The Lineweaver - Burk plot (Figure 1) shows an enzyme-catalyzed reaction in the absence and presence of 0.1µM inhibitor (ketoconazole). O Estimate Vmax and Km in the absence and presence of the inhibito.. (i) Determine the type of inhibition shown by the inhibitor. Explain. 0.1
Q: What is the relationship between a transitionstate analog and the induced-fit model of enzyme…
A: Induced-fit model : A model of enzyme catalysis in which the enzyme conformation changes in response…
Q: 1.1)the following data duscribe an enzyme-catalyzed reaction(hydrolysis of…
A: Background information Km is that substrate concentration at which velocity is half of the maximum.…
Q: Compare and contrast Bound Fraction equation in ligand binding and Michaelis-Menten equation in…
A: The Michaelis-Menten equation is the rate equation for a one-substrate enzyme-catalyzed reaction.…
Q: When enzyme solutions are heated, there is a progressive loss of catalytic activity over time due to…
A: Enzyme is a protein and its denatured at high temperature. High temperature broke its peptide bond.…
Q: In an enzyme kinetics study, three inhibitors resulted to the following results: Inhibitor ABC…
A: Enzymes are biological catalysts that help chemical processes occur faster. Enzymes are proteins…
Q: e2 S2 e1 So e3 S3 For the above metabolic pathway, each reaction is catalyzed by an enzyme, E, with…
A: Given, three sub-reactions and 1 side reaction happen, in the overall reaction to produce P from S0.…
Q: The Michaelis-Menten equation models the hyperbolic relationship between [S] and the initial…
A: The Michaelis-Menten equation is represented as follows: V0 =VmaxSKm + S Initial velocity…
Q: 1. You are studying the enzyme catalyzed reaction below, and you find the KM is 3.3x104 M,. You also…
A: The Michaelis-Menten equation will be Vo = Vmax [S] / {Km + [S]} (1) and kcat = Vo / [ES]…
Q: Án enzyme that follows Michaelis-Menten kinetics has a KM value of 3.00 µM and a kat value of 181s1.…
A: An enzyme is a type of biological catalyst that aids in the acceleration of chemical reactions.…
Q: What is a word equation for the enzyme catalys phenoloxidase?
A: enzymes are bio catalyst which lower the energy of activation and increase the speed of the reaction…
Q: 41 The following data describe an enzyme-catalyzed reaction (hydrolysis of…
A: We are authorized to answer three subparts at a time, since you have not mentioned which part you…
Q: For a simple enzyme-catalyzed reaction, double reciprocal plots were determined for three different…
A: If ET is increased, Vmax will increase, because Vmax= k2[ET]. But KM= (k-1 + k2); i.e. it is…
Q: Based on the definition of kcat, substitute a value that can be measured and yet still represents…
A: since this is a multipart question, so I will be answering the first question only, kindly post the…
Q: UTSASE is an enzyme that catalyzes reactions that produce bluish-orange saliva in roadrunners. UTSA…
A: Lineweaver-Burk plot, also known as double-reciprocal plot, is the graph plotted for Lineweaver-Burk…
Q: The following questions deal with a fundamental understanding of enzyme catalysis. a. Why is the…
A: Hi! Since you have posted a question with multiple sub-parts, we will solve the first three…
Q: For the following aspartate reaction in the presence of inhibitor, Km = 0.00065 M. Determine Vmax in…
A: Enzymes are usually protein molecules which catalyzes biochemical reaction by decreasing the…
Q: In an enzyme kinetics study, three inhibitors resulted to the following results: Inhibitor ABC…
A: Asked : Type of inhibitor PQR
Q: Suppose that the data below are obtained for an enzyme catalyzed reaction in the presence and…
A: The enzyme kinetics in the presence and absence of inhibitor is determined by lineweaver Burk plot.…
Q: The Michaelis-Menten equation models the hyperbolic relationship between [S] and the initial…
A: Enzymes are the proteinous substance that involves in the catalysis (speed up) of biological…
Q: Michaelis and Menten assumed that the overall reaction for an enzyme-catalyzed reaction could be…
A: Enzymes are bio-catalyst that participate in biochemical process and they are highly specific in…
Q: concentration of each enzyme and with [X] = 1 µM. Which curve corresponds to which enzyme? Explain.
