4. An enzyme hydrolyzed a substrate concentration of 0.03mmol/L, the initial velocity was 0.5 X 10-3...
6. An enzyme with a km of 0.06mmol/L hydrolyzed a substrate of a concentration 0.03 mmol/L. The initial velocity ws 0.0015 mmol/L.min!. Calculate the substrate concentration which gives an initial velocity of 0.003 mmol/L. min-1 7. 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 Calculate the initial velocity of the enzyme reaction when using [s]=0.12mmol/L
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...
If the enzyme concentration is 3.8 X 10-8, what concentration of substrate would generate a velocity equal to 0.25 Vmax? Km is not needed. Km= 15.42M
What is substrate concentration, expressed as a multiple of Km, when an enzyme reaction is observed to have an initial rate Vo = 0.75 Vmax. Select one: O a. [S] = 0.33 x km O b. [S] = 0.25 km O c. [S] = 0.75 x Km O d. [S] = 0.3 x km O e. [S] = 0.5 x km Check Next page ime Jump to...
If the enzyme concentration is 3.8 X 10-8, what concentration of substrate would generate a velocity equal to 0.25 Vmax? Km is not needed.
1) 2) If the total enzyme concentration was 9 nmol/Lnmol/L, how many molecules of substrate can a molecule of enzyme process in each minute? Express your answer to three significant figures. 3) The kcat for neuraminidase at pH=6.15pH=6.15, 37 ∘C∘C is 26.8 s−1s−1. Calculate KMKM for the hydrolysis of sialic acid. Express your answer with the appropriate units. An enzyme that follows Michaelis-Menten kinetics has a Ky value of 6.00 uM and a keat value of 176 s-1. At an...
An enzyme that follows Michaelis-Menten kinetics has a initial velocity of 300 nM/s at a substrate concentration of 30 uM. The maximum velocity of 400 nM/sec. What is the Km for this enzyme in uM? (Give your answer as a number only. Type your response
An enzyme catalyzes the reaction A ⇌ B. The enzyme is present at a concentration of 2 nM, and the Vmax is 1.2 μM s−1. The Km for substrate A is 10 μM. Calculate the initial velocity of the reaction, V0, when the substrate concentration is (a) 2 μM, (b) 10 μM, (c) 30 μM.
(15 points) The following data is for a reaction catalyzed by tyrosine monoxygenase: Substrate Concentration (mol/L) Initial Velocity (mM/min) 1.5 0.66 1.2 0.65 0.81 0.45 0.65 0.39 0.49 0.32 0.27 0.21 a) Plot the velocity (y-axis) versus substrate concentration [S] (x-axis) curve and insert/draw the graph in the space below. What are the approximate KM and Vmax values? b) Construct a 1/v (y-axis) versus 1/[S] (x-axis) plot in the space below. Calculate the KM and Vmax values. c) Calculate the...
QUESTION 1 One of the major concerns in fermented foodstuff is the presence of urethane in their products, as this compound is known to be carcinogenic. Therefore, the removal of urea, a precursor of urethane, must be achieved efficiently to comply with governmental limiting levels of urethane. One of the most common processes for the removal of urea in the industrial production of alcoholic beverages is the use of urease enzyme. Using 10 g∙dm-3 of urease, initial laboratory tests...