Q. Why do enzymes have a maximum rate of reaction?
By increasing the enzyme concentration, the maximum reaction rate greatly increases. Conclusions: The rate of a chemical reaction increases as the substrate concentration increases. Enzymes can greatly speed up the rate of a reaction. However, enzymes become saturated when the substrate concentration is high.
Q. Why do enzymes reach a maximum velocity?
Enzymes. Maximal Velocity (Vmax): Increasing the substrate concentration indefinitely does not increase the rate of an enzyme-catalyzed reaction beyond a certain point. This point is reached when there are enough substrate molecules to completely fill (saturate) the enzyme’s active sites.
Table of Contents
- Q. Why do enzymes have a maximum rate of reaction?
- Q. Why do enzymes reach a maximum velocity?
- Q. What happens to kcat when enzyme is doubled?
- Q. What happens to kcat when enzyme concentration increases?
- Q. Is kcat affected by substrate concentration?
- Q. Is Vmax dependent on kcat?
- Q. Are enzymes equally active on D and L isomers?
- Q. Which are true enzymes?
- Q. Are enzymes stable at high temperatures?
- Q. What makes an enzyme stable?
Q. What happens to kcat when enzyme is doubled?
When you change enzyme concentration how does that affect Vmax, KM, and kcat? Vmax depends on the enzyme concentration, so if you double the amount of enzyme you double Vmax. Km and kcat are constants so changing the enzyme concentration will not change their value.
Q. What happens to kcat when enzyme concentration increases?
5. As one increases the amount of substrate for an enzymatic reaction, the velocity of the reaction (concentratioin of product made per time) increases. If one uses more enzyme, one produces a faster velocity.
Q. Is kcat affected by substrate concentration?
Most of the time Kcat just equals K2 (NOT the case when there are more reaction steps). Kcat/Km represents the rate of the reaction at negligible substrate concentration.
Q. Is Vmax dependent on kcat?
Km is a constant for a given substrate acting on a given enzyme. However, Vmax is directedly proportional to enzyme concentration as Kcat is a constant for a given enzyme.
Q. Are enzymes equally active on D and L isomers?
They are generally equally active on D and L isomers of a given substrate. They can increase the equilibrium constant for a given reaction by a thousand fold or more.
Q. Which are true enzymes?
The answer is: It is a protein; It is a catalyst. Enzymes are proteins and they act as catalysts in a cell. They increase the rate at which chemical reactions occur within the cell. After the reaction, they are not altered or consumed fully. An enzyme can act as a catalyst of the same chemical reaction multiple times.
Q. Are enzymes stable at high temperatures?
Extracellular and cell-bound hyperthermophilic enzymes (i.e., saccharidases and proteases) are optimally active at temperatures above—sometimes far above—the host organism’s optimum growth temperature and are, as a rule, highly stable.
Q. What makes an enzyme stable?
Enzyme stability in aqueous media is influenced primarily by temperature and pH and to some extent by the presence of the substrate. For enzyme operating in oils and fats, it is still the temperature and pH that are key factors for optimum enzyme activity and stability.
