Nearly a century after its publication, the 1913 paper by Michaelis and Menten remains a cornerstone in enzymology. The authors translated the original German text into English, providing a modern perspective on their groundbreaking work. They re-analyzed the data using contemporary computational methods, revealing a sophisticated and comprehensive analysis that was previously overlooked. Michaelis and Menten not only derived the Michaelis-Menten equation but also performed a global analysis of their full time course kinetic data, including product inhibition. Their analysis led to the derivation of a single constant, Vmax/Km, which they described as the "specificity constant" times the enzyme concentration (kcat/Km *E0*). This constant, not the Michaelis constant (Km), was derived from their data. The paper also highlights the contributions of Victor Henri, whose work laid the groundwork for enzyme kinetics, and discusses the steady-state approximation introduced by Briggs and Haldane. The authors conclude that the original Michaelis constant, derived from their global analysis, is more significant than the commonly recognized Km, and suggest a revised form of the Michaelis-Menten equation to better reflect this.Nearly a century after its publication, the 1913 paper by Michaelis and Menten remains a cornerstone in enzymology. The authors translated the original German text into English, providing a modern perspective on their groundbreaking work. They re-analyzed the data using contemporary computational methods, revealing a sophisticated and comprehensive analysis that was previously overlooked. Michaelis and Menten not only derived the Michaelis-Menten equation but also performed a global analysis of their full time course kinetic data, including product inhibition. Their analysis led to the derivation of a single constant, Vmax/Km, which they described as the "specificity constant" times the enzyme concentration (kcat/Km *E0*). This constant, not the Michaelis constant (Km), was derived from their data. The paper also highlights the contributions of Victor Henri, whose work laid the groundwork for enzyme kinetics, and discusses the steady-state approximation introduced by Briggs and Haldane. The authors conclude that the original Michaelis constant, derived from their global analysis, is more significant than the commonly recognized Km, and suggest a revised form of the Michaelis-Menten equation to better reflect this.