A: Given, the substrate concentration is [X] =1 μM Km of enzyme A = 2.0 μM Km of enzyme B = 0.5 μM
Q: Draw a hypothetical Michaelis-Menten plot for an enzyme reaction (i) without and (ii) with a pure…
A: Enzymes are the class of proteins that elevates the rate of the chemical reaction within the living…
Q: Construct a Lineweaver-Burk plot to answer the following questions: (a) What are the apparent KM and…
A: The Lineweavwe-Burk plot is the plot between 1/[V] vs 1/[S]. Km = -1/ x-intercept Vmax= 1/y…
Q: Suppose that you have isolated the enzyme sucrase (able to hydrolyze sucrose into glucose and…
A: Enzyme is a catalytic molecule that increases the rate of any chemical reaction without being used…
Q: At what substrate concentration would an enzyme with a kcat of 33.0 s-1 and a Km of 0.0046 M operate…
A: The Michali s-Menten kinetics is enzyme kinetics that is common in biochemistry to detect and…
Q: In concerted model, all subunits in the enzyme are either in the low affinity or high affinity…
A: There are two models of allosteric regulation of enzymes:- - concerted model -sequential model
Q: In the scheme for enzymatic catalysed reaction proposed by Michaelis and Menten, the steps involve…
A: Enzymes are biological catalyst. It catalysed almost all biological reactions that…
Q: Suppose that you have isolated the enzyme sucrase (able to hydrolyze sucrose into glucose and…
A: The Michaelis-Menten plot shows the relationship between substrate concentration and velocity of a…
Q: In what way is the observed mode of action of hexokinase consistent with the induced-fit theory of…
A: In enzymology, allosteric regulation is the inhibition or activation of an enzyme by a small…
Q: For the following aspartase reaction in the presence of the inhibitor hydroxymethylaspartate,…
A: A graph between 1/[S] (x-axis) versus 1/V (y-axis) gives a straight-line plot that helps to…
Q: a) Is this reaction better characterized by Michaelis-Menten kinetics or simple mass action? b) What…
A: Enzyme kinetics is used to study the rates of enzyme catalysed biochemical reactions. We can observe…
Q: What are the measures to inhibit the Maillard reaction in undesirable situations. please explain…
A: Maillard reaction is a type of chemical reaction in the field of Biochemistry. It occurs between a…
Q: In this problem, we are asked to complete the following: a) Discover sources other than mushroom…
A: As stated, to get the answers to such questions, one must perform database or internet searches to…
Q: Two experiments were performed with the enzymeribonuclease. In experiment 1 the effect of…
A: Proteins that catalyze all the biochemical reactions in the body are called enzymes. They decrease…
Q: Using the appropriate graph and table above, explain what the R48C mutation appears to be doing to…
A: The rate of reaction when the enzyme is saturated with substrate is the maximum rate of reaction,…
Q: Why do structural analogs of the transition-state intermediate of an enzyme inhibit the enzyme…
A: Transition state structural analogs of enzymes are chemicals with a structure that resembles the ES…
Q: An uncatalyzed reaction has keq=50. in the presence of an appropriate enzyme.the forward rate of the…
A: The enzyme does not change the equilibrium constant (Keq) of a reaction. Hence the value of the…
Q: In the scheme for enzymatic catalysed reaction proposed by Michaelis and Menten, the steps involve…
A: The Michaelis-Menten equation catalyzed by the enzyme catalyzed reaction involves the saturation…
Q: For an enzyme catalyzed reaction, the presence of 5nM of a reversible inhibitor yields a Vmax value…
A: Biochemical reactions are catalyzed by enzymes by binding substrates to their active sites. The…
Q: In an enzyme kinetics study, three inhibitors resulted to the following results: Inhibitor ABC…
