a) You evaluate the lipoxygenase inhibition by different concentrations of octyl protocathechuate. The curve numbers 0-4 are 0, 0.1, 0.2, 0.4, and 0.6 μM, respectively. What is the type of inhibition? Explain your answer in terms of the binding site of the inhibitor and the overall kinetic effect on lipoxygenase. 1/v (μmol/min) 1.0 0.8 0.6 0.4 0.2 .06 -0.03 0.00 0.03 0.06 0.09 1/[S] (μM)
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4a
![a) You evaluate the lipoxygenase inhibition by different concentrations of octyl protocathechuate. The
curve numbers 0-4 are 0, 0.1, 0.2, 0.4, and 0.6 μM, respectively. What is the type of inhibition?
Explain your answer in terms of the binding site of the inhibitor and the overall kinetic effect on
lipoxygenase.
1/v (μmol/min)
1.0
0.8
0.6
0.4
0.2
0
.06 -0.03 0.00 0.03 0.06 0.09
1/[S] (μM)](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2Fd7323f76-5a9c-46b6-9930-86cefe6607d1%2F167a2956-42b9-4289-bf41-6f4f9442193f%2Ffdlroo_processed.jpeg&w=3840&q=75)
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- The KM for the reaction of chymotrypsin with N-acetylvaline ethyl ester is 8.8 × 10−2 M, and the KM for the reaction of chymotrypsin with N-acetyltyrosine ethyl ester is 6.6 × 10−4 M. (a) Which substrate has the higher apparent affi nity for the enzyme? (b) Which substrate is likely to give a higher value for Vmax?1.1)the following data duscribe an enzyme-catalyzed reaction(hydrolysis of cabobenzoxyglycyl-L-tryptophan) Plot these results using a lineweaver-Burk method, and determine values for Km and Vmax. substrate concenrate(mM) Velocity(mM.sec-1) 2,5 0.024 5 0.036 10 0.053 15 0.060 20 0.061 25 0.062For a Michaelis-Menten enzyme, k1 = 5.2 ⅹ 108 M-1 s -1 , k-1 = 3.1 ⅹ 104 s -1 , and k2 = 3.4 ⅹ 105 s -1 . a) Write out the reaction, showing k1, k-1, and k2. Calculate Ks and Km. Does substrate binding approach rapid equilibrium or the steady state? Show work justify b) What is kcat for this reaction? Show work justify c) Calculate Vmax for the enzyme. The total enzyme concentration is 25 pmol L-1 , and each enzyme has two active sites.
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