Steady state kinetics of an enzyme reaction with one substrate and one modifier

1968 ◽  
Vol 30 (2) ◽  
pp. 253-277 ◽  
Author(s):  
Wayne P. London
Keyword(s):  
Steady State ◽  
Enzyme Reaction ◽  
Steady State Kinetics ◽  
Kinetics Of

scholarly journals The steady-state kinetics of isotope exchange for one substrate–one product enzymic reactions

1973 ◽  
Vol 135 (4) ◽  
pp. 861-866 ◽  
Author(s):  
Ivan G. Darvey
Keyword(s):  
Steady State ◽  
Isotope Exchange ◽  
Kinetic Equations ◽  
Enzyme Reaction ◽  
Radioactive Material ◽  
First Order ◽  
Steady State Kinetics ◽  
The One ◽  
Allosteric Mechanisms ◽  
Kinetics Of

Steady-state kinetic equations for isotope exchange are derived for a number of one substrate–one product enzymic mechanisms in which two molecules of substrate or product can be combined with an enzyme molecule at the one time (e.g. allosteric mechanisms). The usual assumption, that the radioactive material is distributed among the substrate and product components according to a first-order law, is not valid. One can recognize whether isotope-exchange kinetics of an enzyme reaction follows first-order behaviour by using various initial concentrations of the labelled substance added to a mixture.

scholarly journals Theoretical approach to the steady-state kinetics of a bi-substrate acyl-transfer enzyme reaction that follows a hydrolysable-acyl-enzyme-based mechanism. Application to the study of lysophosphatidylcholine:lysophosphatidylcholine acyltransferase from rabbit lung

1990 ◽  
Vol 266 (1) ◽  
pp. 47-53 ◽  
Author(s):  
J Martín ◽  
J Pérez-Gil ◽  
C Acebal ◽  
R Arche
Keyword(s):  
Steady State ◽  
Kinetic Equations ◽  
Enzyme Reaction ◽  
Great Accuracy ◽  
Acyl Transfer ◽  
Rabbit Lung ◽  
Steady State Kinetics ◽  
Kinetic Pattern ◽  
Covalent Intermediate ◽  
Kinetics Of

A kinetic model is proposed for catalysis by an enzyme that has several special characteristics: (i) it catalyses an acyl-transfer bi-substrate reaction between two identical molecules of substrate, (ii) the substrate is an amphiphilic molecule that can be present in two physical forms, namely monomers and micelles, and (iii) the reaction progresses through an acyl-enzyme-based mechanism and the covalent intermediate can react also with water to yield a secondary hydrolytic reaction. The theoretical kinetic equations for both reactions were deduced according to steady-state assumptions and the theoretical plots were predicted. The experimental kinetics of lysophosphatidylcholine:lysophosphatidylcholine acyltransferase from rabbit lung fitted the proposed equations with great accuracy. Also, kinetics of inhibition by products behaved as expected. It was concluded that the competition between two nucleophiles for the covalent acyl-enzyme intermediate, and not a different enzyme action depending on the physical state of the substrate, is responsible for the differences in kinetic pattern for the two activities of the enzyme. This conclusion, together with the fact that the kinetic equation for the transacylation is quadratic, generates a ‘hysteretic’ pattern that can provide the basis of self-regulatory properties for enzymes to which this model could be applied.

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

Steady-state kinetics of bezafibrate retard in hyperlipidemic geriatric patients

1988 ◽  
Vol 66 (6) ◽  
pp. 250-256 ◽  
Author(s):  
G. Neugebauer ◽  
D. Platt ◽  
T. Vömel ◽  
W. Lösch
Keyword(s):  
Steady State ◽  
Geriatric Patients ◽  
Steady State Kinetics ◽  
Kinetics Of
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