Kinetic analysis of a Michaelis-Menten mechanism in which the enzyme is unstable.
A kinetic analysis of the Michaelis-Menten mechanism is made for the cases in which the free enzyme, or the enzyme-substrate complex, or both, are unstable, either spontaneously or as a result of the addition of a reagent. The explicit time-course equations of all of the species involved has been derived under conditions of limiting enzyme concentration. The validity of these equations has been checked by using numerical simulations. An experimental design and a kinetic data analysis allowing the evaluation of the parameters and kinetic constants are recommended.
Departamento de Química-Física, Escuela Universitaria Politécnica, Universidad de Castilla-La Mancha, Albacete, Spain.
C
C
Garrido-del Solo
F
F
García-Cánovas
B H
BH
Havsteen
R
R
Varón-Castellanos
D002384:Catalysis; D003198:Computer Simulation; D004791:Enzyme Inhibitors / Q000494:pharmacology; D004795:Enzyme Stability; D004798:Enzymes / Q000378:metabolism*; D007700:Kinetics; D008433:Mathematics; D012044:Regression Analysis
D004791:Enzyme Inhibitors; D004798:Enzymes