1, What is the initial velocity (V0) of an enzymatic reaction? Velocity achieved
ID: 197961 • Letter: 1
Question
1, What is the initial velocity (V0) of an enzymatic reaction?
Velocity achieved just after initiating the reaction
2. All enzymes must satisfy the Michaelis-Menten equation.
3. The higher the value of the Michaelis constant, the tighter the substrate binding to the enzyme is.
4. The model of allosteric regulation of enzymes that requires all subunits to be in the same state (conformation) is called:
5. Activity of enzymes is the highest at an optimum pH and decreases for higher and lower pH conditions. The reason for this effect is:
6. What type(s) of enzyme inhibition can be reversed?
7.
A reversible inhibitor binds only to the enzyme-substrate complex. What is the effect of this inhibitor on Vmax (maximal velocity) and KM (Michaelis constant) of the enzyme?
8. What conclusion can be drawn if KM is the same in the presence and absence of the inhibitor?
The inhibitor binds to the same site in the enzyme as the substrate
The inhibitor does not bind to the same site in the enzyme as the substrate
9. You are testing a new drug in a laboratory. The drug is a reversible inhibitor of a certain enzyme. You find that no matter how high concentration of the substrate is, the drug is able to inhibit the enzyme activity. You can exclude which type of inhibition:
10. In which type of enzyme inhibition both substrate and inhibitor bind to the same site in an enzyme?
Velocity when the substrate concentration is very lowExplanation / Answer
Ans.1 velocity when the substrate concentration is very high. Because when substrate is very high that means reaction is just started.
Ans 2. False
Allosteric reaction do not follow michalis menten equation.
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