A: The rate of a enzyme catalyzed reaction increases with temperature until a point and once the…
Q: The accompanying figure shows three Lineweaver–Burk plots for enzymereactions that have been carried…
A: Enzymes are proteins. They are biological catalysts. Tertiary and quaternary structures are crucial…
Q: Which of the listed effects would be brought about by any enzyme catalyzing the following simple…
A: Introduction: Those compound that increases the rate of the reaction without undergoing any change…
Q: Construct a Michaelis-Menten plot, and a Lineweaver-Burk plot, for all six of these experiments on…
A: Given, For experiment 1, for control with [I] = 0mM Substrate concentration(S) Velocity(Vo) 1/s…
Q: At body temperature (37°C), k of an enzyme-catalyzed reaction is 2.3X10¹⁴ times greater than k of…
A: Given: Body temperature, T = 370C = 310 K let rate constant of catalysed reaction be k' and rate…
Q: From the Lineweaver-Burke plot of an enzyme-catalyzed reaction containing 4 μM total enzyme, you…
A: Hi. Thank you for the question. As per the honor code, We'll answer the first question since the…
Q: In 1966, Ferdinand showed that a random-order ternary-complex mechanism for a two-substrate…
A: Ferdinand in the year 1966 showed that a randon order reaction for the two substrate enzyme…
Q: What TYPE of inhibition is observed in the following: S E S
A: A chemical that binds to an enzyme and inhibits its activity is known as an enzyme inhibitor.…
Q: Consider this intermediate in the derivation of the Michaelis-Menten equation. [E] [S] k-1 + k2 [ES|…
A: Km : The concentration of substrate at which enzyme achieves half Vmax-maximum velocity
Step by step
Solved in 3 steps
- An enzyme-catalyzed reaction has a KM of 20.0 mmol L-1 and Vmax of 17.0 pmol s-1. When a mixed inhibitor is added, the apparent KM is 50.0 mmol L-1 and the apparent Vmax is 5.20 pmol s-1. Calculate α.A particular enzyme-catalyzed reaction has an apparent Vmax = 9.00 nmol s-1 and α' = 3.00 when 2.00 µmol L-1 inhibitor X is present and uncompetitively inhibiting the reaction. Calculate Vmax for the uninhibited reaction in nmol s-1.The accompanying figure shows three Lineweaver–Burk plots for enzymereactions that have been carried out in the presence, or absence, of aninhibitor. Indicate what type of inhibition is predicted based on eachLineweaver–Burk plot. For each plot indicate which line corresponds to thereaction without inhibitor and which line corresponds to the reaction withinhibitor present.
- In an enzyme kinetics study, three inhibitors resulted to the following results: Inhibitor ABC Inhibitor XYZ Inhibitor PQR Without Inhibitor Vmax 40.2 mM/ sec 40.3 mM/ sec 12.32 mM/ sec 65.43 mM/ sec Km 24.3 mM 28.5 mM 24.3 mM 15.7 mM d. Draw the estimated Michaelis Menten Curve of Inhibitor ABC and the curve without the inhibitor.(b) You are investigating the effects of several agents on the activity of alcohol dehydrogenase. The enzyme activity data are shown in the table below. Construct a [substrate] vs. activity plot and a double-reciprocal plot for this enzyme. Be sure to label all axes. Determine the Vmax and KM for AD from the graphs in each type of plot. AD activity (nM/min) AD activity + agent A (nM/min) AD activity + agent B (nM/min) [Alcohol] (nM) 0.1 14 2 0.5 50 7 8. 1.0 65 10 30 2.0 72 12 45 4.0 80 14 62 8.0 85 15 75 32.0 90 16 90Shown below are Km, and Vmax values obtained for an enzyme A which catalyze the transformation of the following substrates. Enzyme concentration used was 0.01 M. Km, mM 0.02 Vmax, mM/min 5.3 Substrate 1 2 1.5 13.7 3 2.6 100 4 0.1 25 0.05 62 1. Which substrate have the highest affinity for the enzyme? Explain. 2. Which will show higher efficiency of converting the substrate to the product? Show solutions and еxplain.
