Under what circumstances may we believe that KM represents the substrate-enzyme binding affinity?
Q: What is the difference between lock-and-key and induced-fit models for binding of a substrate to an…
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Q: Define a different theories proposed for mechanism of enzyme substratecomplex formation ?
A: Answer: Introduction: Enzymes are biocatalyst enhance the rate of chemical reactions.
Q: Why can we say that having a pure noncompetitive inhibitor present is similar to just having less…
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Q: Why can it be said that the enzymatic action is highly specific?
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Q: What is the impact of the lower value km 0.01 on the affinity of enzyme for substrate?
A: The value of KM is inversely related to the affinity of the enzyme for its substrate. High values of…
Q: Other things being equal, what is a potential disadvantage of an enzyme having a very high affinity…
A: Enzymes are the catalytic proteins that are known to catalyze the reaction and forms the product.
Q: In the absence of substrate, an allosteric enzyme that follows the concerted model has a T/R ratio…
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Q: Can enzyme inhibition be reversed in all cases?
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Q: Under what conditions can we assume that KM indicates the binding affinity between substrate and…
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Q: Show graphically the dependence of reaction velocity on substrate concentration for an enzyme that…
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Q: -Inhibitor +Inhibitor _[S] (mM) νο&νβσπ:(μmol/sec) ν0&νβσπ; &νβσπ;(μmol/sec) 0.0001 33 17 0.0005 71…
A: From the given data, I have calculated 1/S and 1/V0 in absence and presence of inhibitor. The plot…
Q: What do “Eco”, “R” and “I” refer to in the enzyme EcoRI?
A: EcoRI is a restriction endonuclease that cleaves the DNA helix at a specific site called the…
Q: What is the biological purpose of enzyme regulation, i.e., why is it necessary to regulate enzyme…
A: Introduction: Enzymes are biological catalysts that are synthesized by the living cells of the body.…
Q: Why can we say that having a pure non- competitive inhibitor present is similar to just having less…
A: Enzymes are often regulated by feedback inhibition, allosteric regulation, competitive inhibition,…
Q: What are the similarities and differences in the regulation of monomeric, single substrate and…
A: Enzymes are proteins that act as biological catalysts. They work by aiding in reducing the…
Q: Discuss how enzyme, together with its cofactors/ coenzymes, interact with its substrate. How do…
A: Enzymes are proteins that bind to the specific substrate and convert the substrate into a product.…
Q: Distinguish between the lock-and-key and induced-fit models for binding of a substrate to an enzyme.
A: The enzyme-substrate complex is a temporary molecule formed when an enzyme comes into perfect…
Q: How would a change in enzyme substrate concentration from 4mM to 2mM affect Vmax, Km and Kcat?
A: Enzymes lower the activation energy of a reaction. This is done by binding itself to a substrate…
Q: Why does a pure noncompetitive inhibitor not changethe observed KM?
A: The non-competitive inhibitor is a molecule that does not compete with the substrate to get bind to…
Q: What is the explanation for enzyme specificity?
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Q: The Hatch–Slack pathway is an alternative name for _____________.
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Q: What would be the result of an enzyme having a greater binding energy for the substrate than for the…
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Q: Why must enzyme activity be monitored under standard conditions?
A: The enzyme is a biocatalyst where the enzyme attracts subtract for the binding to its active site…
Q: Does the behavior of allosteric enzymes become more or less cooperative in the presence of…
A: Introduction: Cooperativity is a phenomenon where the binding of more than one ligand on a protein…
Q: Distinguish between the lock-andkey and induced-fit models for binding of a substrate to an enzyme.
A: Introduction: Enzymes are proteins that serve as biological catalysts. Catalysts help to speed up…
Q: What is the reciprocal substrate relation in the synthesis of ATP and GTP?
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Q: Each type of enzyme contains a unique, intricately shaped binding surface called a(n) _____________.
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Q: Explain the structural basis for cooperative substrate binding and allosteric control in ATCase.
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Q: What is the evidence for the existence of an enzyme–substrate complex?
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Q: Which of the following is true regarding substrate level phosphorylation?
A: A metabolic reaction which results in the formation of ATP or GTP by the transfer of an inorganic…
Q: An enzyme with a low Km is considered to have a higher affinity for the substrate. Provide…
A: Michaelis–Menten proposed the enzyme kinetics model that describe the characteristics of the…
Q: How would a competitive inhibitor change the Km and the Vmax for an enzyme? Explain why a…
A: A competitive inhibitor is interruption of a chemical pathway owing to one chemical substance…
Q: At which enzyme concentration does all of the available substrate react with the enzyme?
A:
Q: What is the spatial relationship of the critical amino acid residues in the active site?
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Q: On what structural level of the enzyme (primary, secondary, tertiary or quaternary) does the enzyme-…
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Q: Is the term KM used with allosteric enzymes? What aboutcompetitive and noncompetitive inhibition?…
A: Enzymes are biocatalysts that increase the rate of a reaction without getting used up in the…
Q: What effect will competitive inhibitor have on the apparent Km of an enzyme for its substrate?
