Which of the following statements DOES NOT describe the enzyme active site? O Itis where the substrate binds. O It coversa large portion of the enzyme structure. Otis where catalysis occurs. Olis wherc an inhibitormay bind.
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- 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 OAn enzyme can organize substrates to be nearby in such a way where the local/nearby concentration of substrate is much higher than the actual cellular concentration of substrate. What phenomenon is described here? Orientation O Proximity Concentration O OrganizationConsider the following diagram of an enzyme capa- ble of interacting with two different substrates, Z and S: Eo ka k on off 'off Es Ez Derive expressions for the rates at which Z and S are transformed by the enzyme.
- 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 trueI 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 plot of 1½5 venut VSL, Glld a Br-weaver Burk or double-reciprocal plot, is a useful tool for identifying the type of Madily each gaph by dragging the endpoints to show the various types of enzyme inhibition. What is the inhibition mechanism for the competitive inhibitor? The inhibisr binde cenly in recemyne The inhibitor bindx only lo cozyme- substrate complexe The inhibike binds tas bath free enzyme and enzyme xubxirale completes with identical binding axolante. The inhibikr binds to both free enzyme and cozyme substrate completes with different binding constants. What is the inhibition mechaniam for the uncompetitive inhibitor? The inhibitor binds only to free ENZYMES. The inhibitor bind is both tree enzyme and enzyme auhdraic compleaca with identical binding coulants. The inhibar binds only in enzyme ubrale complex.ca. The inhibir bindis in bath free enzyme and cxyme aubairale complicaca with dill crcnt binding costanix. LAST Nompumps dve shk with inbibus WHEY Pullie mechanism kot…
- 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 aboveWhich 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 andtemperatureWhat statement about states of the allosteric enzyme is TRUE? The value of KM for the T state is lower than for the R state. O The value of Vmax for the T state is lower than for the R state. O The value of KM for the T state and the R state is the same. The value of Vmax for the T state is higher than for the R state. O The value of KM for the T state is higher than for the R state.
- A prokaryotic species is facing a new environmental stressthat can be ameliorated by a catalytic activity that requiresthe side chain of a unique amino acid derivative called pyrovaline. How would such an organism develop a mechanism for the incorporation of this nonstandard amino acidinto an enzyme molecule? What would be the properties ofthe molecules required to solve this problem?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 onlyIn the following example an enzyme is being inhibited. This is an example of Active site Inhibitor Altered active site O Non-competitive inhibition O Competitive inhibition MacBook Air
