An enzyme has no activity at an extremely low pH. What could be an explanation for this observation? a. enzyme inhibition b. protein denaturation c. lack of cofactors d. substrate deactivation e. no correct response given

Q: Summarize three ways in which an enzyme might lower the energy of a activation of a raction

A: The three ways in which an enzyme might lowe the energy of activation of a reaction are as follows:

Q: 5: Using the following plot as a standard, how would Vmau Km, and the graphs look when.? Sobtrate…

A: Enzymes are biocatalyst which accelerate the biochemical reactions. Molecules on which enzymes act…

Q: TABLE 2: EFFECT OF TEMPERATURE ON CATALASE ACTIVITY STRENGTH OF REACTION Temperature…

A: The explanation is given below-

Q: The effect of reversible competitive inhibitor can be cancelled by: increasing the product…

A:

Q: Uninhibited enzyme enzyme + inhibitor Substrate Concentration The graph above measures the rate of…

A: For competitive inhibition, enzyme activity should increase with increasing substrate concentration

Q: A non-substrate molecule binds to an enzyme at the active site, causing the enzyme to stop working…

A: A non-substrate molecules binds to an enzyme at the active site causing the enzyme to stop working…

Q: An enzyme whose KM is 10-4 M in the presence of a substrate concentration of 10-2 M It is capable of…

A:

Q: c) Will the rate of the reaction increase, decrease or remain unchanged when additional enzyme…

A: The enzyme substrate reaction takes place in two steps and the reaction mechanism is, The…

Q: Define the optimum pH for enzyme activity.

A: The optimum pH for enzyme activity is defines as follows:

Q: What type of enzyme is affected by the binding of a regulating substance at a point other than the…

A: Enzymes are the substance which increase the rate of reactions by providing the path of low…

Q: 1. How will each of the following changes in condition alter the rate of the enzyme-catalyzed…

A: a. Decreasing the temperature from 37°C to 10°C = Temperature is directly proportional to the enzyme…

Q: Why does an enzyme lose activity when the pH is drastically changed from optimum pH?

A: Enzymes are the catalyst that, within the mild condition of temperature, pH, and pressure of cells…

Q: How is the Km value influenced in the presence of the inhibitor?

A: The Km value is the concentration of substrate that provides the rate halfway to maximum velocity…

Q: Consider the following image depicting enzyme regulation for a two subunit enzyme. Ro Which of the…

A: Enzymes: The enzymes are known as the biological catalyst. Mostly, enzymes are made up of proteins.…

Q: In the experiments of Barrick et al. (as shown), it was observed thatreplacement of histidine by a…

A: Hemoglobins have two alpha chains and two beta chains. When oxygen binds hemoglobin, there is a…

Q: From the given activity,  1.) What is the effect of temperature to the enzyme? 2.) What are some…

A: Hi, we are supposed to answer one question. To get the remaining questions solved please mention the…

Q: Concentration, uM Vo (umol/min) w/o Vo (umol/min) with substance B substance B 0.4 0.08 0.069 0.7…

A:

Q: 10. Applying the Michaelis-Menten Equation II An enzyme catalyzes the reaction M N. The enzyme is…

A: The Michaelis -Menten equation is shown below: Where; [E0] = enzyme concentration Vmax = maximum…

Q: How is the maximal rate of the enzyme changed in the presence of an inhibitor?

A: Maximum rate of reaction is characteristic of a particular enzyme at a particular concentration and…

Q: If you wanted to decrease the deltaG of an enzyme-catalyzed reaction and could make only one change,…

A: Gibbs free energy is the free energy difference between the products and reactants of a chemical…

Q: OH HNL CN R' + HCN One of the proposed mechanisms for this enzyme is shown in the scheme below.…

A:

Q: When designing a competitive inhibitor, why might the substrate, transition state, and product of an…

A: Answer -  competitive inhibitor - According to the question - In competitive inhibition, an…

Q: ular features that stabilize structure. 4. You perform Michaelis-Menten kinetics on (i) trypsin and…

A: a. Specific constant of the enzyme is the indicator of efficiency of the enzymes. The more is the…

Q: (a) What is the difference between a zymogen and an allosteric enzyme? (b) Why would the active…

