Choose the False statement about enzyme binding sites Binding at an allosteric site ca affect binding and catalysis at the Ortho steric site. In addition to ortho steric sites , some enzymes have other sites where catalysis can be conducted. They are called , allosteric sites, from “allo,” the other. In principle, allosteric ligands can have structures that do not resemble those of substrates. Ligand binding at an allosteric site can cause a conformational change of an enzyme. Enzyme can be inhibited by an allosteric ligand that does not complete with substrate

Choose the False statement about enzyme binding sites Binding at an allosteric site ca affect binding and catalysis at the Ortho steric site. In addition to ortho steric sites , some enzymes have other sites where catalysis can be conducted. They are called , allosteric sites, from “allo,” the other. In principle, allosteric ligands can have structures that do not resemble those of substrates. Ligand binding at an allosteric site can cause a conformational change of an enzyme. Enzyme can be inhibited by an allosteric ligand that does not complete with substrate

Biology: The Dynamic Science (MindTap Course List)

4th Edition

ISBN:9781305389892

Author:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Publisher:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Chapter6: Energy, Enzymes, And Biological Reactions

Section: Chapter Questions

Problem 8TYK: Which of the following statements about the allosteric site is true? a. The allosteric site is a...

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Which of the following statements about the allosteric site is true? a. The allosteric site is a second active site on a substrate in a metabolic pathway. b. The allosteric site on an enzyme can allow the product of a metabolic pathway to inhibit that enzyme and stop the pathway. c. When the allosteric site of an enzyme is occupied, the reaction is irreversible and the enzyme cannot react again. d. An allosteric activator prevents binding at the active site. e. An enzyme that possesses allosteric sites does not possess an active site.
1. Please fully explain (use illustrate where appropriate) the Modes of Enzyme Catalysis exemplified by the serine protease: Chymotrypsin. In your answer discuss employing the illustration whenever possible: the overall reaction mechanism, stability of the reaction transition state, proximity and orientation effects, acid-base catalysis, and covalent catalysis. (c) (0) Ap Asp Toe His Asp 10 C-N bond cleavage HN Ho Ser Ger Binding of substi 196 Ser Gly alto video LBHB NH Sere HAR Proton donation by H (h) Fel of amino product yest OHN Hig Ser Ap (0) Formation of covalent (ES) Alp Me complex Serios
1.The class of enzyme that catalyzes addition of a group to a double bond is? oxidoreductases lyases ligases isomerases hydrolases transferases 2. Suppose an enzyme and its substrate obey the lock and key model of enzyme catalysis. Which of the following would be true of the enzyme? the active site of the enzyme must be rigid the active site of the enzyme must be flexible only one substrate could be converted to product by the enzyme the enzyme could bind different substrates if the substrates shared a common motif somewhere in their structures the entire enzyme must be rigid 3. Which of the following enzymes is found in blood serum and is diagnostic of prostate cancer if enzyme levels are elevated? alanine aminotransferase phosphohexose isomerase lactate dehydrogenase acid phosphatase alkaline phosphatase 4. A blood test returns elevated aspartate aminotransferase levels. You suspect that the patient has suffered a heart attack. What other serum enzyme level of…
On the figure below are shown three Lineweaver-Burk plots for enzyme reactions that have been carried out in the presence, or absence, of an inhibi- tor. Indicate what type of inhibition is predicted based on each Lineweaver- Burk plot. For each plot indicate which line corresponds to the reaction without inhibitor and which line corresponds to the reaction with inhibitor present. 1 1 1 [S] [S] [S]
Allosteric Inhibitors ● are constructed of level of protein polypeptide chains (demonstrating on each polypeptide. structure) with an ● The enzyme moves back and forth between an active state and an inactive state ● If a substance binds to the allosteric site and puts the enzyme into the active state, that substance is called an ● If a substance binds to the allosteric site and puts the enzyme into the inactive state, that substance is called
