Concerning enzymatic activity, a larger Km value indicates a/an: Select one: O lower affinity for its substrate O inhibitory process O larger enzyme O larger Vmax O greater affinity for the substrate Which is the least common type of chemical bond? Select one: O Hydrogen O Peptide O Covalent Olonic O Disulphide D-gluconic acid is: Select one: O an integral membrane protein O a codon O an oxidized sugar O phosphorylated O a large lipid molecule
Q: Which of the following statements regarding enzyme function is false? U A) An enzyme's function…
A: Enzymes are proteins which can act as a catalysts. They can decrease the activation energy needed…
Q: An allosteric inhibitor does which of the following? a. Binds to an enzyme away from the active site…
A: The allosteric inhibitor binds to an enzyme at a site other than the active site. The shape of the…
Q: What docs an allosteric inhibitor molecule do? O It causes the active site of an enzyme to have a…
A: “Since you have asked multiple question, we will solve the first question for you. If you want any…
Q: KM is— a measure of substrate turnover. the rate at which the enzyme binds the…
A: Enzymes refer to the protein that functions as the biological catalyst. It comprises the active site…
Q: Which of the following statement about the enzymes is (are) true : i. Enzyme speed up the reaction…
A: Those proteins or biological catalysts which help to speed up the chemical reaction are termed…
Q: The effect of a competitive inhibitor can be reversed by O changing the pH O heating the reaction…
A: Viruses are simple, noncellular entities consisting of one or more molecules of either DNA or RNA…
Q: Use the given representations for an enzyme and substrate to illustrate the difference between the…
A: Enzymes are biomolecules that help in the catalysis of a reaction by binding to a substrate on the…
Q: Which of the following types of inhibitors binds to the active site of an enzyme? Select one: a.…
A: Inhibitors are the substances that bind the enzyme and decrease the catalytic activity of the…
Q: Which statement incorrectly describes kcat. O It relates to substrate concentration at Vmax. O It is…
A: You have asked two questions. I will answer 1st question, as per guidelines. Asked : Incorrect…
Q: Item: Statement: a) Active site b) Induced fit c) Enzymes d) Enzyme-substrate complex 1. Decreases…
A: Metabolic activity is constant in living things. All live cells are constantly undergoing thousands…
Q: Describe how the enzyme-substrate complex lowers the reaction's activation energy.
A: An enzyme is a substance that decreases the reactants' activation energy to enable a reaction to…
Q: Refer to graph D, the graph level off art point B because.* A D The enzyme is beginning to denature…
A: Enzymes are proteins whose activity is affected by factors that disrupt protein structure, or affect…
Q: Which of the following is incorrect? a. Without an enzyme, reaction rate can be increased by…
A: Enzymes are the catalysts of biochemical reactions that increase the rate of reaction. Enzymes have…
Q: Doubling the concentration of enzyme will the Vmax and the KM- O double, double O halve, halve not…
A: Introduction: Those substances that increase the pace of the reaction without undergoing any change…
Q: -Inhibitor +Inhibitor [S] (mM) Vη&νβσπ:(μmol/sec). V0&νβσπ&ν βσπ (μmol/sec) 0.0001 33 17 0.0005 71…
A: Km is the michaelis menton constant which is a substrate concentration at half Vmax. This can be…
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: A noncompetitive inhibitor (Circle one). a. Binds at the active site of the enzyme. b. Alters the…
A: During enzyme inhibition the inhibitors are bind to the enzyme and inhibit the activity of enzyme.…
Q: Which of the following statements about enzyme character-istics is true?(a) Enzymes generally…
A: Enzymes are biocatalysts that accelerate the rate of biochemical reactions. If there are no enzymes…
Q: All of the following statements about competitive and non-competitive inhibitors are true EXCEPT:(a)…
A: Enzyme Regulation -- Enzyme regulation is done by other molecules which either increases or…
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: (s) mM
A: Given graph is a double reciprocal plot or Lineweaver plot. The graph is plotted between reciprocal…
Q: Enzyme X and enzyme Y catalyze the same reaction and exhibit the νo versus [S] curves shown below.…
A: Enzyme kinetics reaction comprises of the interaction between the enzyme and the substrate…
