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Bookmark or Share- Michaelis-Menten Equation | ChemTalkThe Michaelis-Menten Equation describes the relationship between the rate of an enzyme-catalyzed reaction and the concentration of the substrate. It was named after the scientists Leonor Michaelis and Maud Menten, who developed it in 1913.
- Leonor Michaelis and Maud Leonora Menten - Science History InstituteLeonor Michaelis and Maud Leonora Menten. In 1912 Michaelis and Menten published their seminal work on enzymes—almost all of which are proteins. Their research cast new light on these complex compounds that make possible the chemical reactions of life. about SCIENTIFIC BIOGRAPHIES.
- Michaelis–Menten kinetics - WikipediaIn biochemistry, Michaelis–Menten kinetics, named after Leonor Michaelis and Maud Menten, is the simplest case of enzyme kinetics, applied to enzyme-catalysed reactions of one substrate and one product.
- A guide to the Michaelis–Menten equation: steady state and beyond ...Abstract. 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 ...
- Steady states and the Michaelis Menten equationSteady states and the Michaelis Menten equation. Continue your exploration of enzyme kinetics with a focus on Michaelis-Menten kinetics and the steady-state assumption. Explore how enzymes speed up reactions, the role of substrate concentrations, and the importance of the Michaelis constant.
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