What will happen to the enzyme chymotrypsin in the presence of an inhibitor and the type of inhibition?
Chymotrypsin belonging to the family of serine proteases depend mainly on the serine residues present in the active site of enzyme for carrying out proteolytic activity. It's activity is inhibited by DIPF which is a group specific reagent, this reagent irreversibly blocks the enzyme from carrying out any enzymatic activity.
What will happen to the enzyme chymotrypsin in the presence of an inhibitor and the type...
Given the kinetics data for each enzyme in the presence and absence of its inhibitor, determine the type of inhibition. EnzymeK_(M)(mM)V_(max)(mmol//s)carbonic anhydrase8,000600,000+ inhibitor A12,000600,000chymotrypsin5,000100+ inhibitor B5,00075penicillinase502,000+ inhibitor C301,500lysozyme60.5+ inhibitor D150.5carboxypeptisase A31,000+ inhibitor E3800
An enzyme-catalyzed reaction to the presence of 5 nM of reversible inhibitor yields a Vmax value that is 80% of the value in absence of the inhibitor. The KMvalue is unchanged. a) what type of inhibition is occurring? b) what proportion of the enzyme molecule will have bound inhibitor? c) Draw the Lineweaver-Burk (known as double-reciprocal plot) for uninhibited and inhibited reaction. SHOW ALL YOUR WORK PLEASE
The activity of an enzyme was tested in the presence of a mixed type of inhibitor. The Lineweaver-Burke plot below shows the results from the experiment without inhibitor and with inhibitor. Knowing that the inhibitor concentration was 12mm, calculate Ki and Ki'. K0.5 ki' =
18. The following kinetic scheme that shows the Inhibitor () only binding to the enzyme-substrate (ES) complex is typic of what type of enzyme inhibition? E + SEES -E + PSN ESI no reaction A) Irreversible B) Competitive C) Noncompetitive D) Uncompetitive or acetylcholinesterase 19. DIFP acts as an inhibitor of the enzyme chymotrypsin. A) Irreversible B) Competitive C) Uncompetitive D) Mixed
For a report, after plotting the lineweaver-burk plot for a protease enzyme with and without inhibitor. It shows that the km value increases in the presence of inhibitor and Vmax decreases. what type of inhibition is it? The inhibitor is an azide.
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...
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 catalyzed reaction was performed in the presence and in the absence of an inhibitor. The Lineweaver Burk plot showed competitive kinetics with x-intercepts of -10mm -1 and -3.5mm -1 in the presence and absence of the inhibitor respectively. If the inhibitor concentration used was 2micro molar (UM), calculate KI for the inhibitor enzyme binding? a. none of the above b. 0.135nM c. 0.054nM d. 0.225nM e. 1077 nM
protease action of Chymotrypsin as a model of a specific type of enzyme mechanism. Answer the following questions about chymotrypsin. List the residues involved in the “catalytic triad”: What is the specificity of Chymotrypsin? (where does it cut) What type of protease is Chymotrypsin? What type of general enzyme mechanism is used by chymotrypsin? What is the oxyanion hole used for? Briefly outline the steps in catalysis for the enzyme.
Which amino acids in chymotrypsin are found in the active site and are participants in substrate cleavage? His, Ser, Asp His, Ser, Arg His, Ser Lys, Ser, Asp Where does cleavage of the peptide bond by chymotrypsin occur? On the C-terminal side of positively charged residues (lysine or). On the N-terminal side of aromatic residues (e.g. phonylalanine or tryprophase). On the C-terminal side of aromatic residues (e.g. phenylalanine or). All of the above When substrate concentration is much greater than...