Q: Under conditions where this enzyme is saturated, which parameter will change significantly as you…
A: Saturation of enzyme means all the enzyme molecules are occupied by the substrate molecule. No free…
Q: Which of the following statements regarding competitive enzyme inhibition is correct? O The…
A: Enzyme inhibitors are the substances that bind to enzyme either at active site or allosteric site…
Q: nthe foilowing figure, one of the following statemants is FAISE With Inhibitor 1Wmax Without…
A: Enzymes are protein molecules that increase the rate of reaction by decreasing the activation energy…
Q: When testing the effect of substrate concentration on the reaction rate, there comes a point at…
A: Enzyme-substrate reaction Enzymes are the biological catalysts that increase the rate of reactions.…
Q: Label the graph for 'no inhibitor' to show the position of V,½V K State the effect that inhibitor A…
A: Enzyme catalysis a reaction where substrate is converted into product with a minimal activation…
Q: Write Cif only statement A is correct, Hif only statement B is correct, Eif both statements are…
A: Enzymes are proteinous compounds. They act as catalysts for biochemical reactions. Like inorganic…
Q: What factors might affect the rate of enzyme action (slow it down)? O Temperature O pH O None of…
A: Both A and B(Temperature and PH) can affect the rate of enzyme action
Q: Allosteric enzyme activator binds. Any site on enzyme .a O surface none of the options is .b O…
A: Allosteric enzymes are the enzymes that change its conformation and thus its activity if some…
Q: After a HUGH meal, which of the following is most likely to occur in the body? (substrate] >…
A: Enzymes are a type of protein acting as a catalyst for biochemical reactions, they fasten the…
Q: Which of the following enzymatic regulation mechanisms involves direct interaction between substrate…
A: Protein catalysts are known as enzymes. A catalyst is a substance that speeds up the rate of a…
Q: I Shown below is a plot of the rate of enzyme reaction to substrate concentration, where a substrate…
A:
Q: If a drug is built to bind to the active site of the enzyme, it will prevent substrate binding. This…
A: Enzyme are biocatalysts that enhance the biochemical reactions in our body. They are made up of 2…
Q: -Inhibitor +Inhibitor [S] (mM) Vο&νβσπ: (μmol/sec). Vο&νβσπ:&νβσπ: (μmollsec) 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: Write Cif only statement A is correct, Hif only statement B is correct, Eif both statements are…
A: The chemical substance that are attached to enzyme and slows down / Inhibit the function of enzymes…
Q: Which figure represents the non- competitively inhibited enzyme? Figure 1 Suhatrate Product Enzyme O…
A: Enzymes are essential components of all metabolic processes in the body. They are catalytic…
Q: Choose the plot that best reflects the activity of an enzyme inhibited irreversibly. 100% A B C D…
A: Enzyme inhibitors are the substances that bind to enzyme either at active site or allosteric site so…
Q: An enzyme catalyzes the reaction MN. The enzyme is present at a concentration of 0.0000000022 M, and…
A: Enzyme catalyzed reaction involves the binding of enzyme to substrate leading to the formation of…
Q: The enzyme becomes denatured if the temperature is compared to its optimal temperature: O a. Too low…
A: Enzymes are the biomolecules that act as a catalyst in the biochemical reaction and can increase the…
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: 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: What is the minimum and maximum pH in which Enzyme X will work? What is the optimal (best) pH? Rate…
A: The enzymes are proteinaceous molecules that helps in accelerating the rate of the reaction that is…
Q: Which statement BEST explains why enzymes bind to specitic substrates? O An enzyme can be inhibited…
A: The biocatalysts, enzymes are proteins that accelerate a chemical reaction. The enzyme act on a…
Q: The inhibition that make permanent damage to an enzyme is called: O Noncompetitive O Competitive O…
A: The enzymes are biocatalysts. These work as biochemical catalysts and catalyze different reactions…
Q: Which of the following is true for competitive inhibition? A) The affinity of the enzyme to its…
A: competitive inhibition: The binding of the inhibitor to the active site of the enzyme preventing…
Q: Which statement BEST explains why enzymes bind to specific substrates? An enzyme can be inhibited so…
A: Different amino acid sequences cause variations in the shapes of an enzyme's active sites.
