The speed of a reaction is increased when the amount of reactants reaching the activation energy (energy barrier) is increased. This can be done via two ways: increasing temperature or adding a catalyst. Increasing temperature will add kinetic energy to the reactant and increase the amount of reactants reaching the energy barrier. Adding a catalyst will decrease the activation energy and, subsequently, increase the amount of reactants reaching the energy barrier.

Since the temperature is kept relatively constant in the human body (due to homeostasis), the most common way human body increases the speed of a reaction is by using catalysts. Biological catalysts are called enzymes and they are usually named with the suffix -ase. The only molecule that is an enzyme in this question is DNAase, which catalyzes the hydrolysis of phosphodiester bonds in the backbone of DNA.

ATP provides energy for active reactions but it cannot speed up the reaction. Histones are proteins found in nucleus that are involved in DNA packaging. They are irrelevant to this question.

To solve this problem we need to use the Michaelis-Menten equation.

where is reaction rate, is maximum reaction rate, is substrate concentration, and is the Michaelis constant. If we plug in the given values we get a reaction rate of

Note that the Michaelis-Menten equation implies that the will never exceed . Regardless of how high the substrate concentration is, the reaction rate will approach but will never equal or exceed it. You can try this by substituting very high values for substrate concentration. The will get very close to 0.2 () but will never equal or exceed it.

An adiabatic reaction is characterized as a reaction that neither gains nor loses net heat. This means that the process of converting the reactants to products does not alter the heat in the system (reaction) or the surroundings; therefore, both the heat inside and outside the system will be constant.

To solve this problem we need to use the Michaelis-Menten equation.

where is reaction rate, is maximum reaction rate, is substrate concentration, and is the Michaelis constant. If we plug in the given values we get a reaction rate of

Note that the Michaelis-Menten equation implies that the will never exceed . Regardless of how high the substrate concentration is, the reaction rate will approach but will never equal or exceed it. You can try this by substituting very high values for substrate concentration. The will get very close to 0.2 () but will never equal or exceed it.

An adiabatic reaction is characterized as a reaction that neither gains nor loses net heat. This means that the process of converting the reactants to products does not alter the heat in the system (reaction) or the surroundings; therefore, both the heat inside and outside the system will be constant.

The speed of a reaction is increased when the amount of reactants reaching the activation energy (energy barrier) is increased. This can be done via two ways: increasing temperature or adding a catalyst. Increasing temperature will add kinetic energy to the reactant and increase the amount of reactants reaching the energy barrier. Adding a catalyst will decrease the activation energy and, subsequently, increase the amount of reactants reaching the energy barrier.

Since the temperature is kept relatively constant in the human body (due to homeostasis), the most common way human body increases the speed of a reaction is by using catalysts. Biological catalysts are called enzymes and they are usually named with the suffix -ase. The only molecule that is an enzyme in this question is DNAase, which catalyzes the hydrolysis of phosphodiester bonds in the backbone of DNA.

ATP provides energy for active reactions but it cannot speed up the reaction. Histones are proteins found in nucleus that are involved in DNA packaging. They are irrelevant to this question.

To answer this question we need to first figure out the equation for slope and x-intercept of Lineweaver-Burk plot. The Linweaver-Burk plot is a graphical way to plot the Michaelis-Menten equation. It is defined as the reciprocal of Michaelis-Menten equation. Michaelis-Menten equation is as follows.

where is reaction rate, is maximum reaction rate, is substrate concentration, and is the Michaelis constant. Taking the reciprocal of this gives us

The slope, therefore, is . The x-intercept can be found by plugging in zero for the Y value (the reaction rate, ). The x-intercept is .

The question states that the slope is and the x-intercept is . Using the equation for x-intercept we can solve for .

Using the equation for slope we can solve for

Recall that the addition of a noncompetitive inhibitor alters the but not the ; therefore, is still after the addition of noncompetitive inhibitior.

Note that if we were asked to solve for the , we would have had to use the new slope () and the same value ().

To answer this question we need to first figure out the equation for slope and x-intercept of Lineweaver-Burk plot. The Linweaver-Burk plot is a graphical way to plot the Michaelis-Menten equation. It is defined as the reciprocal of Michaelis-Menten equation. Michaelis-Menten equation is as follows.

where is reaction rate, is maximum reaction rate, is substrate concentration, and is the Michaelis constant. Taking the reciprocal of this gives us

The slope, therefore, is . The x-intercept can be found by plugging in zero for the Y value (the reaction rate, ). The x-intercept is .

The question states that the slope is and the x-intercept is . Using the equation for x-intercept we can solve for .

Using the equation for slope we can solve for

Recall that the addition of a noncompetitive inhibitor alters the but not the ; therefore, is still after the addition of noncompetitive inhibitior.

Note that if we were asked to solve for the , we would have had to use the new slope () and the same value ().

Michaelis constant, or , is defined as the concentration of substrate at which the reaction rate is half the maximum (). It is a useful measure of how much substrate is needed for reaction to proceed rapidly. A reaction with a high Michaelis constant will need lots of substrate to reach high reaction rates whereas a reaction with low Michaelis constant will need small amounts of substrate to reach high reaction rates.

Michaelis constant, or , is defined as the concentration of substrate at which the reaction rate is half the maximum (). It is a useful measure of how much substrate is needed for reaction to proceed rapidly. A reaction with a high Michaelis constant will need lots of substrate to reach high reaction rates whereas a reaction with low Michaelis constant will need small amounts of substrate to reach high reaction rates.