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- 2. 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 + Adenosine3.) Islandicin is a simple anthraquinone molecule. Propose a biosynthetic pathway of the compound. он он CH3 он1. Consider the following parameters related to an enzyme that follows Michaelis-Menten kinetics for the reaction: k(1) k(2) S ----> ES ----> P k(-1)
- 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 AcetylSCoScheme 1: CH3 HNO,/ H,SO, NaOCI CH, HO, CH,OH / H* NO, HNO, / H,SO, NaOC1 OCH HNO,7 H,SO, он но NO2 NO2 CH,OH / H* OCH 3 CH,OH/H* NO2 1. You decide to perform step three of the green pathway first. You start with 1.81 g of the starting material. After the reaction is complete, you weigh 1.18 g of the product, which is a dry solid. What is the percent yield for the third step of the green pathway? Show all of your work!In the biosynthesis of heme, ring cyclization, isomerization, and decarboxylation reactions take place. Identify the potential intermediates and show the electron flow in the following diagram. HO,C R1 HO2C- -R2 NH HN- но- NH HN- HO2C R R2 unstable intermediate Uro'gen II HO2C Me Me NH HN- -CO2H HN NH Me Me HO2C CO2H Coproporphyrinogen II
- Conversion of glucose-6-phosphate to fructose-6-phosphate is a/an ... reaction Ogroup transfer O aldol condensation isomerization O elimination O redoxWhich 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.10. Chymotrypsin is a serine protease enzyme. The Km for the reaction of chymotrypsin with N-acetylvaline ethyl ester is 8.8*102, and the Km for the reaction of chymotrypsin with N- acetyltyrosine ethyl ester is 6.6*10“ M. catalytic triad Ser 195 His 57 Gly 193 N-H OH R-N- Ca N-H O-C- Asp 102 N-acetyl valine N-acetyl tyrosine Chymotrypsin Active Site a. What is the nucleophile here and how is it activated? b. Which substrate has an apparent higher affinity for the enzyme. c. Propose a reason for the difference in affinity based on the shape of each of the substrates (see active site figure, cleaves on the C-side of aromatic residues).
- 1/Vo 1/[S] with I without I with I with I 1/vo without I *-*- 1/vo without I 1/[S] 1/[S] 3. The above graphs are lineweaver-burk plots that demonstrate how inhibitors affect Michaelis Menten enzymes. For each graph identify the type of inhibition and explain how you determined that this enzyme is kinetically demonstrating this type of inhibition.The dye used to complex with the proteins is:* Coomassie Brilliant Blue Dye G-250 Bromophenol Blue Dye R-250 Bromophenol Blue Dye G-250 OCoomassire Brilliant Blue Dye R-250Reaction Profile 2 Reaction Profile 3 Reaction Profile 1 Reaction Profile 4 Reaction Profile 5 Choices: HO ! Sweet potato tuber extract H. OOH он HO H- H- -OH но. H- OH OH CH,OH OH ÓH ÓH H # Pig liver homogenate CH,OH H- -O- H- -OH H- OH CH,OH
