The original 1913 paper by Michaelis and Menten on enzyme kinetics has been translated and analyzed to reveal its historical significance. The paper describes their study of invertase, an enzyme that catalyzes the hydrolysis of sucrose into fructose and glucose. They demonstrated that the rate of the reaction is proportional to the concentration of the enzyme-substrate complex, as predicted by the Michaelis-Menten equation. Their analysis included initial velocity measurements and fitting of full time course data to the integrated form of the rate equations, accounting for product inhibition. They derived a single global constant, which was not the Michaelis constant (Km), but rather Vmax/Km, the specificity constant times the enzyme concentration (kcat/Km * E0). Michaelis and Menten's work was groundbreaking, as they not only analyzed initial velocity data but also considered the full time course of the reaction. They recognized the importance of product inhibition and used this to derive a comprehensive model of enzyme kinetics. Their analysis revealed an unexpected level of precision and rigor in their original data, which has been overlooked in subsequent decades. The paper also highlights the historical context of their work, including the influence of Victor Henri and the challenges faced in early enzymology research. The translation of the original paper provides insight into the language and terminology used by Michaelis and Menten, as well as the scientific concepts they introduced. The paper also discusses the evolution of enzyme kinetics, including the steady state approximation and the double reciprocal plot. The authors emphasize the importance of Michaelis and Menten's work in the development of modern enzyme kinetics and the need to recognize the significance of their contributions. The paper concludes with a summary of their findings and the implications of their work for the field of biochemistry.The original 1913 paper by Michaelis and Menten on enzyme kinetics has been translated and analyzed to reveal its historical significance. The paper describes their study of invertase, an enzyme that catalyzes the hydrolysis of sucrose into fructose and glucose. They demonstrated that the rate of the reaction is proportional to the concentration of the enzyme-substrate complex, as predicted by the Michaelis-Menten equation. Their analysis included initial velocity measurements and fitting of full time course data to the integrated form of the rate equations, accounting for product inhibition. They derived a single global constant, which was not the Michaelis constant (Km), but rather Vmax/Km, the specificity constant times the enzyme concentration (kcat/Km * E0). Michaelis and Menten's work was groundbreaking, as they not only analyzed initial velocity data but also considered the full time course of the reaction. They recognized the importance of product inhibition and used this to derive a comprehensive model of enzyme kinetics. Their analysis revealed an unexpected level of precision and rigor in their original data, which has been overlooked in subsequent decades. The paper also highlights the historical context of their work, including the influence of Victor Henri and the challenges faced in early enzymology research. The translation of the original paper provides insight into the language and terminology used by Michaelis and Menten, as well as the scientific concepts they introduced. The paper also discusses the evolution of enzyme kinetics, including the steady state approximation and the double reciprocal plot. The authors emphasize the importance of Michaelis and Menten's work in the development of modern enzyme kinetics and the need to recognize the significance of their contributions. The paper concludes with a summary of their findings and the implications of their work for the field of biochemistry.