-11- E + SF k_1 ES ₂ E + P k2 › 10.0 + S ↓↑K IS ESS st Based on this model, please answer the following questions: midysis On i) This is the model for what? on competitive different protelas ii) Show the rate equation for an enzyme reaction of this type. iii) Show the Lineweaver-Burk plot for this case.
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- In enzyme kinetics, for the reversible with two central complexes mechanism, please provide complete proof that the rate equation is the equation below. The variables denoted with f indicate forward direction while the variables denoted with b indicate backward direction.The enzyme, fumarate, has the following kinetic constants: k 1 k 2 k -1 where k 1 = 10 9 M -1 s -1 k -1 =4.4 x 10 4 s -1 k 2 = 10 3 s -1 a. What is the value of the Michaelis constant for this enzyme? b. At an enzyme concentration of 10 -6 M, what will be the initial rate of product"Trypsin, a peptidase that hydrolyzes polypeptides, functions in the small intestine at an optimum pH of 7.7–8.0. How is the rate of a trypsin-catalyzed reaction affected by each of the following conditions?
- In enzyme kinetics, for the reversible with one complex mechanism, please provide complete proof that the rate equation is the equation below. The variables denoted with f indicates forward direction while the variables denoted with b indicate backward direction.At what substrate concentration would an enzyme with a kcat of 25.0 s-1 and a KM of 3.5 mM operate at 25% of its maximal rate? How many reactions would the enzyme catalyze in 45 seconds when it is fully saturated with substate, assuming the enzyme has one active site?Sketch the complete reaction free energy diagram for an enzyme-catalyzed conversion of a single substrate (S) into product (P), where the reaction is spontaneous in the forward direction Overlay the free energy diagram for the uncatalyzed reaction and indicate delta delta G〒 on your sketch: Chemical step is rate limiting
- Consider the following data for an enzyme-catalyzedhydrolysis reaction in the presence and absence ofinhibitor I: Using a Michaelis-Menten plot, determine Km for theuninhibited reaction and the inhibited reaction.For 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.Explain why each of the following data sets from a Lineweaver–Burk plot are not individually ideal for determining KM for an enzymecatalyzed reaction that follows Michaelis–Menten kinetics.
- Given the following information, calculate the catalytic efficiency of the enzyme. Step by step please [S] = 100 mM k1 = 10 sec-1 k2 = 3000 sec-1 k-1 = 20 sec-1 [E]T = 1 \muμMDerive the rate law for the following enzyme reaction chain. Linear the equation you have derived as a Lineweaver-Burk type equation.Graphically explain the term saturation of the enzyme? Why is the rate of an enzymecatalyzed reaction proportional to the amount of E.S complex?