Why do enzymes saturate? Michaelis-Menten kinetics show reaction rate climbing with substrate then plateauing at Vmax — and how an inhibitor sabotages the curve.
Enzyme Kinetics (Michaelis-Menten)Live
reaction rate vs substrate
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Michaelis-Menten kinetics describe how reaction rate rises with substrate and saturates at Vmax. Km is the substrate concentration giving half-maximal rate — a measure of enzyme affinity. A competitive inhibitor raises the apparent Km without changing Vmax, seen as a shift in the double-reciprocal Lineweaver-Burk line.
Reading this result: With Km 5, the rate hits half of Vmax (100) at [S]=5; pushing substrate well past Km barely raises v as the curve flattens toward saturation.
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How it works
The Michaelis-Menten equation v = Vmax·[S]/(Km+[S]) describes enzyme-catalyzed reaction rates. Km, the substrate concentration for half-maximal rate, gauges enzyme affinity. A competitive inhibitor raises the apparent Km while leaving Vmax unchanged — a signature seen clearly in the linearized Lineweaver-Burk double-reciprocal plot.
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