An enzyme has a maximum velocity of 48 nmoles substrate converted per sec. In the presence of 4 microM inhibitor, Vmax is 36 nmoles substrate converted per sec with no change in Km. Determine the Ki of the inhibitor. What type of inhibitor is this?
Since the inhibitor affects the Vmax of the reaction but the Km remains constant hence we can say that it is non-competitive inhibition.
Ki = [Vmaxapp.] [I] / Vmax
= 36 x 4 x 10 -4 / 48
= 3 x 10 -4 moles
An enzyme has a maximum velocity of 48 nmoles substrate converted per sec. In the presence...
An enzyme has a maximum velocity of 48 nmoles substrate converted per sec. In the presence of 4 M inhibitor, Vmax is 36 nmoles substrate converted per sec with no change in Km. Determine the Ki of the inhibitor. Identify the type of inhibitor with explanation.
Q1: A marine microorganism contains an enzyme that hydrolyzes glucose-6- sulfate (S). The assay is based on the rate of glucose formation. The enzyme in a cell-free extract has kinetic constants of km = 6.7 x 10-4, Vmax = 300 nm/L/min in presence of 10-5M competitive inhibitor (Galactose-6-sulfate) and 2 x 10-5M substrate (Glucose-6-sulfate), velocity was 1.5 nmoles /L/min. a) Calculate Ki for Galactose-6-sulfate b) Calculate velocity in absence of the inhibitor
1. The kinetics of an enzyme was examined at various substrate concentrations in both the presence and absence of 3 mM inhibitor Z. The initial velocity data obtained are shown below: [S] (mmoles liter) v (mmoles"litermin) no inhibitor inhibitor Z 1.25 1.67 2.50 5.00 10.0 1.72 2.04 2.63 3.33 4.17 0.98 1.17 1.47 1.96 2.38 (4 pts) Estimat e Vmax and Kw in the presence and absence of inhibitor using the Michaelis Menton curve-fitting program on Kaleidagraph (see lab manual)....
The following observations come from Lineweaver-Burke plots, based on kinetic data generated from a Michaelis/Menton-type enzyme (E) that catalyzes the hydrolysis of a peptide substrate (S). All data were generated in the presence of 18.0 μM total enzyme. The enzyme-catalyzed reaction has a Km of 3.00 μM and a Vmax of 2.00 μM/sec. The enzyme-catalyzed reaction in the presence of 15.0 μM of Inhibitor A has an apparent Km of 2.25 μM and an apparent Vmax of 1.50 μM/sec. The...
An enzyme has a Km of 4.7X10^-5 M. If the Vmax of the preparation is (22 micromoles X liters^-1 Xmin^-1). What velocity would be observed in the presence of 2X10^-4 M substrate and 5X10^-4M of a. a competitive inhibitor b. a noncompetitive inhibitor c. an uncompetitive inhibiter Ki in all three cases is 3X10^-4M. What is the degree of inhibition in all three cases?
1. An enzyme has a km of 4.7 X 105M. If the Vmax of the preparation is 224M/min, what velocity would be observed in the presence of 2 X 10^M substrate and 5 X10+M a competitive inhibitor. Ki is 3 X 10^M. What is the degree of inhibition? (10pts)
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
You have an inhibitor for an enzyme that you are studying. The concentration of inhibitor used is 5.50 µM. The following data was collected for the non-inhibited reaction as well as the reaction that was inhibited. mmol/(mL min) mmol/(mL min) mM Substrate Vo Substrate Vo + Inhibitor 0.200 5.000 3.751 0.400 7.500 4.998 0.800 10.000 5.995 1.000 10.700 6.173 2.000 12.500 6.807 4.000 13.600 7.143 a. Plot this data using Excel or a graphing program. Make sure you give your graph has a...
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...
An enzyme binds to a competitive inhibitor with Kd = 1.2 × 10-6 M at pH 7.0 and 25°C.(a)At what inhibitor concentration will 75% of the enzyme be bound to the inhibitor if there is no substrate present? (b) This enzyme has a Km of 4.0 × 10-5 M and a Vmax of 50 μM/s. At a substrate concentration of 3.0 × 10-4 M, calculate (i) the velocity of reaction in the presence of the inhibitor at 4.8 x 10-5 M (ii) the degree of...