a. Using the graph paper below, to plot the enzyme velocity versus the substrate concentration in the absence of ibuprofen, estimate the Km and Vmax for this enzyme.
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- List two ways that enzyme catalysis of a reaction is superior to normal conditions.Plot the following information using both the michaellis-Menten and Lineweaver-Burt plots. (Assume enzyme concentrationis constant)For Michaelis-Menton kinetics: Given an enzyme with KM of 10. at what substrate concentration will the velocity of the enzyme reach 1/2 of the Vmax?
- The following data were obtained in a study of an enzyme known to follow Michaelis-Menten kinetics. Product formed (mmol/min) Substrate added (mmol/L) 217 0.8 325 2 433 4 488 6 647 1000 The Km for this enzyme is approximately: 4 mM. 2 mM. 1 mM. 6 mM. 1000 mM.. Relation between Reaction Velocity and Substrate Concentration: MichaelisMenten Equation: At what substrate concentration would an enzyme with a kcat of 30.0s−1 and a Km of 0.0050 M operate at one-quarter of its maximum rate?Construct a figure of Lineweaver-Burk plot. Determine the K, and Vmx of the enzyme- substrate complex from this figure. Please make sure that your figure has all the necessary components such as axis title, axis scale, axis unit etc. concentration (in mM) of substrate (NPP): 0.005mM 0.01mM 0.025mM 0.5mM 0.075mM 0.1mM 0.125mM p-nitrophenol (PNP): 0.00021mMmin-1 0.00023mMmin-1 0.00029mMmin-1 0.00043mMmin -1 0.00069mMmin-1 0.00028mMmin -1 0.00055mMmin -1
- In the "Catalysis by Preferential Transition State Binding" mechanism, the substrate perfectly fits with the enzyme binding site after its geometry gets changed. Who does it? And how?Give the Vmax and Km for this enzyme that obeys Michaelis-Menten kinetics. Use 2 sig figs.For an enzyme that follows Michaelis-Menten kinetics, choose the best statement: O Vmax is completely independent of enzyme concentration. O Vmax can be attained as you add heat to the system. O Vmax can be approached but never truly attained. OVmax is attained at very high substrate concentrations.
- :The following data were obtained in a study of an enzyme known to follow Michaelis-Menten kinetics Vo (mmol/min) S (mmol/L) 0.8 3 4 217 325 433 488 1,000 :The Km for this enzyme is approximately 647 mM 4 O mM 1 O mM 1,000 Ⓒ mM 3 O mm 6 OThe steady state assumption, as applied to enzyme kinetics, implies: A. Km = Ks. B. the enzyme is regulated. C. the ES complex is formed and broken down at equivalent rates. D. the Km is equivalent to the cellular substrate concentration. E. the maximum velocity occurs when the enzyme is saturated. O A O B O C O D O E2. For an enzyme obeying Michaelis-Menten kinetics, at what concentration of S (substrate, expressed as a multiples of Km) will the initial velocity be equal to 75% of Vmax?