5) The reaction, 2A + B P (P is the product). proceeds via a rapid pre-equilibrium...
A chemical reaction, A+B → P, has the following mechanism: 2A< Ki>A, (fast to equilibrium) A+B&K, ™C (fast to equilibrium), A,+C-k>P+ 2A (slow) where Kį and K2 are the equilibrium constants for the first two reactions, respectively. k3 is the rate constant for the third reaction. (a) [5 points] Based on this mechanism, show that the rate of product (P) formation is: d[P] – k[A[B], where k is the rate constant of the overall reaction. Write k in terms of...
2.4 Using the steady state approximation derive the rate expression for the formation of C in the reaction 2A + B (g) → 2C(9) on the basis of the following proposed mechanism ki ZA K-1 X + B K2 20 To what expression does the rate expression reduce if the second reaction is slow, the initial equilibrium established very rapidly. (8)
Please answer all of those questions 7. Which of the followings is correct about the mechanisms of enzymatic reactions? General acid-base mechanism b. Metal elements mediated mechanism a. Covalent bonding mediated mechanism d. All above c. e. None a bove Which of the followings is correct about the meaning of the constant (Km) of Michaelis-Menten equation of enzyme catalyzed reactions? a. The constant and Michaelis-Menten equation is applicable only to the stage of reaction immediately after mixing of substrate(s) with...
Consider a description of an enzymatic reaction pathway that begins with the binding of substrate S to enzyme E and ends with the release of product P from the enzyme. E+S →ES → EP E+P Under many circumstances, KM = [E] [S] / [ES] What proportion of enzyme molecules are bound to substrate when [S] = KM? Why? Recall that when [S] = KM, the reaction rate is Vmax/2. Does your answer to Part A make sense in light of...
Below is a mechanism for the reaction A+B- P 5. 2A ? A+C rate constant kl AtC 2A rate constant k B+C Prate constant k2 In this mechanism, C is an intermediate. nd the steady state approximation if necessary, determine the rate law for the reaction. (B) Under what conditions does the rate law become first order in [AJ? (C) Under what conditions does the rate not depend on [B]?
The Michaelis-Menten equation models the hyperbolic relationship between [S) and the initial reaction rate V, for an enzyme-catalyzed, single-substrate reaction E+S ES E + P. The model can be more readily understood when comparing three conditions: [S] << Km, [S] = Km, and [S] >> K. Match each statement with the condition that it describes. Note that "rate" refers to initial velocity V where steady state conditions are assumed. (E l refers to the total enzyme concentration and [Erre refers...
s- (3 pts) The flowing rates have been an enzyme- catalyzed reaction at various substrate concentrations: Run no. 103 [S]M Rate, v/ (Ms') 2.41 3.33 4.78 6.17 7.41 9.52 0.0 12.5 0.4 0.6 4 2.0 4.0 a- From Line-Weaver double reciprocal plot, obtain and Mechaelis-Menten constant, max b- If the enzyme concentration is 1.00 x 10-11 M calculate kz.
The Michaelis-Menten equation models the hyperbolic relationship between [S] and the initial reaction rate V for an enzyme-catalyzed, single-substrate reaction E+S E S E+P. The model can be more readily understood when comparing three conditions: (S) <<K.. [S] = Km, and [S] >> Km. Match each statement with the condition that it describes. Note that "rate" refers to initial velocity V, where steady state conditions are assumed. Etotal) refers to the total enzyme concentration and Etree refers to the concentration...
2. In a single substrate enzyme-catalyzed reaction, the forward rate constant (formation of ES) is 2.1x105 M-1 s-1 , the reverse rate constant (dissociation of ES to E +S) is 9.4x103 s-1 , and the catalytic rate constant (turnover of ES to P) is 7.2x102 s-1 . From this data, KM is:
Consider the mechanism. Step 1: Step 2: Overall: 2A B B+C HD 2A+ C D equilibrium slow Determine the rate law for the overall reaction, where the overall rate constant is represented as k. rate = 1