Enzyme · 2017 · 59 citations · 0 references
Life SciencesBiochemistryChemical KineticsEnzyme MechanismEnzymologyChemical Kinetics ModelingEnzyme BiophysicsEnzyme InhibitionEnzyme KineticsKinetic ModelingMichaelis-menten KineticsEnzyme Inhibition KineticsEnzyme Kinetic AnalysisEnzyme Kinetic ModelsEnzyme Reaction KineticsInhibition ConstantsInhibition KineticsMichaelis ConstantMichaelis-menten Analysis
A weighted nonlinear least-squares curve-fitting program, implemented in compiled BASIC for the IBM-PC is described to estimate the parameters of enzyme kinetics obeying Michaelis-Menten kinetics and seven inhibition models. The effects of the inhibitor on the maximal velocity (Vm) and the Michaelis-Menten constant (Km) are used to select automatically the most plausible model of inhibition and to calculate initial estimates of parameters. The program is used to demonstrate that the inhibition of carbamyl-phenylalanine hydrolase by the product phenylalanine is consistent with the pure mixed noncompetitive model.