Multiple Intermediates in Steady-state Enzyme Kinetics. IV. The Steady State Kinetics of Isotopic Exchange in Enzyme-catalyzed Reactions

1962 ◽  
Vol 84 (23) ◽  
pp. 4381-4384 ◽  
Author(s):  
Robert A. Alberty ◽  
Victor. Bloomfield ◽  
Leonard. Peller ◽  
Edward L. King
Keyword(s):  
Steady State ◽  
Enzyme Kinetics ◽  
Isotopic Exchange ◽  
Steady State Kinetics ◽  
Catalyzed Reactions ◽  
Enzyme Catalyzed Reactions ◽  
Kinetics Of

Steady-State Kinetics of Enzyme Reactions in the Presence of Added Nucleophiles

1972 ◽  
Vol 50 (12) ◽  
pp. 1334-1359 ◽  
Author(s):  
Irwin Hinberg ◽  
Keith J. Laidler
Keyword(s):  
Specific Binding ◽  
Specific Binding Sites ◽  
Steady State Kinetics ◽  
Special Cases ◽  
Kinetics Of Formation ◽  
Catalyzed Reactions ◽  
Enzyme Catalyzed Reactions ◽  
Concentration Graphs ◽  
Kinetics Of ◽  
Hydrolysis Of

Many enzyme-catalyzed reactions, such as hydrolyses, give rise to two products P1 and P2 which are formed in different reaction steps. The second product P2 is frequently formed by hydrolysis of an intermediate such as an acyl-enzyme or a phosphoryl-enzyme. An alternative nucleophile N introduced into the system forms an additional product P3. The present paper is concerned with the kinetics of formation of P1, P2, and P3 in the presence of added nucleophiles. A number of alternative mechanisms are considered, and equations are derived for the rates of formation of the three products, and the Michaelis constant, as functions of nucleophile concentration. Graphs are presented showing the variations of these parameters with the concentration of N, for a variety of special cases. Special attention is given to the possibility of specific binding sites for the water and the nucleophile molecules.The data for a number of enzyme systems are discussed with reference to the treatment. For reactions catalyzed by alkaline phosphatase it is concluded that only one mechanism (mechanism VI) is consistent with the results.

Computer-based derivation of rate equations for enzyme-catalyzed reactions. I. Effects of modifiers on kinetics of multireactant systems

1969 ◽  
Vol 47 (9) ◽  
pp. 889-894 ◽  
Author(s):  
Arthur R. Schulz ◽  
Donald D. Fisher
Keyword(s):  
Steady State ◽  
Reaction Mechanism ◽  
Rate Equations ◽  
Connection Matrix ◽  
Computer Based ◽  
Catalyzed Reactions ◽  
Enzyme Catalyzed Reactions ◽  
Kinetics Of

A computer-based method for the derivation of rate equations of enzyme-catalyzed reactions under steady-state assumptions is presented. This method is based on the description of the reaction mechanism in terms of a connection matrix. The utility of the method is demonstrated by applying it to complete the derivation of rate equations of multireactant enzymic mechanisms with modifiers as discussed by Henderson.

Pre-steady-state kinetics of Escherichia coli aspartate aminotransferase catalyzed reactions and thermodynamic aspects of its substrate specificity

Biochemistry ◽  
1990 ◽  
Vol 29 (23) ◽  
pp. 5469-5476 ◽  
Author(s):  
Seiki Kuramitsu ◽  
Keitaro Hiromi ◽  
Hideyuki Hayashi ◽  
Yoshimasa Morino ◽  
Hiroyuki Kagamiyama
Keyword(s):  
Escherichia Coli ◽  
Steady State ◽  
Substrate Specificity ◽  
Aspartate Aminotransferase ◽  
Steady State Kinetics ◽  
Catalyzed Reactions ◽  
Kinetics Of

Steady-state kinetics of valproic acid in epileptic patients

1978 ◽  
Vol 24 (3) ◽  
pp. 324-332 ◽  
Author(s):  
J. Bruni ◽  
B. J. Wilder ◽  
L. J. Willmore ◽  
R. J. Perchalski ◽  
H. J. Villarreal
Keyword(s):  
Valproic Acid ◽  
Steady State ◽  
Steady State Kinetics ◽  
Epileptic Patients ◽  
Kinetics Of
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