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Write the significance of Km and Vmax in enzyme activity

Enzymes are specialized biological molecules that play a critical role in accelerating biochemical reactions. They function by lowering the activation energy required for substrate conversion into products. The study of enzyme kinetics provides a quantitative understanding of how efficiently enzymes work under various conditions. Two of the most important parameters that describe enzyme activity are the  Michaelis constant (Km)  and the  maximum reaction velocity (Vmax),  both derived from the  Michaelis-Menten equation.  These parameters help in understanding enzyme efficiency, substrate binding strength, catalytic turnover, metabolic regulation and response to inhibitors. 1. Significance of Km (Michaelis Constant) The Michaelis constant (Km) is a fundamental concept in enzyme kinetics that represents the substrate concentration at which an enzyme-catalyzed reaction proceeds at  half of its maximum velocity (Vmax/2).  It is a crucial indicator of...

What is Lineweaver Burk plot? Derive Lineweaver Burk equation from Michaelis-Menten equation

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The Lineweaver-Burk plot is a graphical method used in  enzyme kinetics  to analyze enzyme function and the effects of various factors. It was introduced by  Hans Lineweaver  and  Dean Burk  in  1934  as a method to simplify the interpretation of enzyme kinetics data. This plot is derived from the  Michaelis-Menten equation,  which was first formulated in  1913  by  Leonor Michaelis  and  Maud Menten.  Their work provided a mathematical model to describe the relationship between  enzyme activity  and  substrate concentration.  The equation they developed was based on experimental observations and a mathematical analysis of enzyme-catalyzed reactions. However, the Michaelis-Menten equation produces a  non-linear hyperbolic curve,  making it difficult to determine key kinetic parameters like  Vmax  (maximum reaction velocity) and  Km  (Michaelis constant, which...

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