title: A century of enzyme kinetic analysis, 1913 to 2013.
abstract: This review traces the history and logical progression of methods for quantitative analysis of enzyme kinetics from the 1913 Michaelis and Menten paper to the application of modern computational methods today. Following a brief review of methods for fitting steady state kinetic data, modern methods are highlighted for fitting full progress curve kinetics based upon numerical integration of rate equations, including a re-analysis of the original Michaelis-Menten full time course kinetic data. Finally, several illustrations of modern transient state kinetic methods of analysis are shown which enable the elucidation of reactions occurring at the active sites of enzymes in order to relate structure and function.
authors.affiliation: Institute for Cell and Molecular Biology, Department of Chemistry and Biochemistry, University of Texas at Austin, 2500 Speedway, MBB 3.122, Austin, TX 78735, USA. kajohnson@mail.utexas.edu
authors.forename: Kenneth A
authors.initials: KA
authors.lastname: Johnson
mesh_terms: D000465:Algorithms; D003198:Computer Simulation; D003627:Data Interpretation, Statistical; D004798:Enzymes / Q000737:chemistry* / Q000266:history; D049673:History, 20th Century; D049674:History, 21st Century; D007700:Kinetics; D008956:Models, Chemical; D011487:Protein Conformation
chemical_list: D004798:Enzymes
keywords: 5-enoylpyruvoylshikimate-3-phosphate; 7-diethylamino-3-[([(2-maleimidyl)ethyl]amino)carbonyl]coumarin; Computer simulation; EPSP; Enzyme kinetics; Global data fitting; HIV reverse transciptase; HIVRT; MDCC; Michaelis–Menten; S3P; shikimate 3-phosphate