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 inhibition.
An enzyme binds to a competitive inhibitor with Kd = 1.2 × 10-6 M at pH 7.0 and 25°C.
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 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?
A simple noncompetitive inhibitor of acetylcholinesterase binds to the enzyme to affect Vmax only; it does not affect KM. Part A For an inhibition constant of KI=2.9×10?4M, what concentration of inhibitor is needed to give a 90% inhibition of the enzyme? Express your answer using two significant figures and include the appropriate units. [I] =
10.What type of inhibitor is this? How do you know? (2)
11.For your assigned inhibitor 1, what are the apparent Km &
Vmax? (NOTE: apparent Km& Vmax are just the Km & Vmax in
presence of inhibitor, at a given concentration.) (2)
Kinetics experiments were performed on PGI. Enzyme activity
(initial velocity, Vo) was measured at varying concentrations of
Glucose-6-phosphate (G6P). The enzyme concentration used in all
experiments was 1.5 μM.
12.What will be the reaction rate with 0.500 mM...
An enzyme catalyzes the reaction M↽−−⇀N .
An enzyme catalyzes the reaction M = N. The enzyme is present at a concentration of 3.5 nM, and the Vmax is 1.9 uM -. The Km for substrate M is 2.9 uM. Calculate kcat kcat = 542.86 What values of Vmax and Km would be observed in the presence of sufficient amounts of an uncompetitive inhibitor to generate an a' of 1.5? apparent Vmax = 0.526 UM s-1 apparent Km = 1.2
a) What concentration of competitive inhibitor is required to yield 75% inhibition at a substrate concentration of 1.5x10-3 M if Km=2.9x10-4 and Ki=2x10-5? b)To what concentration must the substrate be increased to re-establish the velocity at the original uninhibited value?
The following data was obtained for an enzyme in the absence of an inhibitor, and in the presence of two different inhibitors. The concentration of each inhibitor was 10 mM. The total concentration of enzyme was the same for each experiment. [S] {mM} without inhibitor v, {umol/(ml*s)} with inhibitor A v, {umol/(ml*s)} With inhibitor B v, {umol/(ml*s)} 0.0 0.0 0.0 0.0 1.0 3.6 3.2 2.6 2.0 6.3 5.3 4.5 4.0 10.0 7.8 7.1 8.0 14.3 10.1 10.2 12.0 16.7 11.3...
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.
A compound is a strong competitive inhibitor with an a = 10. The total enzyme concentration in the reaction is 10 nM. What substrate concentration reduces the velocity to 250 nM/min, knowing that this enzyme is characterized by a specificity constant of 2.1 x 105 M-1s-1 and a kcat of 25/min?
2. hypothesize the best conditions (pH and temperature) under
which the enzyme chymotrypsin functions with an appropriate
reference. also, hypothesize what will occur in the presence of an
inhibitor and the type of inhibition.
EXPERIMENT 5: ENZYME ACTIVITY WITH a-CHYMOTRYPSIN Prelab Assignment 1. Prepare a flow chart, covering one half of the experimental work (either part A and C if your lab bench is on the window side of the lab or part B and D if your locker is...