At what substrate concentration would an enzyme with a kcat of 30.0 sec-1 and a Km of 0.0030 M have an initial velocity that is 25% of the maximum velocity?
a. 0.0010M
b 0.0090 M
c. 0.0015 M
d. 0.0060 M
e.Cannot be determined
At what substrate concentration would an enzyme with a kcat of 30.0 sec-1 and a Km...
At what substrate concentration would an enzyme with a kcat of 30.0 sec-1 and a Km of 0.0030 M have an initial velocity that is 25% of the maximum velocity? a. 0.0010M b 0.0090 M c. 0.0015 M d. 0.0060 M e.Cannot be determined
The relation between Reaction Velocity and Substrate Concentration: Michaelis-Menten Equation a) At what substrate concentration would an enzyme with a kcat of 30.0 s-1 and a Km of 0.0050 M operate at one-quarter of its maximum rate? b) Determine the fraction of Vmax that would be obtained at the following substrate concentrations: [S]=Km/2, [S]=2Km, [S]=10Km
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
An enzyme has a Km for substrate of 10 mM and Vmax of 5 mol L-1 sec-1 at a total enzyme concentration of 1 nM. At [S] = 10 mM, kcat is: A) 2500 per M per sec. B) 5000 per M per sec. C) 1250 per M per sec. D) 2500 per sec. E) 5000 per sec.
Values for an Enzyme and a substrate are: Km=4 uM and kcat=20/min. For an experiment where [S]=6mM, it was found that Vo=480nM/min. What was the enzyme concentration? Give your answer in nM. Using the same kcat and Km as the previous question, if [Et]=0.5uM gives a Vo=5 uM/min, what wat the [S]? Give your answer in uM. reaction is run with the kcat=20/min and the Km=4uM. Use the enzyme concentration from question 1 above. A very strong inhibitor is added creating...
An enzyme that follows Michaelis-Menten kinetics has a KM value of 20.0 μM and a kcat value of 211 s−1. At an initial enzyme concentration of 0.0100 μM, the initial reaction velocity was found to be 1.07×10−6 μM/s. What was the initial concentration of the substrate, [S], used in the reaction ? Express your answer in micromolar to three significant figures.
54. What is the catalyze reaction rate? Km=2 mM Kcat= 3 s-1 At the enzyme concentration=10 nM and substrate concentration= 3 mM
For her undergraduate project, Jessica studied an enzyme that catalyzes the reaction A B. For substrate A, she determined 30 min that Km 3.0 HM and kcat Jessica graduated and her project has been passed on to you. Unfortunately, Jessica was so busy that she sometimes forgot to record all of the details of an assay in her lab notebook. Your mentor suggests that you try to back calculate some of the missing concentration values. Assume that the enzyme follows...
Kcat= 30.0sec^-1 Km= 0.0050M Total enzyme Concentration= 1uM What is the max rate of the enzyme?
Below are the Kcat and Km values for 5 hypothetical enzymes. Which enzyme would have the largest specificity constant? Enzyme A - Kcat = 2.6 x 103 , Km = 4 x 10-4 Enzyme B - Kcat = 9 x 102 , Km = 6.1 x 10-6 Enzyme C - Kcat = 1.7 x 10-3 , Km = 3.2 x 105 Enzyme D - Kcat = 2.6 x 10-7 , Km = 4 x 104 Enzyme E - Kcat =...