A double-reciprocal plot for a typical Michaelis-Menten enzyme and an allosteric enzyme that have the same V max and K M is to be drawn. The double-reciprocal plot for the same allosteric enzyme in the presence of allosteric inhibitor and allosteric stimulator is to be drawn. Concept introduction: The enzyme which is able to do the conformational changes if an effector gets attached to it is known as allosteric enzyme. This enzyme responds to the environmental signal which works as an effector.

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Chapter 10, Problem 15P

Interpretation Introduction

Interpretation:

A double-reciprocal plot for a typical Michaelis-Menten enzyme and an allosteric enzyme that have the same Vmax and KM is to be drawn. The double-reciprocal plot for the same allosteric enzyme in the presence of allosteric inhibitor and allosteric stimulator is to be drawn.

Concept introduction:

The enzyme which is able to do the conformational changes if an effector gets attached to it is known as allosteric enzyme. This enzyme responds to the environmental signal which works as an effector.

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not true about the Michaelis-Menten equation? The equation that gives the rate, v, of an the substrate concentration [S] is the Michaelis-Menten equation = Vmax[S]/(Km + [S]), where V, enzyme-catalyzed reaction for all values of max and Km are constants. Which of the following is a) for [S] << Km, V = Vmax applies to most enzymes, but allosteric enzymes have different kinetics when [S] = Km, then v = Vmax/2 gives the rate when the enzyme concentration, temperature, pH, and ionic strength are constant for very high values of [S], v approaches Vmax e) Which is correct about the constant Km in the Michaelis-Menten equation? also called the catalytic constant or turnover number equal to the number of product molecules produced per unit time when the enzyme is saturated with substrate it is the constant in the first order rate equation v = k[A] it is the constant in the second order rate equation v = equal to the substrate concentration at which the velocity or rate of a reaction is ½ the…