Show how the addition of a competitive inhibitor would affect the reaction velocity and double-reciprocal plots shown below. 1 Reaction velocity (Vo) Vmax Vmax/2 max KM Substrate concentration [S]->> 1/Vo Slope=KM/Vmax Intercept = -1/KM 0 Intercept = 1/Vmax 1/[S]
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question is attached
![8. Show how the addition of a competitive inhibitor would affect the reaction velocity and
double-reciprocal plots shown below.
1
Reaction velocity (V)
Vmax
Vmax/2
- KM
Vmax
Substrate concentration [S] -
1/Vo Slope=KM/Vmax
Intercept = -1/KM
0
Intercept = 1/Vmax
1/[S]](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F321fd000-515a-4cf5-ac03-99096af58e6a%2F03c31203-e2fe-4060-8eca-920c3daffcc1%2Fnuuhrf_processed.jpeg&w=3840&q=75)
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- 1 the concentration of the enzyme competition inhibitor was 1×10-3M. If 1 µmol of the inhibitor is present inthe 1 mL reaction mixture, Indicate how much the initial degree of hydrolysis decreases as a proportion(in thepresence of inhibitors/in the absence of inhibitors) with respect to the absence of inhibitors.1. As seen in the picture: - What kind of inhibition (competitive, uncompetitive, mixed) is involved? - Calculate Vmax and Kmax in the absence and presence of inhibitor A Show complete solution.1.In a kinetics data set, in case a substrate concentration is given [S] in uM and inhibitor concentration [I] uM, initial velocity (Vo) in umol/min , Km , Vmax, apparent Km, apparent Vmax, and Ki, is there any way of finding Kcat ? 2.Which formula would be used in that case? What would the process be for finding Kcat?
- 4. a. Use the data in the graph above to estimate a KM value for the enzyme in the presence of these metabolites, and enter them into the table below. b. Classify these metabolites as either activators or inhibitors, and explain your rationale below.Calculate KI (in units of nmol L-1) for a competitive inhibitor that has α = 1.65 when 11.0 nmol L-1 inhibitor is present.5.5 Explain the effect of each type of inhibitor on the apparent kinetic parameters: (1) Inhibitor binds only free enzyme does Km increase, decrease, not change? does Vmax increase, decrease, not change? (2) Inhibitor binds only ES complex does Km increase, decrease, not change? does Vmax increase, decrease, not change? (3)Inhibitor binds E and ES equally does Km increase, decrease, not change? does Vmax increase, decrease, not change?
- Hi, if I have the substrate concentration as 20, 40 , 65 and the V(mol/min) no inhibitor 602, 690, 833 and with inhibitor 370, 476, 526. How would I plot these numbers on both a MMplot and an LB plot and How would I claulate the Km and Vmax for each graph1. The concentration of substrate X is high. What happens to the rate of the enzyme-catalyzed reaction if the concentration of substrate X is reduced? Explain. 2. An enzyme has an optimum pH of 7.2. What is most likely to happen to the activity of the enzyme if the pH drops to 6.2? Explain1. How much faster is a reaction with the faster enzyme than without a catalyst? * A. Approximately 10 times faster. B. About 100 times faster. C. Approximately 1,000 times faster. D. About 10,000 times faster. E. About 10X^20 times faster. 2. For competitive inhibition * A. KM value decreases B. the value of Vmax decreases C. it is possible to overcome the effect of the inhibitor by increasing the concentration of substrate D. None of the above
- For an enzyme-catalyzed reaction, the presence of 5 nM of a reversible inhibitor yields a Vmax value that is 80% of the value in the absence of the inhibitor. The KM value is unchanged. (a) What type of inhibition is likely occurring? (b) What proportion of the enzyme molecules have bound inhibitor? (c) Calculate the inhibition constant.10. For the situations described below, indicate whether KM , Vmax, both parameters, orneither parameter would be altered. Assume that [S] in in excess.(a) After [S] has been doubled(b) In the presence of a competitive inhibitor(c) After the [E] has been doubledA biochemist wants to determine the effect of inhibitor A to enzyme B which catlyzes the conversion of C to D. The effect of A to the rate of formation of D is shown below: 1. The Km (report to the nearest whole number) for the enzyme-catalyzed reaction in the absence of inhibitor A is _____ mM. 2. The Km for the enzyme catalyzed reaction in the presence of inhibitor A is ____mM. 3. The Vmax for the enzyme catalyzed reaction in the absence of inhibitor A is ____ mM/min 4. The Vmax for the enzyme catalyzed reaction in the presence of inhibitor A is ____mM/min 5. Inhibitor A is a/an ________ inhibitor of enzyme B