A: (a)  the difference between enzyme and zymogen  is that enzyme is a globular protein that catalyses…

Q: 8. Identify the inhibitor from the following list for the selective target of the enzyme having C in…

A: o Acrylamide groups act as Michael acceptors and thus react with nucleophiles like thiol (SH) groups…

Q: Explain why an irreversible inhibitor of an enzyme might be more toxic to humans than a reversible…

A: Enzyme are the biological catalyst. The inhibitor is the molecule that binds to an enzyme and…

Q: 6.) Vmax represents the rate of reaction for an enzyme-substrate pairing under what conditions? B)…

A: Value of Michaelis constant (km) tells about the affinity of enzyme to the substrate.

Q: Match each enzyme with the correct substrate. Enzyme Substrate lactose maltose fumarate lactate…

A: Enzyme reaction with substrate are as follow.

Q: A type of enzyme regulation, where a product acts as an inhibitor molecule, iscalled inhibition. a.…

A: In end product inhibition, end product acts as an inhibitor molecule.

Q: What do we mean when we say an enzyme is saturated with substrate? When an enzyme is saturated with…

A: Introduction- Enzymes are proteins that act as biocatalysts in the living organisms. Active sites…

Q: .) If the optimum temperature of a particular enzyme is 33°C, which of the following will likely…

A: Ans (E) Optimized temperature of the enzyme is the maximum temperature at which enzyme shows maximum…

Q: Allosteric proteins a) contain distinct regulatory sites and have multiple functional sites. b)…

A: e) All of the above.

Q: irreversible enzyme

A: Enzyme inhibitors are the chemical compound that decrease the rate of velocity of an…

Q: A. Determine the type of interaction and what protein residues for the phenyl ring labeled 1. B.…

A: A question based on intermolecular forces, which is to be accomplished.

Q: Match the words in the left column to the appropriate blanks in The sentences on the right. Reset…

A: In the protein synthesis the inhibitors are the one which delays or stops the growth or…

Q: At what pH.do the following enzymes work best? 1.2 Sucrase 0.8 E 0.6 0.4 0.2 10 15 pH a. Sucrase: b.…

A: a) Sucrase = The given enzyme work best at pH 6.0.

Q: You are purifying an enzyme and notice that your sample has a lower activity at each step, yet the…

A: We know that the specific activity indicates how much of the total protein is the enzyme we are…

Q: - MULTIPLE CHOICE - Please answer properly QUESTION : Which of the following best describes the…

A: Introduction :-  Catalyst :-  Catalyst is a substance which increase the rate of reaction without…

Q: For an enzyme that obeys Michaelis-Menten kinetics, which one of the following best indicates a…

A: Given: Vo = (1/3)Vmax

Q: H20 A: Name? N- B: Enzyme? N' H. ZI

A: Given as,

Q: An enzyme has an optimal pH of 7.1 and an optimal temperature at 37° C. Which statement describes a…

A: Given, An enzyme has an optimal pH of 7.1. An optimal temperature of 37oC. At a constant temperature…

Q: An enzyme catalyzes the reaction M ⇌ N. The enzyme is present at a concentration of 1 nM, and the…

A:

Q: Q 21: After the substrate diffuses with the enzyme, the next action in series is the A. amino acids…

A: In this question, we have to find out the correct answer of given problem by the help of the…

Q: 17.) In the left graph below, the dashed line (- - - -) represents what? В) Km A) Vmax C)…

A: Vmax is the maximum rate of reaction when enzyme reacts with substrate and Km is the Michael's…

Q: The Km value of an enzyme is affected in the presence of a competitive inhibitor because it requires…

A:

Q: A substance that can bind to an enzyme at a location other than the active site and increase or…

A: A substance that can bind to an enzyme at a location other than the active site and increase or…

Q: 460 410 360 310 260 210 160 110 60 -10 -510 4 5 10 15 20 25 30 35 40 45 50 55 1/[S] per mM 1. What…

A: Michaelis Menten equation shows the effect of the concentration of the substrate on the rate of an…

Vitamins and Coenzymes

A class of organic compounds needed in the human body for normal activities is known as vitamins. They are characterized into two parts depending upon their solubility in water. They can act as coenzymes, cofactors, or prosthetic groups for enzymes.