Enzyme Kinetics Analysis: An online tool for analyzing enzyme initial rate data and teaching enzyme kinetics

Abstract

Enzymes are nature's catalysts, mediating chemical processes in living systems. The study of enzyme function and mechanism includes defining the maximum catalytic rate and affinity for substrate/s (among other factors), referred to as enzyme kinetics. Enzyme kinetics is a staple of biochemistry curricula and other disciplines, from molecular and cellular biology to pharmacology. However, because enzyme kinetics involves concepts rarely employed in other areas of biology, it can be challenging for students and researchers. Traditional graphical analysis was replaced by computational analysis, requiring another skill not core to many life sciences curricula. Computational analysis can be time‐consuming and difficult in free software (e.g., R) or require costly software (e.g., GraphPad Prism). We present Enzyme Kinetics Analysis (EKA), a web‐tool to augment teaching and learning and streamline EKA. EKA is an interactive and free tool for analyzing enzyme kinetic data and improving student learning through simulation, built using R and RStudio's ShinyApps. EKA provides kinetic models (Michaelis–Menten, Hill, simple reversible inhibition models, ternary‐complex, and ping‐pong) for users to fit experimental data, providing graphical results and statistics. Additionally, EKA enables users to input parameters and create data and graphs, to visualize changes to parameters (e.g., or number of measurements). This function is designed for students learning kinetics but also for researchers to design experiments. EKA (enzyme-kinetics.shinyapps.io/enzkinet_webpage/) provides a simple, interactive interface for teachers, students, and researchers to explore enzyme kinetics. It gives researchers the ability to design experiments and analyze data without specific software requirements.

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“…The V max value denotes the maximum velocity or speed of the reaction. At this maximum rate, all active sites of the enzyme are saturated with the substrate . To investigate the impact of concentration on the reaction rate of both free and immobilized enzymes, the reaction rate was determined at varying sucrose concentrations.…”

“…At this maximum rate, all active sites of the enzyme are saturated with the substrate. 43 To investigate the impact of concentration on the reaction rate of both free and immobilized enzymes, the reaction rate was determined at varying sucrose concentrations. A Lineweaver–Burk plot was used to compare the performance of the immobilized enzyme to that of the free enzyme.…”