Steady-state kinetics and transient studies of substrate and coenzyme analogue binding to clostridial glutamate dehydrogenase (GDH) during oxidative deamination

1994 ◽  
Vol 22 (3) ◽  
pp. 319S-319S ◽  
Author(s):  
LUIZ A. BASSO ◽  
PAUL C. ENGEL ◽  
ADRIAN R. WALMSLEY
Keyword(s):  
Steady State ◽  
Glutamate Dehydrogenase ◽  
Oxidative Deamination ◽  
Steady State Kinetics

scholarly journals A steady-state random-order mechanism for the oxidative deamination of norvaline by glutamate dehydrogenase

1983 ◽  
Vol 211 (1) ◽  
pp. 99-107 ◽  
Author(s):  
C LiMuti ◽  
J E Bell
Keyword(s):  
Steady State ◽  
Glutamate Dehydrogenase ◽  
Dissociation Constants ◽  
Random Order ◽  
Kinetic Mechanism ◽  
Order Model ◽  
Oxidative Deamination ◽  
Steady State Kinetics ◽  
Rapid Equilibrium ◽  
Good Agreement

The kinetic mechanism of glutamate dehydrogenase with the monocarboxylic substrate norvaline was examined by using initial-rate steady-state kinetics and inhibition kinetics. To a first approximation the reaction mechanism can be described as a rapid-equilibrium random-order one. Binding synergism between the monocarboxylic substrate and coenzyme is not observed. Dissociation constants for NAD+ and 2-oxoglutarate calculated from the kinetic data assuming a rapid-equilibrium random-order model are in good agreement with independently obtained estimates. Lineweaver-Burk plots with varied norvaline concentration are not strictly linear, and it is concluded that a steady-state random-order model more accurately reflects the observed kinetics with norvaline as substrate.

Effect of ammonia on the glutamate dehydrogenase catalyzed oxidative deamination of L-glutamate. The steady state

Biochemistry ◽  
1979 ◽  
Vol 18 (26) ◽  
pp. 5924-5928 ◽  
Author(s):  
Allister Brown ◽  
Alan H. Colen ◽  
Harvey F. Fisher
Keyword(s):  
Steady State ◽  
Glutamate Dehydrogenase ◽  
Oxidative Deamination
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