The fractional saturation of an enzyme is 80% at a substrate concentration of 20 mM. In the presence of 5 mM of a competitive inhibitor the fractional saturation at the same substrate concentration is 40%. The Km for this reaction is mM, and the apparent Km is mM. The value of alpha is while the Ki of the inhibitor is mM.

Q: For an enzyme-catalyzed reaction, the presence of 5 nM of a reversible inhibitor yields a Vmax value…

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Q: A researcher has measured the initial rate of an enzyme-catalyzed reaction as a function of…

A: Km and Vmax are important features of an enzyme thatvcan determine the efficiency of the enzyme.…

Q: f the new higher KM value is 0.1 mM resulting in the new plot red curve is due to presence of…

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Q: The graph shows the fractional occupancy of an enzyme's substrate binding site as a function of…

A: Allosteric enzymes have an additional site other than active site or substrate binding site. The…

Q: (a) (c) 1/v + inhibitor 1/[S] (b) + inhibitor X 1/v 1/[S] + inhibitor + inhibitor (d) 1/v 1/V I i…

A: Non competitive inhibition is a type of inhibition where the inhibitor binds to a site other than…

Q: On the graph provided, sketch a plot of Vo/Vmax vs. [S] for an allosteric enzyme, 1.0 0.8 0.6 0.4 02…

A: Allosteric enzymes are a class of regulatory enzymes which increases or decreases catalytic…

Q: Based on the Lineweaver-Burke plot attached.  Kinetic data were generated in the (1) absence of any…

A: Given Values: Y-intercept of A and B = 0.9 secμM Y-intercept of C = 0.3 secμM Slope of A = 1.8 sec…

Q: In an enzyme kinetics study, three inhibitors resulted to the following results: Inhibitor ABC…

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Q: In noncompetitive inhibition, can both the substrate and the inhibitor bind at the same time?  I…

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Q: A substance that is able to interact with an enzyme, reducing its ability to process a substrate, is…

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Q: enzyme reactions

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Q: In an experiment, three batches of the same enzyme were incubated with 5 mM of substrate and 2 mM of…

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Q: The change in the amount of product B in a reaction which is catalyzed by Enzyme A is given in the…

A: Michaelis menten constant, Km= It is the substrate concentration required to produce half maximum…

Q: . The graph below shows Ve vs Vo / [S] for an enzyme-catalyzed reaction. The blue curve was obtained…

A: An enzyme is a substance that acts as a catalyst in living organisms, regulating the rate at which…

Q: A variety of factors influence enzyme activity. Substances that bind to the enzyme and interfere…

A: Enzymes are biocatalyst that increases the rate of reaction. Enzyme inhibition can be of 5 types :-…

Q: Penicillin is an example of what A. Competitive B. Noncompetitive type of enzyme inhibitor? C.…

A: Penicillium affects bacterial growth by inhibiting cell wall synthesis. It is an antibiotic that…

Q: A plot of 1/Vo versus 1/[S], called Lineweaver-Burk or double-reciprocal plot, is a useful tool for…

A: Lineweaver-Burk plot is also known as the double reciprocal plot. Plot between the reciprocal of…

Q: Write C if only statement A is correct, H if only statement B is correct, E if both statements are…

A: An enzyme is a biocatalyst that increases the rate of chemical reaction without itself being changed…

Q: Enzyme Activity vs. Drops of Enzyme 0.030 0 025 0.020 0 015 0.010 0.005 0.000 10 Enzyme (drops) 15…

A: The rate of a chemical reaction increases when the substrate concentration increases. Enzymes speed…

Q: n an enzyme reaction the enzyme has a KM of 72 mM. At which substrate concentration will the rate of…

A: "Since you have asked multiple questions, we will solve the first two question for you. If you want…

Q: Does this figure illustrate competitive or noncompetitive inhibition of enzyme function? How can you…

A: Enzymes are macromolecular biological catalysts that accelerate chemical reactions. The molecules…

Q: You have isolated a dimeric enzyme that contains two identical active sites. The binding of…

A: Enzymes are specialized proteins that catalyze all biochemical reactions in living systems. The…

Q: A mixed inhibitor of an enzyme (sometimes called a mixed non-competitive inhibitor) can decrease the…

A: Inhibitors are those substances that decrease the catalytic activity of an enzyme. It can be organic…

Q: Since KM is an intrinsic property of an enzyme, its value does not depend on the enzyme…

A: Km is the Michaelis constant. It is defined as the substrate concentration at which half of the Vmax…

Q: In the induced-fit model of enzyme action, the active site on the enzyme provides an exact fit for…

A: Enzyme are substances that catalyze chemical reactions. They bind to reactant molecules, called…

