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Urea denatures the enzyme as it disrupts the 3-D structure of the enzyme, this changes the shape of the enzymes' active site, thus meaning that the enzyme is unable to create an enzyme-substrate complex which then means that the reaction cannot occur thus the rate of the enzyme controlled reaction becomes very slow.
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What does the enzyme activity curve reveal about the relationship between enzyme concentration and reaction rate?
The enzyme activity curve shows that as enzyme concentration increases, the reaction rate also increases. However, there is a point where adding more enzyme does not further increase the reaction rate, indicating that there is a limit to the effect of enzyme concentration on reaction rate.
What is the rate-limiting step of an enzyme-catalyzed reaction?
The rate-limiting step of an enzyme-catalyzed reaction is the slowest step in the reaction that determines the overall rate at which the reaction proceeds.
What affect does too much substrate have on the rate of an enzyme reaction?
If there is too much substrate present, it can saturate all available enzyme active sites, leading to maximum reaction rate being reached (Vmax). Further increases in substrate concentration will not increase the reaction rate since all enzyme active sites are already occupied. This is known as enzyme saturation.
What does the enzyme graph reveal about the reaction rate of the catalyzed reaction?
The enzyme graph shows that the reaction rate of the catalyzed reaction is faster compared to the uncatalyzed reaction. This indicates that the enzyme is effectively speeding up the reaction process.
Why would you expect the rate of an enzyme-catalyzed reaction to increase proportionately to enzyme concentration given an unlimited supply of substrate?
No, since the reaction reaches a max rate depending on the speed of which the Enzyme bonds to the substrate and the speed at which the enzyme catalyzes the reaction to produce enzyme and product (shown below). E + S --> ES (E - enzyme, S - substrate, P - products) ES --> E + P Thus, if each reaction rate is not equal to each other, the rate of the overall reaction is not only proportional to both the concentration of enzyme and substrate.
What has no effect on the rate of an enzyme-catalyzed reaction?
Enzyme concentration has no effect on the rate of an enzyme-catalyzed reaction after reaching a saturation point where all enzyme active sites are occupied. At this point, adding more enzyme will not increase the reaction rate further.
What does the enzyme activity curve reveal about the relationship between enzyme concentration and reaction rate?
The enzyme activity curve shows that as enzyme concentration increases, the reaction rate also increases. However, there is a point where adding more enzyme does not further increase the reaction rate, indicating that there is a limit to the effect of enzyme concentration on reaction rate.
How does competitive inhibition affect the value of Vmax in enzyme kinetics?
Competitive inhibition decreases the value of Vmax in enzyme kinetics by reducing the rate at which the enzyme can catalyze a reaction. This is because the inhibitor competes with the substrate for binding to the active site of the enzyme, slowing down the overall reaction rate.
What is the rate-limiting step of an enzyme-catalyzed reaction?
The rate-limiting step of an enzyme-catalyzed reaction is the slowest step in the reaction that determines the overall rate at which the reaction proceeds.
What affect does too much substrate have on the rate of an enzyme reaction?
If there is too much substrate present, it can saturate all available enzyme active sites, leading to maximum reaction rate being reached (Vmax). Further increases in substrate concentration will not increase the reaction rate since all enzyme active sites are already occupied. This is known as enzyme saturation.
What does the enzyme graph reveal about the reaction rate of the catalyzed reaction?
The enzyme graph shows that the reaction rate of the catalyzed reaction is faster compared to the uncatalyzed reaction. This indicates that the enzyme is effectively speeding up the reaction process.
What do you call the rate of an enzyme catalyzed reaction?
The rate of an enzyme-catalyzed reaction is often referred to as the enzyme's catalytic activity or turnover rate. It is a measure of how quickly the enzyme can convert substrate molecules into products.
What happens to the reaction rate as the enzyme concentration is increased?
As enzyme concentration increases, the reaction rate usually increases because there are more enzyme molecules available to catalyze the reaction. This is because enzymes can bind to more substrate molecules simultaneously, leading to a greater frequency of successful collisions and faster conversion to product. However, once all substrate molecules are bound to enzymes (enzyme saturation), further increases in enzyme concentration will not significantly affect the reaction rate.
How does the non-competitive inhibitor decrease the rate of an enzyme reaction?
Noncompetitive inhibitors decrease the rate of an enzyme reaction by bonding to an enzyme somewhere other than the active site, deforming it and permanently disabling the enzyme, so that enzyme can never function again, so the rate of reaction decreases.
How salt concentration affect the rate of enzyme reaction?
Each enzyme has an optimal salt concentration. Changes in the salt concentration may also denature enzymes.
What three factors affect the rate of a biochemical reaction?
The three factors that affect the rate of a biochemical reaction are temperature, substrate concentration, and enzyme concentration. Temperature influences the kinetic energy of molecules involved in the reaction, substrate concentration determines the amount of reactants available for the reaction, and enzyme concentration affects the number of catalysts available to facilitate the reaction.
Why would you expect the rate of an enzyme-catalyzed reaction to increase proportionately to enzyme concentration given an unlimited supply of substrate?
No, since the reaction reaches a max rate depending on the speed of which the Enzyme bonds to the substrate and the speed at which the enzyme catalyzes the reaction to produce enzyme and product (shown below). E + S --> ES (E - enzyme, S - substrate, P - products) ES --> E + P Thus, if each reaction rate is not equal to each other, the rate of the overall reaction is not only proportional to both the concentration of enzyme and substrate.
