9. Devise a reaction path for the following synthesis. Indicate any required reagent(s) and show the structures of the major product after each step. Do not give mechanism/arrow pushing. Br OH CH2CH3
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- 6. Consider the reaction: H H SCOA a. What kind of reaction is being performed here? b. What enzyme performs this reaction? c. What cofactors, if any, are required for this reaction? H H SCOAa. Why is it important to eat food containing antioxidants? Write at leasttwo reactions to prove the answer. b. Write in four ways the following nucleotide sequence: ATGCA. c. Explain i. Hoogsteen pairing & ii. Hyperchromic effectiii. Epimers Iv. Mutarotaton v. Aldose vi. Anomers vii. Mutarotation2. a. Label the following structures as ATP, ADP, AMP, P₁, PPi, or Adenosine. Place your answers in the boxes provided. HO H OH H OH OH O N. H H OH + ATP NH₂ . + ADP 01210 ++++++ O-AMP O O Adenosine *+-+ O 0=210 HO b. Put an "X" in the box for the reaction that is thermodynamically most favorable. OH OPP OPP Adenine + AMP + Adenosine
- 1. 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.12 Determine the type of biochemical reaction that occurs in the reaction shown below. O O O O O redox isomerization group C-C bond formation/cleavage transfer hydrolysis/condensation Previous Ex-xx-xx OH (ATP) OH OH OH OH + AMP OH OPO₂² OH OH +AMP1 OH (ADP)Can the target compound at right be efficiently synthesized from the starting material at left? Br starting material Br ? Br target If so, draw a synthesis below. If no synthesis using reagents ALEKS recognizes is possible, check the box under the drawing area. Be sure you follow the standard ALEKS rules for submitting syntheses. More... Br : ☐ T Add/Remove step X Br G Br ос E ol Ar
- 5Which 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.Lysosyme catalyzes the hydrolysis of the carbohydrate linkage in part of the bacterial cell wall (peptidoglycan layer). 1. Propose a mechanism using general acid/base catalysis 2. Propose a mechanism using covalent catalysis. (An intermediate has been observed that indicates a glycosidic bond to the aspartate).
- 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 SeriosShown below is a substrate for a Trypsin. Draw the mechanism for this serine protease using the artificial substrate. Be sure to draw the catalytic triad, and show the role of the oxyanion hole. Draw the complete structure of every intermediate and product and PUSH ARROWS!!!!! Do not abbreviate structures using R and R' H₂N _N_CH. сно CH₂ CH₂ CH₂ NH d=19H₂ NH₂ O CH- H₂C HN O CH2
