Effect of Pressure on a Heavy-Atom Isotope Effect of Yeast Alcohol Dehydrogenase

2006 ◽  
Vol 128 (6) ◽  
pp. 1868-1872 ◽  
Author(s):  
Hyun Park ◽  
Gary G. Girdaukas ◽  
Dexter B. Northrop
Keyword(s):  
Alcohol Dehydrogenase ◽  
Isotope Effect ◽  
Heavy Atom ◽  
Effect Of Pressure ◽  
Yeast Alcohol Dehydrogenase

Untersuchungen zur Reaktion der Alkoholdehydrogenase mit Tritium-markierten Substraten

1966 ◽  
Vol 21 (6) ◽  
pp. 540-546 ◽  
Author(s):  
Dieter Palm
Keyword(s):  
Alcohol Dehydrogenase ◽  
Temperature Dependence ◽  
Isotope Effect ◽  
Substrate Binding ◽  
Isotope Effects ◽  
Direct Interaction ◽  
Enzyme Complex ◽  
Temperature Range ◽  
Yeast Alcohol Dehydrogenase ◽  
Rate Controlling Step

Unexpectedly, the isotope effect of ethanol-1-Τ as a substrate of yeast alcohol dehydrogenase, increases with rising temperature from kH/kT = 3.2 at 5 —15°C to 3.8—4.7 at 20 —35 °C. This suggests a change of the rate controlling step as proposed by MÜLLER-HILL and WALLENFELS, who investigated the temperature dependence of the activation energies in this temperature range. A comparison of the affinities of propanol and butanol with the isotope effects of the corresponding tritium labelled compounds (propanol-1-Τ 6.7 at 25 °C, butanol-1-Τ 6.8 at 25 °C) supports the proposal, that during substrate binding, there must be a direct interaction between the enzyme complex and hydrogen which is removed in the reaction. These influences are less pronounced for the ethanol homologues which are bound less tightly to the enzyme. Therefore the H transfering step proper gives a greater contribution to the overall experimental isotope effect.

Effect of Pressure on Nucleotide Binding to Yeast Alcohol Dehydrogenase

2005 ◽  
Vol 12 (5) ◽  
pp. 495-497 ◽  
Author(s):  
Gene Kidman ◽  
Dexter Northrop
Keyword(s):  
Alcohol Dehydrogenase ◽  
Nucleotide Binding ◽  
Effect Of Pressure ◽  
Yeast Alcohol Dehydrogenase

Untersuchungen zur Reaktion der Alkoholdehydrogenase mit Tritium -markierten Substraten

1966 ◽  
Vol 21 (6) ◽  
pp. 547-551 ◽  
Author(s):  
Dieter Palm
Keyword(s):  
Alcohol Dehydrogenase ◽  
Isotope Effect ◽  
Isotope Fractionation ◽  
Kinetic Isotope Effect ◽  
Retention Volume ◽  
Deae Cellulose ◽  
Yeast Alcohol Dehydrogenase ◽  
Kinetic Isotope ◽  
Direct Indication ◽  
Rate Controlling Step

The temperature dependence of the kinetic isotope effect of NADH-T in the acetaldehyde reduction by yeast alcohol dehydrogenase showed a discontinuity which can be explained by a change of the rate controlling step. The magnitude of the isotope effect is largely dependent on the nature of the unlabelled aldehyde and increases in the order acetaldehyde, propionaldehyde, butyraldehyde. This is a direct indication that the second substrate influences the nature of the H-transfer from NADH. During substrate binding the aldehyde causes an effect on the transferable H of NADH. This effect is less pronounced for the less effective substrates propionaldehyde and butyraldehyde. Comparing the homologue aldehydes the small size of the isotope effect gives an indication that acetaldehyde is the natural substrate of yeast alcohol dehydrogenase.The purification of NADH-T on DEAE-Cellulose is connected with isotope fractionation which amounts to 0.4 — 1.1% of retention volume.

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

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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