When a competitive inhibitor molecule is bound to amylase, and there is a regular amount of substrate present, will the reaction happen? Please explain
Ans: Competitive inhibitor as the name suggests, compete with the substrate for the binding to the active site of the enzyme. The inhibitor is able to bind with the active site due to the structural similarity between substrate and inhibitor and when the competitive inhibitor binds to the active site than substrate is not able to bind with the enzyme and the reaction will not be proceed.
So when a competitive inhibitor molecule is bound to amylase, and there is a regular amount of substrate present, the reaction will not be proceed because all the active sites will be captured by the competitive inhibitor and substrate will not bind to the amylase's active site for the reaction to proceed. This can be altered by increasing the concentration of substrate as when concentration of substrate is high there will be more chance of binding the substrate to the active site of the enzyme as compared to the competitive inhibitor.
Hence the reaction will not happen when there is regular amount of substrate present.
When a competitive inhibitor molecule is bound to amylase, and there is a regular amount of...
This is a diagram of a known inhibitor of amylase. If you were to make a prediction, what type of inhibitor (competitive or non-competitive) is it? What is your reasoning?
An enzyme binds to a competitive inhibitor with Kd = 1.2 × 10-6 M at pH 7.0 and 25°C.(a)At what inhibitor concentration will 75% of the enzyme be bound to the inhibitor if there is no substrate present? (b) This enzyme has a Km of 4.0 × 10-5 M and a Vmax of 50 μM/s. At a substrate concentration of 3.0 × 10-4 M, calculate (i) the velocity of reaction in the presence of the inhibitor at 4.8 x 10-5 M (ii) the degree of...
A competitive inhibitor is a molecule that: Preferentially binds to an enzyme at a site other than the active site Enhances the catalysis of an enzyme Binds to an enzyme and increases the bind strength of the substrate Binds to the active site and blocks the substrate More than one of the above.
b. Look at the graph below of how a competitive inhibitor affects the kinetics of an enzyme C. Rate of reaction is the Vmax of the enzyme affected? Why or why not: explain in terms of substrate concentration and enzyme active site saturation) Without inhibitor With competitive inhibitor d. is Vmax/2 affected? Why or why not: explain in terms of Vmax. Substrate concentration e. Is Km affected? Explain in terms of the active site. Hint a competitive inhibitor is competing...
Reset Help noncompetitive enzyme irreversible acetylcholinesterase competitive active site 1. A inhibitor binds to a site on the enzyme that is not the active site. 2. Insecticides and nerve gases act as irreversible inhibitors of nerve conduction. an enzyme needed for 3. A inhibitor has a structure that is so similar to the substrate that it can bond to the enzyme just like the substrate. 4. Usually, an nhibitor forms a covalent bond with an amino acid side group within...
need help 7f and 7h Figure 3: Reaction rate produced by Enzyme X with various inhibitor treatments Reaction rate 30 mM 30 mM 60 mM 60 mM substrate +100 60 mM 30 mM substrate +100 l Inhibitor substrate+ substrate+ Substrate substrate +100 ul Inhibitor +100 l Inhibitor no inhibitor no inhibitor pet inhibe hhthitohior in Figure 3 (on the previous page), you can tell that Inhibitor B is a or poor ) inhibitor of Enzyme X. Y13 pts) Explain your...
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Questions #1-2 refer to Atorvastatin, which is a competitive inhibitor of the rate limiting step of cholesterol biosynthesis. 1. What is the downstream effect of treating cells with this competitive inhibitor? A. Atorvastatin decreases the Vmax of HMG CoA synthase. B. Atorvastatin decreases the KM of HMG CoA synthase. C. Atorvastatin decreases the Vmax of HMG CoA reductase. D. Atorvastatin decreases the KM of HMG CoA reductase. E. Atorvastatin increases the KM of HMG CoA reductase. 2. Mechanistically, how does...
Microbiology In the competitive inhibition of enzyme activity, which statement is correct? Inhibitor directly competes with the substrate. Less substrates must be added in order to reach Vmax. The number of active sites is unlimited. None of the above. In the noncompetitive inhibition of enzyme activity, which statement is correct?Inhibitors will cause a conformational change in the enzyme, more substrate must be added to reach Vmax, Enzymes bound to the inhibitor can still bind substrate, none of the above. ....
An enzyme-catalyzed reaction to the presence of 5 nM of reversible inhibitor yields a Vmax value that is 80% of the value in absence of the inhibitor. The KMvalue is unchanged. a) what type of inhibition is occurring? b) what proportion of the enzyme molecule will have bound inhibitor? c) Draw the Lineweaver-Burk (known as double-reciprocal plot) for uninhibited and inhibited reaction. SHOW ALL YOUR WORK PLEASE