Homework Answers
Ans.)
K1 : No change
because it is property of single enzyme molecule. K1 is defined as rate at which a enzyme molecule combines with substrate to form enzyme-substrate (E-S) complex.
K2: No Change
because it is also property of single enzyme molecule. K2 is defined as rate at which a enzyme-substrate (E-S) complex breaks into a free enzyme and a product molecule (P).
K-1: No Change
because it is also property of single enzyme molecule. K-1 is defined as rate at which enzyme-substrate (E-S) complex breaks back free enzyme and free substrate (S).
Km: Decreases
because is it property of total enzyme concentration. It is half of Vmax. It is defined as rate of reaction when half of the enzyme molecule are complexed with substrate molecule. As enzyme concentration is decreased so Km will also decrease.
Vmax: Decreases
because it is also proper of total enzyme concentration. It is defined as rate of reaction when total enzyme molecule are saturated with substrate molecule.
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QUESTION 4 The initial velocity of an enzyme is measured at increasing substrate concentration. Evaluate the...
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4. An enzyme hydrolyzed a substrate concentration of 0.03mmol/L, the initial velocity was 0.5 X 10-3 mmol/L.min' and the maximum velocity was 4.5 x 10-3 mmol/L.min.l. Calculate the Km value. 5. Urease hydrolyzed urea at [s]=0.03mmol/L with a km of 0.06 mmol/L. The initial velocity observed was 1.5X10-3 mmol/L.min-1 Calculate the maximum velocity of the enzyme reaction.
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112 marks] 3. The relationship between initial velocity (V.) and substrate concentration of most of the enzyme- catalized reactions are explained by Michaelis-Menten equation. IMPORTANT: Show the calculations and indicate the units for all your answers. a. For an enzyme which follows the Michaelis-Menten enzyme kinetics, Km is 50 mmol L. Calculate the substrate concentration required to obtain the initial velocity (V.) equivalent to 90% of the maximum velocity (Vmax). b. The Vmax of the above reaction is 250 mmol...
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You measure the initial rate of an enzyme reaction as a function of substrate concentration in the presence and absence of an inhibitor. The following data was obtained: Create a Michaelis-Menten plot (inhibited and uninhibited should be on the same plot! You MUST use Excel and follow the provided instructions "Non-Linear Regression Fitting of Kinetics Data". Calculate the V_max in the presence and absence of the inhibitor. Calculate the K_m in the presence and absence of the inhibitor. What type...
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