What is the minimum and maximum pH in which Enzyme X will work? What is the optimal (best) pH? Y X 1 2 3 45 67891011121314 pH Rate of Enzyme Action
Q: In metalloenzymes metals are Attached to enzyme through coordinate bonds. o Covalently attached to…
A: A coordinate bond is a covalent bond which formed by sharing a pair of electrons. It is also known…
Q: The line does not cross the X-axis when the Y-variable is equal to zero 1점 because Why does this…
A: The picture is showing the graph between the rate of a reaction and the enzyme concentration.
Q: Which of the following statements about competitive inhibitors of an enzyme catalyzed reaction is…
A: Enzymes are the molecules with speed up the rate of a biological reaction without being consumed in…
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: Enzyme C Substance X + Substance Y Substance W What data should be collected to support the…
A: Note: According to the guidelines, we are supposed to answer only one question. Please repost other…
Q: the enzyme and substrate should be mixed only when the reaction is initiated (when the absorbance…
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Q: 10 20 30 40 50 60 70 80 Temperature (°C)
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Q: which of the following is a primary function of the active site of an enzyme?
A: Given: Enzymes are the largest and most specialised class of protein molecules. They are composed of…
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A: Note: Since you have posted multiple independent questions in the same request, we will solve the…
Q: True or False In the presence of enzymes, the value of free energy of activiation (delta G°‡) for…
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Q: Define
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Q: -Inhibitor +Inhibitor [S] (mM) Vη&νβσπ:(μmol/sec). V0&νβσπ&ν βσπ (μmol/sec) 0.0001 33 17 0.0005 71…
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Q: Given the active site and reaction mechanism below, what is the mechanism of irreversible inhibition…
A: The given example is uncompetitive inhibition. Uncompetitive inhibition, also known as…
Q: 8). Which statement best describes 1 point the enzyme represented in the graphs? * O 10 20 30 40 60…
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Q: 0 10 20 30 40 50 60 70 temperature / °C a. What is the optimal temperature for this enzyme? b. What…
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Q: Why does an optimal pH promote enzyme activity
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Q: Carboxylesterase 0 1 2 3 4 5 6 7 pH Enzyme activity -
A: Carboxylesterases are a group of enzymes that hydrolyze compounds containing a functional group such…
Q: Which of the following can cause the rate of enzyme activity to increase? Increasing the temperature…
A: Catalysts are those substances that increase the rate of the reaction without undergoing any change…
Q: In which figure (s), the type of inhibition is reversible? Substrate Figure 1 O Figure 1 O Figure 2…
A: The active site of the enzyme is the site where the specific substrate can bind according to the…
Q: You measure the initial rate of an enzyme reaction as a function of substrate concentration in the…
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Q: ion of estion udy As you increase the amount of substrate in a reaction (while keeping the enzyme…
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Q: The optimum temperature for enzyme activity in the body: O A. OC B. 10C O c. 40C O D. 60C 47
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Q: Enzyme X and enzyme Y catalyze the same reaction and exhibit the νo versus [S] curves shown below.…
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Q: Environmental Factors and Enzyme Activity LA 15- 10 5- 10 20 30 40 50 60 Temperature ("C) 9 10 11 12…
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Q: Figure 5.7 LLLLA Substrate concentration The graph at the left in Figure 5.7 shows the reaction rate…
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Q: Which of the two graphs, below, represents an enzyme catalyzed version of the reaction Y-->X?…
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Q: 100 increasing enzyme ativity 50 optimum pH 5 6 7 9 10 11 8 pH 20 40 Temperature 1. How do pH and…
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Q: Which factor can impact enzyme activity? Select all that apply. Group of answer choices pH…
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Q: An Eadie-Hofstee plot is shown below for the different types of enzyme inhibition. Match the line…
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Q: Most enzymes are very sensitive to even small changes in pH. Explain why a slight shift to more…
A: Enzymes are very crucial in all reactions in our body for metabolism and catabolism.
Q: Which of the following statements describes an enzyme ALLOSTERIC site? O It is where an inhibitor…
A: Allosteric site is the site that allows enzyme activity to be activated or inhibited by molecules.
Q: Which of the following factors does NOT always alter the activity of the enzyme? Reactant…
A: INTRODUCTION Enzymes Enzymes are biological catalyst. Enzymes are proteins that increase the…
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Q: Identify the type of enzyme inhibition each of the following inhibitor characteristics is associated…
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Q: Which of the following would be required for an irreversible enzyme inhibitor? O lonic interactions…
A: Introduction: Enzyme inhibitors are molecules or compounds that bind to enzymes and reduce the…
Q: Graph #4 Substrate concentration #4, the solid line represents the rate of an enzyme reaction with…
A: An inhibitor is any molecule which binds to the enzyme and decrease its catalytic efficiency.
