Bistability and the ordered bimolecular mechanism

1991 ◽  
Vol 69 (9) ◽  
pp. 661-664 ◽  
Author(s):  
K. W. Raymond ◽  
Y. Pocker
Keyword(s):  
Steady State ◽  
Kinetic Constant ◽  
Substrate Inhibition ◽  
Enzymatic Reaction ◽  
Reaction System ◽  
Computational Approach ◽  
Instantaneous Velocity ◽  
Liver Alcohol Dehydrogenase ◽  
Horse Liver ◽  
Bimolecular Mechanism

An equation describing the instantaneous velocity of an ordered bimolecular enzymatic reaction that exhibits inhibition by substrate and product was derived. Using kinetic constant values for horse liver alcohol dehydrogenase, the velocity expression was applied to an open-reaction system. The calculated steady-state surfaces displayed regions of bistability, which further substantiates the link between substrate inhibition and multiple steady states. This general computational approach may be applied to any system that can be described by an instantaneous velocity equation.Key words: bistability, steady state, enzyme kinetics.

scholarly journals Evaluation of rate constants for enzyme-catalysed reactions by the jackknife technique. Application to liver alcohol dehydrogenase

1978 ◽  
Vol 175 (3) ◽  
pp. 969-976 ◽  
Author(s):  
A Cornish-Bowden ◽  
J T Wong
Keyword(s):  
Steady State ◽  
Alcohol Dehydrogenase ◽  
Rate Constants ◽  
Ternary Complex ◽  
Random Order ◽  
Liver Alcohol Dehydrogenase ◽  
Horse Liver ◽  
Regression Techniques ◽  
The Individual ◽  
Oxidation Of Ethanol

Steady-state measurements of enzyme-catalysed reactions are capable of providing more information about the rate constants of the individual steps than is commonly obtained. We have applied a combination of the jackknife and non-linear regression techniques to measurements of the rate of oxidation of ethanol by NAD+, catalysed by alcohol dehydrogenase from horse liver. This has permitted values and confidence intervals to be assigned to the eight rate constants that characterize the binding of ethanol and NAD+ in random order to the enzyme, and to the net rate constant kcat. for the breakdown of the ternary complex.

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