Q: Based on the Lineweaver-Burke plot attached.  Kinetic data were generated in the (1) absence of any…

A: Given values: Y-intercept of line A and B = 0.9 sec/μM Y-intercept of C-line = 0.3 sec/μM

Q: A) Competitive inhibition: Where do these inhibitors bind? To what mechanistic form of the enzyme do…

A: The competitive inhibitor is a type of inhibition process in which an enzyme is analogous to the…

Q: Inhibitor X exerts which of the following effects on the above enzyme (lactase)? (inhibitor X…

A: Enzyme inhibition can occur in two ways: reversible and irreversible.  Both results in dissociation…

Q: Based on the Lineweaver-Burke plot attached. Kinetic data were generated in the (1) absence of any…

A: Given Values: Y-intercept of the B line = 0.9 secμM Slope of B line = 0.6 sec

Q: Enzyme X has a Km of 2 µM and a kcat of 104 s1. In the presence of an inhibitor, Km increases to 4…

A: Enzymes are protein molecules that speed up the reactions by decreasing the activation energy.…

Q: The image shows the rate of an enzyme reaction under conditions of no inhibition, competitive…

A: Competitive inhibitors are those which mimic the shape of the actual substrate and binds to the…

Q: In competitive inhibition, increasing concentrations of the inhibitor will have the following effect…

A: When a molecule inhibits the enzyme activity that is called enzyme inhibition and the molecule is…

Q: Based on the Lineweaver-Burke plot attached.  Kinetic data were generated in the (1) absence of any…

A: Three datasets are plotted onto the line-weaver burk plot. One of the lines from A, B, and C…

Q: The concept of “induced fit” refers to the fact that: a. enzyme specificity is induced by…

A: The primary purpose of enzymes is catalysis. Enzymes are extremely effective catalysts. Enzymes are…

Q: the maximal velocity of the reaction the Km value of the uninhibited reaction the Km value of the…

A: Michaelis menten constant, Km is the substrate concentration required to produce half maximum…

Q: In Effect of temperature on ensyme activity lab, what is the negative control?  How does the…

A: While working with enzymes in the lab, optimum temperature of an enzyme can be calculated by…

Q: The Lineweaver-Burke plots of a reaction without inhibitor and one with non-competitive inhibitor…

A: Enzymes are catalysts that enhance the rate of biochemical reactions.

Q: Select the graph that correctly illustrates the effect of a positive modifier (effector) on the…

A: In case of allosteric enzymes they usually have more than one active site that involves binding of…

Q: Consider the Michaelis-Menten equation, below: Vmar S V. k + [S] %3D What is the relationship…

A: [S] : Substrate concentration  V= Vmax[S]/(Km+[S]) Vmax: Maximum velocity  Km: [S] at which V is…

Q: Indicate whether each of the following statements describes a reversible competitive inhibitor, a…

A: A molecule whose shape and charge distribution sufficiently resembles an enzyme substrate is known…

Q: Explain how the following changes affect the rate of an enzyme-catalyzed reaction in the presence of…

A: In uncompetitive inhibition, the enzyme inhibitor binds to the enzyme-substrate complex. This type…

Q: Explain the effect of increasing the substrate concentration in the presence of a non-competitive…

A: Inhibitors of the molecules which affect the activity of enzymes negatively.

Q: An enzyme-catalyzed reaction is studied in the absence and presence of an inhibitor and the…

A: Enzymes are involved in the catalysis of various reactions. There are different classes of enzymes…

Q: Write C if only statement A is correct, H if only statement B is correct, E if both statements are…

A: Enzymes are protein molecules that increase the rate of reaction by decreasing the activation…

Q: In a plot of 1/v vs 1/[S] for an enzyme-catalyzed reaction, presence of a non-competitive inhibitor…

A: Enzymes are protein molecules that increase the rate of reaction by decreasing the activation energy…

Q: The activity of an enzyme is studied with and without an inhibitor. Specifically, the initial rates…

A: With the following details provided you are first supposed to plot a graph between substrate…

Q: What is the relative inhibition of an enzyme by a competitive inhibitor at [S] = KS and [I] = KI?

A: Enzymes are protein molecules that increase the rate of reaction by decreasing the activation…

Q: In a reaction, if the substance concentration equals Km and concentration of inhibitor equals Ki,…

A: Given Values: [S] = Km [I] = Ki

Q: he figure displays the relationship between initial rate of product formation and reactant…

A: in this Figure  At low concentration rate of product formation is directly proportional to…

Q: Using linear regression analysis, determine the values of Vmax and KM of the enzyme in the PRESENCE…

A: Michaelis menten constant, Km is the substrate concentration required to produce half maximum…