ation requires TIP C GIP D. CTP 21. Equilibrium is a state of A Maximum 22. in Exergonic reaction, all of the follin Stability BMinimum D. atability Chntermediate
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Biology section, biology, please solve question 21
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- 7. An enzyme-catalyzed reaction proceeds by the mechanism below: E+S1ES --2E+P E+A 3 EA EA+S4→ EAS --5→ EA + P E+I6 → EI EAS +17→ EAIS -8 EIS + P A. B. C. E = enzyme, S = substrate, I = inhibitor, P = product and A = activator Rate constants (k's) for the forward reactions are: K1, K2, k3, K4, k5, k6, k7, and k8 Rate constants (k's) for the reverse reactions are: k-1, k-3, K.4, k.6, and k.7 Write the enzyme balance for this mechanism. How many total equations will result from applying the RAPID EQUILIBRIUM ASSUMPTION? Using any concentrations of species in the mechanism and any of the rate constants (k's), write ONE of the equations that would result from applying the QUASI STEADY STATE ASSUMPTION. (ONLY ONE EQUATION; ANY OF THEM ARE FINE)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-n f estion B I ut of question PF budy As you increase the amount of substrate in a reaction (while keeping the enzyme concentration the same): Select one: O A. The amount of products formed should decrease OB. The amount of products formed should remain the same OC. The amount of products formed should increase Clear my choice Mixing hydrogen peroxide with an enzyme different than catalase (such as lactase) should also result in the formation of products. Select one: O True O False The temperature at which an enzyme works best can differ from enzyme to enzyme. Select one: O True False B 7 O
- Which 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.7. An enzyme-catalyzed reaction proceeds by the mechanism below: B. E+S1→ ES --2E+P E+A 3 EA EA+S4 EAS --5 EA + P E+I 6 EI EAS+I7 → EAIS -8 EIS + P K. macronutrient L. enzyme activator/cofactor M. liposome N. anaerobic process O. aerobic process E = enzyme, S = substrate, I = inhibitor, P = product and A = activator Rate constants (k's) for the forward reactions are: kı, k2, k3, k4, k5, k6, k7, and ks Rate constants (k's) for the reverse reactions are: k-1, k-3, k-4, k-6, and k-7 Write the enzyme balance for this mechanism. 4 How many total equations will result from applying the RAPID EQUILIBRIUM ASSUMPTION? Using any concentrations of species in the mechanism and any of the rate constants (k's), write ONE of the1. Demonstrate your understanding whether carrier-free biocatalysts should or should not be considered as good biocatalysts. You discussion must be in detail and related to biocatalysis. You can provide detail explanation or provide example. 2. Compare and contrast the following pairs of terms. Relate their similarities and differences to applications in biocatalysis. Zymonomas sp. and Saccharomyces sp.
- 8. Structures of three coenzymes involved in Phase II conjugation reactions are shown below. For each coenzyme, circle the portion of the coenzyme that is transferred during metabolic reaction. NH, CH NH, COO CH, H2C OH CH НО O-UDP HC H H ОН он он UDP-Glucuronate S-Adenosylmethionine (S-AdoMet) SCo AcetylSCo2. Figure 2 illustrates the different between uncatalyzed reaction and catalyzed reaction. Find the following that represents the lowering of the activation energy for catalyzed reaction. * > P AG Q Reactant > R Products Reaction Coordinate Figure 2 A. P--> Q B. P- R C. Q-> R D. Q- S7. To what main enzyme class do the enzymes that catalyze the following reaction belong? (Oxidoreductases, transferases, hydrolases, lyases, isomerases, ligases) со о 8. Label the following as examples of a "lock and key" model or an "induced fit" enzyme model? substrate a. b. tive sihe a. b. yme-bstrate comples
- The role of Zn2+ in catalysis is usually to: a. Stabilize a (-) charge in the transition state O b. Act as a nucleophile Oc. Act as a base Od. Destabilize a (-) charge in the transition state3. b. If chymotrypsin is treated with disopropylfluorophosphate, catalysis cannot occur even in the presence of excess substrate concentration. Is this Inhibltion reversible or Irreversible?. Dilsopropylfluorophosphate Hyd3. How does an enzyme work? (A) Use 3 different colors to color the coding circles and corresponding structures in the figure. (B) Beneath steps 1-3, briefly explain, in your own words, what is happening. 2omysna Ju2io atauoon eu8 3 arit to HA slie EUSAwee se pAbiceph opnyn brorejue Ap su sAG ylsteo of so beeu + uboig s ot slsuas s chrdsetisoinorco O Enzyme O Reactant(s) O Product(s) in resiscpepnselifsa op mm Delits nogieadA noteeguoima fnotlengede bns noltesplb noewied eaneiellib or సూగాత