A guide to the Michaelis–Menten equation: steady state and beyond

The modern definition of enzymology is synonymous with the Michaelis–Menten equation instituted by Leonor Michaelis and Maud Menten. Most textbooks, or chapters within, discussing enzymology start with the derivation of the equation under the assumption of rapid equilibrium (as done by Michaelis–Menten) or steady state (as modified by Briggs and Haldane) conditions to highlight the importance of this equation as the bedrock on which interpretation of enzyme kinetic results is dependent. However, few textbooks or monographs take the effort of placing the equation within its right historical context and discuss the assumptions that have gone into its institution. This guide will dwell on these in substantial detail. Further, this guide will attempt to instil a sense of appreciation for the mathematical curve rectangular hyperbola, its unique attributes and how ubiquitous the curve is in biological systems. To conclude, this guide will discuss the limitations of the equation, and the method it embodies, and trace the journey of how investigators are attempting to move beyond the steady‐state approach and the Michaelis–Menten equation into full progress curve, pre–steady state and single‐turnover kinetic analysis to obtain greater insights into enzyme kinetics and catalysis. The article talks about the primacy of the Michaelis–Menten equation as a framework for the quantitative understanding of enzyme kinetics. It dwells upon the mathematical elegance of and the assumptions that went into framing the equation. Further, it traces the history of the equation and the growth of the field beyond it. The image shows an artistic rendering of the crowded interiors of a cell and the equation dictating how macromolecular interactions of catalytic nature happen.