- 1.1)the following data duscribe an enzyme-catalyzed reaction(hydrolysis of cabobenzoxyglycyl-L-tryptophan) Plot these results using a lineweaver-Burk method, and determine values for Km and Vmax. substrate concenrate(mM) Velocity(mM.sec-1) 2,5 0.024 5 0.036 10 0.053 15 0.060 20 0.061 25 0.062 1.2) If the Km of an enzyme for it's substrate remains constant as the concentration of the inhibitor icreaces, what can be said about the mode of inhibition and why? 1.3) calculate the turnover number for an enzyme, assuming Vmax is 0.5M.sec-1 and the concentration of the enzyme used is 0.002M . why is it usefull to know this? 1.4) discuss the mechanism of the bohr effect that occurs during the interactions of Hb with oxygen under physiological conditions in the lungs and tissues. make use of relavant graphs and diagrams to explain your answer.For the following aspartase reaction in the presence of the inhibitor hydroxymethylaspartate, determine Km and whether the inhibition is competitive or noncompetitive. You have to plot thegraph on the graph paper and also by using excel.[S] V, No Inhibitor V, Inhibitor Present(molarity) (arbitrary units) (same arbitrary units) 1 x 10-4 0.026 0.0105 x 10-4 0.092 0.0401.5 x 10-3 0.136 0.0862.5 x 10-3 0.150 0.1205 x 10-3 0.165 0.142In an enzyme kinetics study, three inhibitors resulted to the following results: Inhibitor ABC Inhibitor XYz Inhibitor PQR Without Inhibitor V 40.2 mM/sec 40.3 mM/sec 12.32 mM/sec 65.43 mM/sec max K 24.3 mM 28.5 mM 24.3 mM 15.7 mM b. What type of inhibitor is inhibitor PQR? Why do you say so?
- You will perform the protocol below for the calf intestinal alkaline phosphatase (CIP) provided. For each reaction, your final enzyme concentration should be 10 nM CIP. Note: Enzymes purchased are typically labelled with their “units of activity” (U), as this relates to how much enzyme is needed to catalyze a reaction. The 100 nM CIP provided has approximately 3 U/mL and was diluted 1 in 1,000 from a 500 U/mL purchased enzyme. 1) Create a table (similar to the one below) to help you determine and keep track of what to add to each of the cuvettes in which your reactions will be measured. The five different concentrations of PNPP should be: 25, 50, 100, 200, 300 μM. Each reaction will be in a final volume of 1 mL and contain 10 nM alkaline phosphatase. Concentrations of stock solutions: 1.0 mM PNPP, 100 nM calf intestinal phosphataseThe enzyme β-methylaspartase catalyzes the deamination of β-methylaspartate. For this aspartate reaction in the presence of the inhibitor hydroxymethylaspartate (3.8 M), determine KM and whether the inhibition is competitive or noncompetitive (KI = 1.0 M). In the ABSENCE of inhibitor: The Lineweaver-Burke equation is 1V=1V= __________ (1[S])(1[S]) + __________, and the KM is __________ M. In the PRESENCE of inhibitor: The Lineweaver-Burke equation is 1V=1V= ____________ (1[S])(1[S]) + ___________, and the KM is ___________ M. The type of inhibition is ____________. Round-off all answers to two (2) significant figures.Give an example of a noncompetitive inhibitor and its target enzyme. Draw a hypothetical Michaelis-Menten curves in the presence and absence of the noncompetitive inhibitor. Discuss the effects of noncompetitive inhibition and the reasons for these effects on the values of Km and Vmax.