Kinetics of an enzyme reaction in which both the enzyme-substrate complex and the product are unstable or only the product is unstable.
A kinetic analysis of the Michaelis-Menten mechanism has been made for the case in which both the enzyme-substrate complex and the product are unstable or only the product is unstable, either spontaneously or as the result of the addition of a reagent. This analysis allows the derivation of equations which under conditions of limiting enzyme concentration relate the concentration of all of the species to the time. A kinetic data analysis is suggested, which leads to the evaluation of the kinetic parameters involved in the reaction. The analysis is based on the equation which describes the formation of products with time and one's experimental progress curves. We demonstrate the method numerically by computer simulation of the reaction with added experimental errors and experimentally by the use of data from the kinetic study of the action of tyrosinase on dopamine.
Departamento de Química-Física, Universidad de Castilla-La Mancha, Albacete, Spain.
C
C
Garrido-del Solo
F
F
García-Cánovas
B H
BH
Havsteen
E
E
Valero
R
R
Varón
D001487:Basidiomycota / Q000201:enzymology; D002384:Catalysis; D003198:Computer Simulation; D004298:Dopamine / Q000378:metabolism*; D004795:Enzyme Stability / Q000502:physiology*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008956:Models, Chemical; D014442:Monophenol Monooxygenase / Q000737:chemistry* / Q000378:metabolism; D010084:Oxidation-Reduction; D011809:Quinones / Q000378:metabolism; D013379:Substrate Specificity
D011809:Quinones; D014442:Monophenol Monooxygenase; D004298:Dopamine