A: Enzymes are biological catalysts that help in catalyzing or speeding up biological reactions by…
Q: The natural enzyme is recreated by mixing isolated regulatory and catalytic subunits of ATCase. What…
A: Aspartate carbamoyltransferase is the enzyme that catalyzes the first step in the pyrimidine…
Q: How can competitive and pure noncompetitive inhibition be distinguished in terms of KM?
A: Km is also known as Michaelis constant. It is one of the parameters to determine enzyme activity.…
Q: Why does the enzyme activity eventually fall as more PALA is present?
A: The binding of Pala switches ATcase from the T to the R state because PALA acts as a substrate…
Q: What are the main theoretical models that try to explain the formation of the enzyme-substrate…
A: Enzymes can be defined as the are proteins that act as biological catalysts. Catalysts enhance…
Q: What is the evidence that ATCase has distinct regulatory and catalytic sites?
A: Introduction: Aspartate transcarbamoylase(ATCase) is the enzyme that catalyzes the first reaction of…
Q: What is the impact of the higher value of Km on the affinity of the enzyme for the substrate?
A: Those class of proteins that helps in increasing the rate of reactions inside the living body…
Q: How do scientists determine the KM of a substrate that ispart of an ordered reaction with two…
A: Interpretation: The KM value of a substrate that is a part of an ordered reaction with two…
Q: In _____________ inhibition, the EI complex readily dissociates and the enzyme is again available…
A: Enzyme inhibition refers to a decrease in enzyme-related processes, enzyme production or enzyme…
Q: at is the difference between enzyme limited and a substrate limited reaction?
A: Enzymes are substances that are mainly protein which acts as biocatalysts in living organisms and…
Under what circumstances may we believe that KM represents the substrate-enzyme binding affinity?
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- Under what conditions can we assume that KM indicates the binding affinity between substrate and enzyme?What is the impact of the higher value of Km on the affinity of the enzyme for the substrate?What are the main theoretical models that try to explain the formation of the enzyme-substrate complex?
- Which model for enzyme-substrate chemical complementarity is described by the following: Before substrate binding, some enzyme molecules have active sites complementary to substrates and other enzyme molecules have non-complementary active sites. Substrate molecules preferentially bind to the enzyme molecules with complementary active sites. Non-complementary enzyme molecules undergo a structural change to become complementary to maintain conformational equilibrium. a) conformational selection b) induced fit c) lock and key...What is the explanation for enzyme specificity?The initial velocities of two different enzyme-catalyzed reactions were measured over a series of substrate concentrations. The following results were obtained: Enyme A: KM = 1.5 mM, Vmax = 10 μM s-1 Enyme B: KM = 5.0 mM, Vmax = 85 µM s-1 (a) Which enzyme binds to its substrate more tightly (assume k.1 >> k₂ in the Michaelis-Menten model)? (b) Calculate the initial velocities of each reaction when the substrate concentration is 2.5 mM. (c) Calculate the Kcat of each enzyme if the total enzyme concentration is 100 nM. (d) Which enzyme is the more efficient catalyst? Explain your answer. The enzyme carbonic anhydrase is strongly inhibited by the drug acetazolamide. A plot of the initial reaction velocity (as a percentage of Vmax) in the absence and presence of the inhibitor is shown below. What type of inhibition is taking place? Explain your reasoning. V (% of Vmax) 100 50 0.2 0.4 No inhibitor Acetazolamide [S] (MM) 0.6 0.8 1
- In a reaction system, the concentrations of Enzyme-Substrate complex [ES], free enzyme [E] and free substrate [S] are 5mM, 2mM and 45 mM respectively. If the enzyme has 5 identical binding sites for this substrate, then calculate the value of Equilibrium Association constant (Ka).On what structural level of the enzyme (primary, secondary, tertiary or quaternary) does the enzyme- substrate interaction depend?Consider this intermediate in the derivation of the Michaelis-Menten equation. [E] [S] [ES| k-1 + kz km Assume that k is negligible compared to the other rate constants. If the k is very small, it suggests that the enzyme has a Select an option affinity for its substrate, while if the if the km is very large, it suggests that the enzyme has a Select an option. affinity for its substrate. Select an option Submit You have used 0 of high Sav low moderate
- An enzyme that follows the MWC (concerted) model for allostery has a T/R ratio of 300 in the absence of substrate. Suppose that a mutation were to reverse that ratio (T/R = 1/300 = 3.3 x 10–3 in the absence of any substrate). How would this mutation affect the relation between the rate of the reaction and substrate concentration, i.e., what would a Vo vs. [S] plot look like, and why?Explain how the following changes affect the rate of an enzyme-catalyzed reaction in the presence of an uncompetitive inhibitor: (a) increasing the substrate concentration at a constant inhibitor concentration, (b) decreasing the inhibitor concentration at a constant substrate concentration.You have isolated a dimeric enzyme that contains two identical active sites. The binding of substrate to one active site decreases the substrate affinity of the other active site. Can the concerted model account for this negative cooperativity?