a. what are the values of Vmax and Km in the abscence if the inhibitor what...
1. What effect would the inhibitor Phenylalanine have on the Km and Vmax values when added to a solution with Tyrosinase. 2. Explain why Kojic acid is an inhibitor of Tyrosinase? 3. What is the difference in using D-DOPA vs. DOPA in a substrate experiment with Tyrosinase?
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)
please graph all 3 lines and explain the vmax&km How to: Lineweaver Burke 1. The following data was determined for an enzyme in the absence of an inhibitor and in the presence of two different inhibitors (V2 and V3). Determine the V. and K for the enzyme (1) Plot the data and determine the type of inhibition for each inhibitor (S) mm 1 V2 4.3 5.5 V1 12 20 29 2 relliate 150b
le glucose Suusti dle! 6. The Vmax and KM values for an unusual hexokinase found in Trypansoma cruzi (the causative agent of Chagas disease) are shown in the presence and absence of a bisphonate inhibitor (structure shown). Without inhibitor With inhibitor KM (MM) Vmax (umol. min . mL-1) 90 0.30 125 0.12 antio- try to con OH 120 Po- O=P-0-16MMUZ 0- A bisphonate compound a. What type of inhibitor is bisphonate? b. The parasite hexokinase, unlike the mammalian enzyme, is...
3. Why is an allosteric enzyme more sensitive to substrate concentration around Km values than a Michaelis-Menten enzyme with the same Vmax? 4. Explain how pH and temperature influence enzyme activity. ( A Lineweaver-Burk (double reciprocal) plot was used to compare the effects of three different reversible inhibitors (A, B and C) on an enzyme. The plot of 1/V vs 1/[S] for the enzyme with no inhibitor is shown in a solid black line. The plot of 1/V vs 1/[S]...
1. Define Vmax and Km (Michaelis constant). What is the mathematical relationship between these two values? 2.What does Km tell you about the affinity of an enzyme for its substrate? 3.Why do we use the slope between the first two data points of Absorbance vs Time to determine V0 when studying enzyme kinetics? Why not use the slope of the entire line?
The value of Km for the shown data for a hexokinase-catalyzed reaction is with the unit of . The value of Vmax for. the same reaction is with the unit of . Be sure to give the values with the correct number of significant figures. You might have to construct a kinetic plot. For units, choose one answer from (uM, 1/ UM, HM/second, uM x second, mM, 1/mM, second, 1/second, mM/second, mM x second) vo (mM/sec) Glucose concentration (mm) 0.10...
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...
Based on the document below, 1. Describe the hypothesis Chaudhuri et al ids attempting to evaluate; in other words, what is the goal of this paper? Why is he writing it? 2. Does the data presented in the paper support the hypothesis stated in the introduction? Explain. 3.According to Chaudhuri, what is the potential role of thew alkaline phosphatase in the cleanup of industrial waste. CHAUDHURI et al: KINETIC BEHAVIOUR OF CALF INTESTINAL ALP WITH PNPP 8.5, 9, 9.5, 10,...