A century of enzyme kinetic analysis, 1913 to 2013. Issue 17 (11th July 2013)

• Record Type: Journal Article
• Authors: Johnson, Kenneth A.
• Is Part Of: FEBS letters. Volume 587:Issue 17(2013)
• Page Start: 2753
• Page End: 2766
• Publication Date: 2013-07-11
• Subjects: Michaelis–Menten -- Enzyme kinetics -- Global data fitting -- Computer simulation -- EPSP -- 5-enoylpyruvoylshikimate-3-phosphate -- HIVRT -- HIV reverse transciptase -- MDCC -- 7-diethylamino-3-[([(2-maleimidyl)ethyl]amino)carbonyl]coumarin -- S3P -- shikimate 3-phosphate; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1016/j.febslet.2013.07.012
• Languages: English
• ISSNs: 0014-5793

Abstract

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.