Isotope effects in the binding of NADH to equine liver alcohol dehydrogenase

Biochemistry ◽  
1976 ◽  
Vol 15 (12) ◽  
pp. 2523-2527 ◽  
Author(s):  
Eugene DeJuan ◽  
K. B. Taylor
Keyword(s):  
Alcohol Dehydrogenase ◽  
Isotope Effects ◽  
Liver Alcohol Dehydrogenase

Deuterium isotope effects on initial rates of the liver alcohol dehydrogenase reaction. V

Biochemistry ◽  
1973 ◽  
Vol 12 (23) ◽  
pp. 4802-4805 ◽  
Author(s):  
Karen Bush ◽  
Vernon J. Shiner ◽  
H. R. Mahler
Keyword(s):  
Alcohol Dehydrogenase ◽  
Isotope Effects ◽  
Liver Alcohol Dehydrogenase ◽  
Dehydrogenase Reaction ◽  
Deuterium Isotope Effects

Untersuchungen zur Reaktion der Alkoholdehydrogenasen mit Tritium-markierten Substraten

1968 ◽  
Vol 23 (5) ◽  
pp. 623-628 ◽  
Author(s):  
Dieter Palm ◽  
Tankred Fiedler ◽  
Dorothea Ruhrseitz
Keyword(s):  
Alcohol Dehydrogenase ◽  
Isotope Effect ◽  
Isotope Effects ◽  
Ternary Complexes ◽  
Liver Alcohol Dehydrogenase

[1,1-T]-ethanol,:1,1-T]-propanol and [1,1-T]-butanol exhibit small isotope effects (kH/kT=1.3-1.8) in the liver alcohol dehydrogenase catalyzed reaction NAD® + alcohol ⇌aldehyde +NADH+H®. Presence of semicarbazide (with [1,1-T] -ethanol) or substrat inhibition (with [1,1-T] -butanol, 2.10-2-m.) raises the isotope effect (up to 4.1 at 25 °C) by introducing partial irreversibility to the interconversion step of the ternary complexes. This is in agreement with the Theorell-Chance mechanism as extended by DALZIEL. Thus, isotope effect determinations confirm both, the presence of ternary complexes and their kinetic insignificance for lower aliphatic substrates.The results are markedly different from analogous kinetics with the yeast enzyme.

Hydride Transfer in Liver Alcohol Dehydrogenase:  Quantum Dynamics, Kinetic Isotope Effects, and Role of Enzyme Motion

2001 ◽  
Vol 123 (45) ◽  
pp. 11262-11272 ◽  
Author(s):  
Salomon R. Billeter ◽  
Simon P. Webb ◽  
Pratul K. Agarwal ◽  
Tzvetelin Iordanov ◽  
Sharon Hammes-Schiffer
Keyword(s):  
Alcohol Dehydrogenase ◽  
Quantum Dynamics ◽  
Isotope Effects ◽  
Hydride Transfer ◽  
Kinetic Isotope Effects ◽  
Liver Alcohol Dehydrogenase ◽  
Kinetic Isotope

Secondary deuterium and nitrogen-15 isotope effects in enzyme-catalyzed reactions. Chemical mechanism of liver alcohol dehydrogenase

Biochemistry ◽  
1981 ◽  
Vol 20 (7) ◽  
pp. 1817-1825 ◽  
Author(s):  
Paul F. Cook ◽  
Norman J. Oppenheimer ◽  
W. W. Cleland
Keyword(s):  
Alcohol Dehydrogenase ◽  
Isotope Effects ◽  
Chemical Mechanism ◽  
Liver Alcohol Dehydrogenase ◽  
Catalyzed Reactions ◽  
Enzyme Catalyzed Reactions

EXAFS INVESTIGATION OF THE STRUCTURAL SITE OF LIVER ALCOHOL DEHYDROGENASE

1986 ◽  
Vol 47 (C8) ◽  
pp. C8-1165-C8-1168
Author(s):  
M. ZEPPEZAUER ◽  
C. HAAS ◽  
W. MARET ◽  
C. HERMES ◽  
R. F. PETTIFER
Keyword(s):  
Alcohol Dehydrogenase ◽  
Liver Alcohol Dehydrogenase ◽  
Structural Site

scholarly journals Binding of substrate in a ternary complex of horse liver alcohol dehydrogenase.

1982 ◽  
Vol 257 (23) ◽  
pp. 14349-14358 ◽  
Author(s):  
H Eklund ◽  
B V Plapp ◽  
J P Samama ◽  
C I Brändén
Keyword(s):  
Alcohol Dehydrogenase ◽  
Ternary Complex ◽  
Horse Liver Alcohol Dehydrogenase ◽  
Liver Alcohol Dehydrogenase ◽  
Horse Liver
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