Q: Which figure represents the non- competitively inhibited enzyme? Figure 1 Suhatrate Product Enzyme O…
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Q: Please choose one of these answers A. An allosteric inhibitor appeared B. There was a dramatic…
A: Enzymes are the molecules which speed up the rate of biological reactions without being consumed in…
Q: kcat is: a measure of the catalytic efficiency of the enzyme the rate constant for the…
A: All biochemical reactions are catalyzed by specialized proteins. They act as catalysts for these…
Q: The apo form of an enzyme: (select all that applies) Group of answer choices Is the cofactor-free…
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Q: Which of the following is NOT TRUE about allostery? O The enzyme changes conformation upon binding…
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Q: Which of the following factors affect enzyme activity? O a. All of the mentioned answers are correct…
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Q: Below which is false about enzyme and catalysis? O Catalytic residues interact with substrates and…
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Q: Identification of the active site of an enzyme: 1.6 The effect of changing pH
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Q: Which of the following statements is true about effect of substrate concentration on enzyme activity…
A: The formation of an enzyme-substrate complex is the first step in enzymatic catalysis. The enzyme…
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- Which of the following environmental conditions may have aninfluence on enzyme activity?a. substrate concentrationb. temperaturec. pHd. All of these are correct.Identify the type of enzyme inhibition each of the following inhibitor characteristics is associated with: 1. An inhibitor that decreases enzyme activity by binding to a site on the enzyme other that the active site. 2. An inhibitor that inactivates enzymes by forming a strong covalent bond of the enzyme acitve site.an enzyme acts on a substrate X. The enzyme exists in four different forms, with different catalytic efficiencies. The table shows the kcatand KM values for each form of the enzyme. If the concentration of substrate X in a solution is 5 µM, which of the four forms of the enzyme is the most efficient? Form of Enzyme kcat (s-1) KM (µM) A 50 10 B 50 1 C 100 4 D 1000 100 a. Form A b. Form B c. Form D d. Form C
- What are the description of the ff?A. Enzyme influence on reactionvelocityB. Effect of temperature onenzymatic activityGive a complete and well descriptive definition of the following:1.1 Enzyme catalysis1.2 Co-enzyme1.3 Negative heterotropic co-cooperativitChoose only the letter, no explanation needed. Enzyme activity is affected by a variety of factors. What factor causes the enzyme to denature if it becomes extremely high? * Choices: A. Water's Effect B. pH C. Temperature D. Activator's Effect An inhibitor binds to the enzyme's active site, preventing the substrate from binding to it. What conclusions can you make from this situation? * A. No reaction occurred B. Non-competitive inhibition occurred C. Enzyme activity occurred D. Competitive inhibition occurred Each enzyme is very selective when it comes to its substrate. What can you conclude from this statement? * A. Any substrate can bind to the active site. B. Enzymes are used up in the reaction. C. Only a specific substrate can bind to the active site. D. Enzymes break down when not used. Lock : Key :: Active Site : _____________________________ * A. Substrate B. Active Site C. Coenzyme D. Cofactor Enzymes only speed up biological functions, so they are NOT used up in the…
- A researcher has measured the initial rate of an enzyme-catalyzed reaction as a function of substrate concentration in the presence and absence of 0.001μM inhibitor. She obtains the following data. What is the Vmax and Km for the "no inhibitor" and "+ inhibitor" experiments. Ans, What would be value of V0 for the "+inhibitor" at [S] = 0.4μM and the inhibitor is most likely a competitive, uncompetitive or mixed inhibitor.Does the enzyme described in each of the following statementsrequire a cofactor to be active?(a) Ni2+ is present in the active site.(b) Addition of FAD allows the reaction to occur.(c) The presence of K+ does not affect the reaction.What would be the turnover number and specific activity of an enzyme (molecular weight=32,000 D) in a reaction. (Vmax= 4 μmol of substrate reacted/min), with enzyme amount = 2 μg
- Which of the following statements is TRUE of enzyme catalysts? for heads up question 2 and 3 are false 1) To be effective, they must be present at the same concentration as their substrate. 2) They can increase the equilibrium constant for a given reaction by a thousand-fold or more. 3) They lower the free energy for conversion of substrate to product. 4) Their catalytic activity is dependent on pH. 5) They are generally equally active on D and L isomers of a given substrate.An Eadie-Hofstee plot is shown below for the different types of enzyme inhibition. Match the line withthe type of inhibition.(a) Line A Inhibition Mechanism. Ans: ________(b) Line B Inhibition Mechanism. Ans: ________(c) Line C Inhibition Mechanism. Ans: ________the amino acid glutamic acid is at the active site of an enzyme. Normally the enzyme is active at pH 7. at pH 4 (higher concentration of H+), the enzyme is inactive. Explain there observations