
Thiol Groups ◽  
Yeast Alcohol Dehydrogenase

scholarly journals Role of the essential thiol groups of yeast alcohol dehydrogenase

1972 ◽  
Vol 126 (1) ◽  
pp. 133-138 ◽  
Author(s):  
F. M. Dickinson
Keyword(s):  
Alcohol Dehydrogenase ◽  
Dissociation Constant ◽  
Binding Capacity ◽  
Ternary Complexes ◽  
Native Enzyme ◽  
Thiol Groups ◽  
Yeast Alcohol Dehydrogenase

1. Yeast alcohol dehydrogenase inactivated by reaction with iodoacetamide retains 85% of the original NADH-binding capacity as measured under conditions of saturating coenzyme concentration. 2. The dissociation constant of the enzyme–NADH complex is unaffected by inactivation of the enzyme with iodoacetamide, and the affinity of the enzyme for NAD+ and pyridine-3-aldehyde–adenine dinucleotide (PAAD+) appears to be similarly unaffected. 3. Enzyme inactivated with iodoacetamide has lost the ability to form normal ternary complexes of the type enzyme–NADH–acetamide and enzyme–PAAD+–hydroxylamine that are characteristic of the native enzyme.

scholarly journals Evidence for a histidine and a cysteine residue in the substrate-binding site of yeast alcohol dehydrogenase

1975 ◽  
Vol 145 (3) ◽  
pp. 581-590 ◽  
Author(s):  
V Leskovac ◽  
D Pavkov-Peričin
Keyword(s):  
Alcohol Dehydrogenase ◽  
Binding Site ◽  
Ternary Complex ◽  
Substrate Binding ◽  
Cysteine Residue ◽  
Histidine Residue ◽  
Thiol Groups ◽  
Substrate Binding Site ◽  
Yeast Alcohol Dehydrogenase ◽  
Diethyl Pyrocarbonate

1. Yeast alcohol dehydrogenase (EC 1.1.1.1) is inhibited by stoicheiometric concentrations of diethyl pyrocarbonate. The inhibition is due to the acylation of a single histidine residue/monomer (mol.wt. 36000). 2. Alcohol dehydrogenase is also inhibited by stoicheiometric amounts of 5,5′-dithiobis-(2-nitrobenzoate), owing to the modification of a single cysteine residue/monomer. 3. Native alcohol dehydrogenase binds two molecules of reduced coenzyme/molecule of enzyme (mol.wt. 144000). 4. Modification of a single histidine residue/monomer by treatment with diethyl pyrocarbonate prevents the binding of acetamide in the ternary complex, enzyme-NADH-acetamede, but does not prevent the binding of NADH to the enzyme. 5. Modification of a single cysteine residue/monomer does not prevent the binding of acetamide to the ternary complex. After the modification of two thiol groups/monomer by treatment with 5,5′-dithiobis-(2-nitrobenzoate), the capacity of enzyme to bind coenzyme in the ternary complex was virtually abolished. 6. From the results presented in this paper we conclude that at least one histidine and one cysteine residue are closely associated in the substrate-binding site of 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.

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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