Enzyme kinetics: the whole picture reveals hidden meanings

• DOI: 10.1111/febs.13275
• Publication Date: 2015-03-24T21:39:59Z
• Authors: Maria F. Pinto; Berta N. Estevinho; Rosa Crespo; Fernando A. Rocha; Ana M. Damas; Pedro M. Martins
• Keywords: Formalism (music); Enzyme Kinetics; Michaelis–Menten kinetics; Enzyme Inhibition; Enzyme Catalysis

The methodology adopted by Michaelis and Menten in 1913 is still routinely used to characterize the catalytic power selectivity of enzymes. These kinetic measurements must be performed soon after purified enzyme mixed with a large excess substrate. Other time scales solution compositions are no less physiologically relevant, but fall outside range applicability classical formalism. Here we show that complete picture an enzyme's mode function critically obscured limited scope conventional analysis, even simplest case single active site without inhibition. This now unveiled mathematically closed form remains valid over reaction for all combinations enzyme/substrate concentrations rate constants. Algebraic simplicity maintained new formalism when stationary phases considered. By achieving this century-old objective, otherwise hidden role reversible binding step revealed atypical profiles explained. Most singular behaviors identified critical region conditions coincide typical cell conditions. Because it not covered Michaelis-Menten model, has been missed until low- high-throughput screenings drugs. New possibilities therefore raised novel once-promising inhibitors therapeutically target