It is a model which best explains the enzyme-substrate action O A. lock & key B. molecular OC. VSEPR D. Kreb
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- Which of the following statements is/are TRUE about the Lock and Key model of enzyme-substrate interaction? I. The active site of the enzyme has flexible conformation. II. Only a certain number of substrates can fit on the enzyme's active site. O Both I and II O Neither I nor II O I only O II onlyWhich of the following statements DOES NOT describe the enzyme active site? O tis where the substrate binds. O is where catalysis occurs, Ctis wherc aninhibilormay bind.Determine how reaction rate (velocity) varies with substrate concentration. F3 $ 4 Substrate concentration R F Additional substrate is added when substrate concentration is low. F4 % 5 T Rate increases G 6 HOLL F5 & H 7 F6 YU J *00 8 DELL F7 K ( 9 Substrate is added when enzyme is saturated with substrate. F8 Rate decreases O Answer Bank F9 P W F10 { [ + 11 F11 } 1 F12 Additional substrate is added when substrate concentration is high but is not yet saturating. Backspace Rate is unchanged Enter Insert Print Screen Delete Home Scroll Lock End 8:26 PM 2 10/15/2023 + PgUp Pause Break PgDn
- 1. A competitive inhibitor for an enzyme a. b. C. d. e. changes the apparent Km but has no effect on Vmax. alters Vmax but has no effect on Km. is competitive with respect to substrate for binding to the enzyme active site. Answers a and care both correct. Answers b and care both correct.The enzyme acts best at a particular pH; this pH is called: O a. neutral pH O b. acidic pH c. basic pH O d. Optimal pH REDMI NOTE 8 AI QUAD CAMERAe If Km1 > Km2, then the affinity of the enzyme to the substrate with Km1 is: Select one: O a. Lower than for Km2 b. Higher than for Km2 c. None of these O d. Equal to Km2
- Allosteric enzyme activator binds. . Any site on enzyme .a O surface none of the options is .b o correct Enzyme active site .C O Regulatory site .d O Allosteric inhibitory site .e OSelect all statements that are correct. Note there might be more than 1 correct statement. Competitive inhibitors bind to an allosteric side on the enzyme Uncompetitive inhibitors bind to the substrate binding site Competitive inhibitors bind to the substrate binding site Competitive inhibitors are usually of similar size and shape than the substrate of the enzyme Non-competitive inhibitors can bind to the free enzyme but not to the enzyme-substrate complex pe here to search C 6 D 88 20°C T ENGWhich of the folowing types of inhibitors binds to the active site of an enzyme? Select one: a. Competitive b. All of them C. Uncompetitive O d. Noncompetitive
- Which of the following is incorrect regarding the active site of anenzyme?a. is unique to that enzymeb. is the part of the enzyme where its substrate can fitc. can be used over and over againd. is not affected by environmental factors, such as pH andtemperatureI Shown below is a plot of the rate of enzyme reaction to substrate concentration, where a substrate S binds reversibly to enzyme E to form an enzyme-substrate complex ES, which then reacts irreversibly to generate a product P and regenerate the free enzyme E. E+S ES →E+ P For many enzymes, the rate of the reaction increases with substrate concentration, till it reaches a plateau, Vmax because the enzyme is sàturated, or all enzyme molecules are bound to substrate molecules. This is shown below in the graph as curve A. The substrate concentration that gives you a rate that is halfway to Vmax is called the Km, and is a useful measure of how quickly reaction rate increases with substrate concentration. a. Which of the curves B or C Vmax best demonstrates enzyme B. activity in the presence of a competitive inhibitor? Explain briefly why. 1/2 Vmax Vmax -- C b. Which of the curves B or C best demonstrates enzyme 1/2 Vmax activity in the presence of a noncompetitive inhibitor? Explain…A type Il beta turn has what residue as one of the four residues that make up the turn? OAP O B. G C.I O D.A O E. Q Once a substrate is bound to the active site, there are a variety of mechanisms that aid in the cleavage and formation of bonds. Thesa incudn. OA General acid base catalysis by amino acid side chains which can act as proton donors and acceptors. OB. Metal ion catalysis where tightly bound metal ligands can participate in cataus. Oc covalent catalysis where the enzyme forms transient covalent bonds with reactants and these bonds are later broken O D.all of the above E. only A and C The Ramachandran plot describes the peptide conformation by illustrating the position of the dihedral angles that can rotate following. OA side-chain steric hindrance B. restrictions imposed by secondary structure OC. main-chain clashes from the bulky carbonyl oxygen or amide nitrogen with other main-chain atoms or side-chains O D. All of the above E. None of the above