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- 9. The transamination of the amino acid aspartate is catalyzed by aspartate aminotransferase. A) Draw out the mechanism for aspartate aminotransferase - you don’t need to show the subsequent formation of glutamate by the transaminase. B) After transamination, write out the subsequent steps (no mechanisms) to generate a molecule of glucose from two aspartates. How many ATP equivalents would this consume? C) After the transamination, write out the subsequent steps (no mechanisms) to fully oxidize aspartate into CO2 through malate (see above). How many ATP equivalents would this produce?. The optimal conditions for salivary lysozyme (hydrolyzing glycoproteins of bacterial wall) are 37 C - temperature and pH is 5.2. Explain the decrease in this enzyme activity if the temperature will rise up to 60 °C and pH will be changed to 8.0. To answer the question: a) draw the graph of the velocity dependency on temperature and pH; b) calculate the relative enzyme activity if 10 mg of lysozyme catalyzes the formation of 5 uM of the product per 2 minutes. Concidor NH3: 5.2. Consider the enzymatic reaction scheme: Asparagine + H20 Aspartate + NH3: a) calculate the specific activity of the enzyme, if in 30 seconds as a result of a reaction involving 3 mg of the enzyme under optimal conditions (pH 8.0, 37 °C) 75 umol aspartate is obtaincd; b) describe the reasons for the decrease in enzyme activity after incubation for 10 minutes at 70 °C (provide an appropriate graph).
- (i) Describe the mechanism of chymotrypsin in cleaving a peptide bond, highlighting the roles of the catalytice triad for the two phases of the catalytic reactions. Explain the significance of the oxyanion hole for the catalysis. (ii) All serine proteases contain the catalytic triad and these amino acids are positioned in the exact same conformation. Since this is true, why do trypsin and chymotrypsin have such different substrate specificity? What features of the enzyme allow for this situation?2. Prokariotic aldolase are mediated by a Zn2+ and are inhibited by EDTA, eukaryotic aldolases though are inactivated by sodium borohydride. A) Draw out the mechanism of the eukaryotic aldolase and propose a parallel mechanism for the zinc catalyzed prokaryotic reaction. B) Propose a strategy that could be could be used to specifically inhibit prokaryotic aldolases and not eukaryotic?The diagram below shows the substrate binding cleft for a protease, providing the substrate structure, and indicating the residues (using one-letter code) that line the four specificity pockets. 1 M F H₂N K R IZ 2 3 P F S W оо E 4 The protease is known to cleave the amide linkage between W and E residues for substrates containing the WEFD sequence. Using 3-letter code with amino acids linked by a "dash" (ex. GLY-ALA), the N-terminal product is A and the C-terminal product is A
- 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 Serios. The mechanism for lysozyme cleavage of its polysaccharide substrate requires Glu35 in its nonionized form, whereas the nearby Asp52 must be ionized (see the figure below). The pK values for the side-chain carboxyl groups on the two amino acids in solution are virtually identical. a) How can one carboxyl group be charged and the other uncharged in the active site of lysozyme? b) The pH optimum for lysozyme is about 5. Why do you suppose that the activity decreases above and below this optimum? Glu3s NAG Asp52 0-H Glu35 -C Asp52 tri-NAG NAGChymotrypsin, trypsin, and elastase all share the same catalytic mechanism, but have different specificities. (a) These proteases are considered serine proteases because the active sites contain serine, histidine and aspartate. Describe the roles that each of these amino acid residues play in hydrolyzing protein substrates. (b) The active site pockets of chymotrypsin, trypsin, and elastase are shown in the image below. Based on the image, which side chain of the amino acids would they prefer to cleave respectively, Ala, Arg, or Trp? Explain your answers. Val 216 Val 190 Asp 189 Chymotrypsin Trypsin Elastase
- Chymotrypsin, trypsin, and elastase all share the same catalytic mechanism, but have different specificities. (a) These proteases are considered serine proteases because the active sites contain serine, histidine and aspartate. Describe the roles that each of these amino acid residues play in hydrolyzing protein substrates. (b) The active site pockets of chymotrypsin, trypsin, and elastase are shown in the image below. Based on the image, which side chain of the amino acids would they prefer to cleave respectively, Ala, Arg, or Trp? Explain your answers. Val 216KVal 190 Asp 189 Chymotrypsin Trypsin ElastaseWill rate ASAP Which of the following amino acid residues would not provide a side chain for acid-base catalysis at physiological pH? (Assume pK values of each amino acid are equal to the pK value for the free amino acid in solution.) I. leucine II. lysine III. aspartic acid IV. histidine A) I, II, III B) I, II C) I D) II E) I, III25. Overall oxidation of glucose can be represented as (2 Points) Glucose + 2ADP + 2GDP + 4 Pi +8NAD+ + 2FAD + 2H2O-----> 6CO2 + 2ATP + 2GTP +8NADH + 6H+ + 2FADH2 Glucose + 4ADP + 2GDP + 4 Pi +8NAP+ + 2FAD + 2H2O-----> 6CO2 + 2ATP +2GTP +8NADH + 6H+ + 2FADH2 Glucose + 2ADP + 2GDP + 4 Pi +8NADP+ + 2FAD + 2H2O-----> 2CO2 + 2ATP + 2GTP +8NADHP + 6H+ + 2FADH2 Glucose + 2ADP + 2GDP + 2 Pi +6NAD+ + 2FAD + 2H2O-----> 6CO2 + 2ATP + 2GTP +6NADH + 6H+ + 2FADH2