6. Sweetzyme® IT Extra is a trademarked immobilized enzyme formulation of glucose isomerase sold by the Danish company Novozymes. The following reaction is carried out in a 4.0 L reactor in the presence of an non-competitive inhibitor, I: E + G EG = 2 => E + F EG+1 EIG G=glucose, F = fructose The Sweetzyme beads added to the reactor have a total surface area, a = 342 cm². Kinetic Parameters k₁ = 0.00820 M₁¹ S¹ k.₁ = 0.00190 s¹ k₂ = 0.570 s¹ Initial/Total Enzyme concentration: Initial Bulk Substrate Concentration: Mass transfer coefficient, Eo 2.30 x 105 M Sb = 0.152 M k₁ = 9.15 x 10 cm/s A. What is the maximum reaction velocity with no inhibitor (in mol/L-s)? (recall that Rapid Equilibrium and Quasi steady state approaches predict the same value for Vmax for this mechanism) B. What is the maximum reaction velocity (in mol/L-s) with the non-competitive inhibitor, I, at a concentration of [1] = 0.0029 M, with K₁ = 1.8 x 10³ M. C. Calculate the Dahmköhler number to determine if the…
Which of the following statements regarding enzymes and transition states is true? stabilization of the transition state must be less than stabilization of ES for catalysis to occur binding of substrate to an enzyme often causes strain, thus promoting transition state formation the transition state conformation of an enzyme catalyzed reaction is identical to the conformation seen in the uncatalyzed transition state formation of the transition state always assures that the reaction will proceed to product none of the above are true
The following statements refer to enzyme inhibition. Match the statement to the one of the following descriptors to which it is best associated. Descriptors: competitive inhibition; non-competitive inhibition; un-competitive; covalent inhibition. 9a. Inhibition is not reversed even after the inhibitor (1) is removed from solution by dialysis or drug metabolism/excretion. 9b. Inhibitor and substrate reversibly compete for occupancy of a common binding site 9c. The inhibitor binds reversibly only to the preformed E.S (enzyme-substrate) complex forming an inactive E.S.I. 9d. The inhibitor binds reversibly and independently of substrate to an allosteric site producing E.I or a ternary E.S.I complex which can't form product. 9f. The relative amount of inhibition decreases as [S] (the concentration of substrate) increases and S better competes for occupancy of the active site.
Competitive inhibitors have been developed as pharmaceuticals are not naturally occurring must be identical in shape and charge to the enzyme's natural substrate prevent the enzyme from binding its natural target even in the presence of an excess of that natural target
Although we have introduced catalytic strategies separately, an enzyme typically employs more than one during a reaction. The catalytic strategies employed by serine protease include: Select one or more: O a. reduction of ASt b. transition state stabilization Oc. metal-assisted catalysis O d. acid/base catalysis O e. covalent catalysis
The diagram below shows the substrate binding cleft for a protease, providing the substrate structure, and indicating the residues (using one-letter code) that line the four specificity pockets. F 1 M The protease is known to cleave the amide linkage between W and E residues for substrates containing the WEFD sequence. 1 O Match the specificity pocket (identified by red number) to the residue that occupies it. 3 R Match the specificity pocket (identified by red number) to the residue that occupies it. 4 W 2 1. D 2. E 3. F 4. R 5. W 6. Y
Match the different names for inhibition mechanisms (1-5) with a description of their properties 7a-7d: 1. competitive inhibitor. 2. allosteric inhibitor also known as non-competitive inhibitor. 3. un-competitive inhibitor. 4. affinity label also known as active site directed covalent (irreversible) enzyme inhibitor. 5. Kcat inhibitor, also known as a mechanism-based covalent (irreversible) enzyme inhibitor. 4a. An enzyme inhibitor in which a substrate or competitive inhibitor is modified so that it contains a chemically reactive electrophile which can bind to and subsequently react with the enzyme active site: 4b. An enzyme inhibitor that contains latent reactive group that upon binding followed by catalytic turnover at the enzyme active site produces a reactive electrophile that reacts covalently with the enzyme: 4c. A reversible inhibitor that competes with the substrate for binding to the enzyme active site: 4d. A reversible inhibitor that can bind independently of substrate to its…