Consider the enzyme-catalyzed reaction with Vmax=164 (μmol/L)min−1 and KM=32μmol/L. |
Part A If the total enzyme concentration was 6 nmol/L, how many molecules of substrate can a molecule of enzyme process in each minute? Express your answer to three significant figures.
Part B Calculate kcat/KM for the enzyme reaction. |
Consider the enzyme-catalyzed reaction with Vmax=164 (μmol/L)min−1 and KM=32μmol/L. Part A If the total enzyme concentration...
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...
What is the rate of an enzyme catalyzed reaction if the Vmax is 100µmol S→P/min and the Km is 7 mM and the substrate concentration is 11mM? Is the enzyme working at Vmax? What if the substrate concentration is raised to 25mM?
To determine the kinetic characteristics of an enzyme you used 1 nmol/L of enzyme in a series of assays where you measured the rate of reactions as you varied the concentration of substrate in each assay (Table A). Estimate from a Michaelis-Menten plot approximate values for Vmax, KM, Kcat, and the specificity constant for this enzyme and substrate. (The only information that is given is this paragraph and the table below). Table 1: [S] (μM) v (μmol/L/min) 0 0 5...
a. An enzyme has a Vmax of 100 umol/min and a Km of 40 uM. When substrate concentration is 40 uM what is the initial reaction rate? b. An enzyme with a Vmax of 100 umol/minute and a Km of 10 uM was reacted with a irreversible active site specific inhibitor. After reaction with the inhibitor, the enzyme was assayed using a 2 mM concentration of substrate, and it gave a reaction rate of 20 umol/min. What percentage of the...
CHEM3250 Assignment-Enzyme Inhibition Consider the data below for an enzyme catalyzed reaction. The rate of the reaction has been determined with and without an inhibitor. A total concentration of enzyme of 20 uM was used in the experiment. SHOW WORK AND UNITS!!! Without Inhibitor With Inhibitor [substrate] (mM)Rate of formation of te of formation of product product (mM/min) mM/min) 6.67 5.25 0.49 7.04 38.91 1.0 2.2 6.9 41.8 44.0 1.5 3.5 1 a) On the same graph, plot the data...
5. The Km of an enzyme of an enzyme-catalyzed reaction is 6.5 uM. What substrate concentration will be required to obtain 55% of Vmax for this enzyme? (10 pts)
At an enzyme concentration of 1microM the Vmax is 100microM/min and the Km is 20nm. At an enzyme concentration of 2microM, what would the V0 be at a substrate concentration of 40mM?
Need help with number 13! I already asked about number 12. The inverse velocity and inverse substrate concentration relationship for an enzyme-catalyzed reaction is given below V Vmax Vmax S For the hydration of CO2 catalyzed by carbonic anhydrase, it was determined experimentally that (dm s mol 4023.9+ 39.934 at a total enzyme IS] concentration of 2.32 × 10-y mol-dm- What is the value of the Michaelis constant KM for this enzymatic reaction? (B). 9.92x103 mol dm3 (D). 100.8 mol...
An enzyme catalyzes the reaction M N. The enzyme is present at a concentration of 3.5 nM, and the Vmax is 2.9 PM s-. The Km for substrate M is 6.5 MM. Calculate kcat kcat = 1 What values of Vmax and Km would be observed in the presence of sufficient amounts of an uncompetitive inhibitor to generate an a' of 1.3? apparent Vmax = UM S-1 apparent Km = UM
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.