Q: Competitive inhibitors are: Select one: O a. bind to another part of an enzyme and making the active…
A: Inhibitors are molecules that bind to enzyme and block it's activity. Enzymes inhibitors are…
Q: What does the Km of an enzyme measure? The affinity (strength of binding) of an enzyme for its…
A: The enzymes are biological catalysts that enhance the rate of the reaction. The enzymes lower the…
Q: How does a non-competitive inhibitor decrease the rate of an enzyme reaction? O A. by binding at the…
A:
Step by step
Solved in 5 steps
- Which of the following statements are correct about the thermodynamics of protein folding (select all that appy)? A. The deltaG for protein folding is negative B. Burial of hydrophobic side provides a positive entropy change that drive protein folding C. The overall entropy change of protein folding is favorable D. Intercations between amino acids provide a large negative deltaH that helps favor the native state. E. The free energy change of protein folding is dependent on the temperatureA simple enzyme reaction can be described by the equation e + s ↔ es ↔ e + p, where e is the enzyme, s the substrate, p the product, and es the enzyme– substrate complex.Why would this equation be an inappropriate description of channel function?Chymotrypsin is a pH dependent protein. Enzymatic activity is the greatest between pH=7.0 to pH=8.5. Which residue in the active site would be most affected by decreasing the pH below this range? Explain.
- In an enzyme's active site, a catalytic histidine residue abstracts a proton from the hydroxyl group of a catalytic serine residue. The catalytic serine then performs a nucleophilic attack on the carbonyl carbon of a peptide bond (on the substrate). The final products of this reaction are a cleaved substrate at the peptide bond, with a new amino group and carboxyl group, and regenerated catalytic residues. In this reaction, the serine residue is displaying what? A. Proximity and Orientation B. Covalent catalysis C. Metal ion catalysis D .A and B E. B and C F. None stated hereAmino acids that potentially can participate in acid-base catalysis in an enzyme active site, by accepting or donating a proton, can be: a. Asp, His, Lys b. Ala, Gly, Val c. Asp, Gly, Val d. Ala, Ile, GlyWhich of the following statements about enzyme character-istics is true?(a) Enzymes generally exhibit a high degree of specificityfor one particular substrate.(b) Enzyme-substrate complexes occur when a substratemolecule collides with the allosteric site of an enzyme.(c) Chemical bonds within a substrate are strength-ened when this substrate forms an enzyme-substratecomplex.(d) Enzymes have a region called the active site, which pro-vides an area where it can form a loose association withits substrate.(e) a and d.
- a. Protein X can be phosphorylated. Why would the phosphorylated form of protein X elute AFTER the unphosphorylated form from an ANION exchange column? Please describe in terms of: The chemical properties of phosphorylation modification b. The chemical properties of an anion exchange column and how it works c. Why is an inhibitor that mimics the transition state more effective at enzyme inhibition than an inhibitor that mimics the substrate? d. Protein X can be covalently modified with many methyl groups. What two general properties would be different between the unmethylated protein versus the methylated protein?Which statements are true? Protein-protein interfaces are most often dry. The exclusion of water results in an unfavorable loss in rotational-translational entropy. The free energy change associated with the formation of an enzyme-substrate complex almost always results in an unfavorable reduction in conformational entropy of the proteins. So-called van der Waals’ interactions are essentially electrostatic in origin. Steric complementarity of the two partners forming a complex is essential to achieve optimal free energy of binding. Structural models of proteins obtained from low temperature crystallography are excellent descriptions of all biochemically relevant aspects of their function.Imagine that you are working with isolated mitochondria and you manage to double the ratio of protons outside to protons inside. In order to maintain the overall Gat its original value (whatever it is), how would you have to change the mitochondria membrane potential?
- A simple enzyme reaction can be described by the equation e + s ↔ es ↔ e + p, where e is the enzyme, s the substrate, p the product, and es the enzyme– substrate complex.Write a corresponding equation describing the workings of a transporter (T) that mediates the transport of a solute (s) down its concentration gradient.Figure 6-33 (Subunit interactions in an allosteric enzyme, and interactions with inhibitors and activators) depicts allosteric modulation of an enzyme through non-covalent interactions. What features of an activator might lead to different levels of enzyme regulation? Select one or more: a. ability to cause a conformational change that results in an altered activity. b. affinity for the regulatory site c. boiling point d. bond flexibility (i.e. abundance of freely rotating single bonds instead of more rigid bonds like double bonds) e. molecular weightA generalized enzyme active site is shaped like a hemisphere with a radius of 45Å. The active site holds the following amino acids in a homeostatic solution (pH = 7.38): -HAVARILKHAVARILKHAVARILK- Assuming the charge is distributed uniformly along the hemisphere, determine the force at which this active site acts upon a single ATP molecule at the center of the hemisphere.