title: Determination of the maximum velocity and Michaelis constant of enzymes by a fixed-point method which avoids the necessity to measure initial rates.
abstract: Measuring the initial velocity is difficult in some enzyme assays where a significant fraction of the substrate is consumed. Here a solution to this problem is proposed; the time to produce a fixed amount of reaction product is measured. This time is inversely proportional to the initial velocity, and is related to the maximum velocity and Michaelis constant by a simple equation and linear plot. The method is illustrated using the reaction catalysed by pyruvate kinase.
authors.affiliation: Department of Biochemistry, University of Queensland, Australia.
authors.forename: R G
authors.initials: RG
authors.lastname: Duggleby
mesh_terms: D004798:Enzymes / Q000378:metabolism*; D007700:Kinetics; D008956:Models, Chemical; D011770:Pyruvate Kinase / Q000378:metabolism
chemical_list: D004798:Enzymes; D011770:Pyruvate Kinase