1x10exp-7 From the following enzyme-catalyzed kinetic data, estimate K, and V, 'm m 25 20 15 10 1 1.2 0.6 0.8 0.2 0.4 1/Sx10exp-3
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- The following reactions were catalyzed by an enzyme that follows the Michaelis-Menten mechanism in the absence and presence of inhibitor (10mM). Assume [E]T is the same for each reaction. Determine K, and/or K'. [S] (mM) Uninhibited v (um/s) Inhibited v. (um/s) 1 3 1.67 2 4.5 2.6 6.8 4.5 10 8.1 6.2 20 9.5 7.7The rate constants of an enzyme-catalyzed reaction, obeying the Michaelis-Menten kinetics, have been determined : E + S K₁ = 2 x 108 M-¹ S-¹ -1 -1 -1 K-₁= 1 x 10³ S K₂ = 5 x 10³ S-1 K₁ 1 K-1 ES K₂ E +P 1- Determine the Michaelis constant Km of the enzyme. 2- Determine the catalytic constant (kcat) of the enzyme. 3- Determine the catalytic efficiency of the enzyme.k_1 E + SES E + P +0 k₂ S ↓↑ KIS ESS Based on this model, please answer the following questions: i) This is the model for what? Uncompet tive ii) Show the rate equation for an enzyme reaction of this type. iii) Show the Lineweaver-Burk plot for this case. A
- 41 The following data describe an enzyme-catalyzed reaction (hydrolysis of carbobenzoxyglycyl-L-tryptophan) Plot these results using the Lineweaver-Burk method, and determine values for KM and Vmax Velocity (mM.sec-) 0 024 0 036 0 053 0 060 0 061 0 062 Substrate Concentration (mM) 25 50 10 0 15 0 200 25 0 42 If the KM of an enzyme for its substrate remains constant as the concentration of the inhibitor increases, what can be said about the mode of inhibition and why? 43 Calculate the turnover number for an enzyme, assumıng Vmax IS 05 M sec1 and the concentration of the enzyme used is 0 002 M Why is it useful to know this? 44 Dıscuss the mechanism of the Bohr effect that occurs during the interactions of Hb with oxygen under physiological conditions in the lungs and tissues Make use of relevant graphs and diagrams to explain your answerWMapp E+S ES E+P Vmax Km =Vmax 2 -1 a = 1+ [1]/K, X intercept = Kcat [E]T Km Question 6 In the simple enzyme-catalyzed reaction below, which of the rate constants would be second-order? E+S ES →E+P k-1 O k2 O k-1 O k1Assume that an enzyme-catalyzed reaction follows the scheme shown: E + S ES E + P k₁ = 1 x 10%/M-s k-1 = 2.5 x 10%/s k2= 3.4 x 107s What is the dissociation constant for the enzyme-substrate, Ks? What is the Michaelis constant, Km, for this enzyme? What is the turnover number, Kcat, for this enzyme? What is the catalytic efficiency for the enzyme? If the initial Et concentration is 0.25mM, what is Vmax?
- The initial rate for an enzyme-catalyzed reaction has been determined at a number of substrate concentrations. Data are as follows: [S(u mol/L) v[(u mol/L) min-'] 5 22 10 39 20 65 50 102 100 120 200 135 (a) Estimate Vmax and K, from a direct graph of v versus [S]. Do you find difficulties in getting clear answers? (b) Now use a Lineweaver-Burk plot to analyze the same data. Does this work better?The initial rates of an enzyme-catalyzed reaction have been determined for five different [S] (see table below). [S]o (mol.L-¹) 1.0 x 10 1.5 x 10-4 2.0 x 10-4 -4 5.0 x 10 7.5 x 10-4 -1 Vo (μmol.L-¹ min-¹) 28 35 42 63 75 1- Determine graphically the value of Km (first with the Michaelis-Menten representation and then with the Lineweaver-Burk representation, then compare by reporting on the Michaelis-Menten representation the values found by the Lineweaver-Burk representation) 2- Calculate the concentration of a competitive inhibitor 1, with a K₁ value of 2.4.104 M, whose action would quadruple the apparent value of Km.For an enzyme that displays Michaelis-Menton kinetics, what is thereaction velocity, V (as a percentage of V max , observed at the followingvalues?[S] = K M[S] = 0.5K M[S] = 0.1K M[S] = 2K M[S] = 10K M
- An enzyme has a V of 1.2 uM s The Km for its substrate is 10 µM. max Calculate the initial reaction velocity, Vo, for each substrate concentration, [S]. Calculate Vo when [S] is 2 µM. Vo = µM s Calculate Vo when [S] is 10 µM. Vo = µM s-1 Calculate Vo when [S] is 30 µM. Vo = µM s-1The Michaelis-Menten equation models the hyperbolic relationship between [S] and the initial reaction rate Vo 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- Match each statement with the condition that it describes. Note that "rate" refers to initial velocity Vo where steady state conditions are assumed. [Etotal] refers to the total enzyme concentration and [Efree] refers to the concentration of free enzyme. [S] > Km Not true for any of these conditions Almost all active sites will [ES] is much lower than [Efree]. be filled. The rate is directly proportional to Increasing [Etotal] will increase [S]. Km: Adding more S will not increase [Efree] is equal to [ES]. the rate.-Inhibitor +Inhibitor [S] (mM) V0 &ν βσπ:(μmol/sec) V0&νβσπ: &ν βσπ:(μmol/sec) 0.0001 33 17 0.0005 71 50 0.001 83 67 0.005 96 91 0.01 98 95 What is the Km of this enzyme WITHOUT iinhibitor?
