A common variant of the Michaelis-Menten model of enzyme kinetics involves inhibition by excess substrate. This phenomenon is known as substrate inhibition and the mathematical description of it requires an inhibition constant (Ki) as well as the usual kinetic parameters (Km and Vmax). Fitting the...
The concentration of an enzyme within a cell is extremely low relative to other materials present, yet functions effectively in its metabolic rate. How can enzymes function and never seem to run out?The active site of an enzyme is a small portion of the enzyme molecul...
What value of(s), as a fraction of km, is required to obtain 20% vmax?(s)equals: Michaelis-Menten Kinetics: Michaelis-Menten kinetics describe enzyme activity under specific conditions. The concentration of the enzyme is held constant while the concentration of the substrate...
Kinetic analysis of the residual enzyme activity from our most conservative construct, Arg211---, determined an apparent Vmax approximately 400-fold reduced from that of the wild type enzyme but detected no change in the apparent Km. Additionally, the pH optimum of this mutant enzyme was narrower...
This paper presents an undergraduate laboratory exercise that allows for the experimental determination of the typical enzyme-kinetics parameters [the Michaelis constant (KM), the maximum rate of the enzyme-catalyzed reaction (Vmax), the turnover number (kcat), and the catalytic efficiency of the en...
The key difference between Km and Vmax is that Km measures how easily an enzyme can be saturated by the substrate, whereas Vmax is the maximum rate at whic
Kinetic analysis of the residual enzyme activity from our most conservative construct, Arg211---, determined an apparent Vmax approximately 400-fold reduced from that of the wild type enzyme but detected no change in the apparent Km. Additionally, the pH optimum of this mutant enzyme was narrower...
If an enzyme is boiled, what happens to it? Why do enzymes have different optimal pH? Why is Kcat/Km referred to as the efficiency of an enzyme? If an enzyme/catalyst works to speed up a reaction, why does the activation energy is lowered? How are enzymes involved in regulating energy...
How does enzyme structure determine the function of the enzyme? In enzyme activity, both co-enzymes and co-factors are greatly involved. Briefly explain the difference between the two and state the functions of each. What are the structural factors that affect an enzyme's kinetics (Km/Vmax)?
A lower Vmax means that the enzyme is operating in sub-optimal conditions. This may be because physical conditions such as temperature and pH are not...Become a member and unlock all Study Answers Start today. Try it now Create an account Ask a question Our experts can answer your ...