Experimental designs for estimating the parameters of the Michaelis-Menten equation from progress curves of enzyme-catalyzed reactions.
When the progress curve for an enzyme catalysed reaction follows the integrated Michaelis-Menten equation, the maximum velocity and Michaelis constant can be determined from a single such curve. In this paper, an experimental design for collecting the data is proposed which is close to optimum in the sense that it produces the smallest standard error in the estimate of the Michaelis constant. This design involves choosing an initial substrate concentration which is approx. two or three times the value of the Michaelis constant.
Duggleby
R G
RG
Department of Biochemistry, University of Queensland, Australia.
Clarke
R B
RB
D002384:Catalysis; D003625:Data Collection / Q000379:methods; D004798:Enzymes / Q000378:metabolism*; D007700:Kinetics; D008433:Mathematics; D008956:Models, Chemical; D010728:Phosphoenolpyruvate / Q000378:metabolism; D011770:Pyruvate Kinase / Q000378:metabolism; D012107:Research Design
D004798:Enzymes; D010728:Phosphoenolpyruvate; D011770:Pyruvate Kinase