Top topic this week
Back to FAQs
Related FAQs
Frequently Asked Question
Questions asked by users might not always be phrased in the clearest way.
Determine the Michaelis constant and maximum velocity of an enzyme catalyzed reaction from the following data. Concentration of substrate [s](moldm ( left.{ }^{-3}right] ) 1.25 2.5 5initial velocity(mmoldm^-3)sec^-1 0.27 0.050 0.833
Accepted Answer
To determine the Michaelis constant (Km) and maximum velocity (Vmax) of an enzyme-catalyzed reaction, you can use the Michaelis-Menten equation and the provided data. Here's how:
1. Plot the data: Plot the initial velocity (v) against the substrate concentration ([S]). This should give you a hyperbolic curve, characteristic of Michaelis-Menten kinetics.
2. Linearize the data: To make the analysis easier, you can linearize the data using a Lineweaver-Burk plot. This involves plotting the reciprocal of the initial velocity (1/v) against the reciprocal of the substrate concentration (1/[S]). This will give you a straight line.
3. Determine the slope and intercept: From the Lineweaver-Burk plot, you can obtain the slope and intercept of the line. The slope of the line is Km/Vmax, and the intercept on the y-axis is 1/Vmax.
4. Calculate Km and Vmax: Using the values of the slope and intercept, you can calculate Km and Vmax. For instance, Vmax = 1/intercept, and Km = (slope
Vmax).
Note: While you provided only three data points, the accuracy of the calculated values would be improved with more data points. Remember that the Michaelis-Menten equation describes the relationship between substrate concentration, initial velocity, and the kinetic parameters Km and Vmax. This relationship is a fundamental concept in enzyme kinetics and plays a vital role in understanding how enzymes function.
Articles you might like