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- #1)What are the main roles of the following amino acids; (within the crystal structure and/or active site. be specific, with pictures and mechanistic arrows as needed) -Glu305 from pyruvate carboxylase -Gln23 from Penecilin Acylase -Ser203 from Acetylcholinesterase #2) Why is L-tetrahydro-2-furoic acid would be a suitable inhibitor for Proline oxidase?1. In a tabular form; identify biochemical reactions and the enzymes in each step in the urea cycle. 2. What is the difference between ketogenic and glucagenic amino acids? 3. What is the difference between transamination and oxidative deamination?#1 Specify the role each of the following amino acids play within the crystal structure and/or active site for Be as specific as possible, with pictures (and mechanistic arrows) as necessary. His11 Arg140 Glu89 Trp68 #2 Provide a step-wise mechanism for the reaction Bisphosphoglycerate mutase catalyzes, using the amino acids responsible for aiding in catalysis. You do not need to add surrounding amino acids that aid in substrate specificity. (drawn out)
- 1.Why do you think glutathione occurs in a concentration as high as glucose? 2.Explain why glutathione must be transported from cytosol to mitochondria. 3.Explain why glutathione can confer therapeutic benefit when taken orally.The M and H subunits of lactate dehydrogenase have very similar sizes and shapes but differ in amino acidcomposition. If the only difference between the two were that theH subunit had a glutamic acid in a position where the M subunithad a serine, how would the five isozymes of LDH separate on electrophoresis using a gel at pH 8.6?1. Consider the three-dimensional model of the tertiary structure of an enzyme below. Amino acids involved in binding are shaded blue, and amino acids involved in catalysis are shaded red. A. Suppose research has shown that amino acid 82 in the red shaded region is lysine, an amino acid with a positively-charged side chain. This lysine is critical for catalysis. Other studies have found that amino acids 12 and 62 in the blue region are both phenylalanine, an amino acid with a nonpolar side chain, and are critical for substrate binding. These amino acids are relatively close in the active site but are separated by 20-70 amino acids in the primary structure. Using what you know about protein structure, explain how amino acids separated in the primary structure can come close together in the active site. B. Use this information and figure 4.2 in your book to answer the following questions: Do you think changing amino acid 82, lysine, an amino acid with a positively-charged side…
- 8. Match each of the following amino acids with the intermediate needed for its synthesis.(a) 3-Phosphoglycerate 1. glutamate 2. serine 3. asparagine (b) oxaloacetate 1. glutamate 2. serine 3. AsparagineLegend: Blue – wild-type β-galactosidase Red – mutant β-galactosidase _________ a. What is the optimum pH of wild type β-galactosidase? _________ b. What is the optimum temperature of mutant β-galactosidase? _________ c. Which enzyme has the greater activity at pH 7.2? _________ d. Which enzyme has the greater activity at a temperature of 42.5oC? _________ e. Which enzyme has greater activity if pH decreases from 7.5 to 6.4? _________ f. Which enzyme has greater activity if temperature increases from 40oC to 41 oC?2. A mixture of the following amino acids (glu, leu, val, arg, ser, phe) was obtained upon complete hydrolysis of a hexapeptide. a. Edman’s reagent releases leucine b. Hexapeptide with carboxypeptidase releases serine. c. Hexapeptide with trypsin forms a tripeptide A with leucine at the N terminal and tripeptide B with valine at the N terminal. d. Tripeptide A with carboxypeptidase releases arginine and a dipeptide with glutamic acid at C terminal. e. Tripeptide B with chymotrypsin form releases serine and another dipeptide. Give: 1. the amino acid sequence of tripeptide A and B. 2. the amino acid sequence in the above hexapeptide.
- 1. The Fehling’s reaction, which is a simple assay for reducing sugars, was used as a diagnostic test for the determination of blood glucose concentrations for a very long time. However, it has now been replaced by the glucose oxidase test. The enzyme glucose oxidase isolated from the mold Penicillium notatum catalyzes the oxidation of β-D-glucose to D-glucono-δ-lactone. This enzyme is highly specific for the β-anomer of glucose and does not affect the α-anomer. In spite of this specificity, the reaction catalyzed by glucose oxidase is commonly used in a clinical assay for total blood glucose—that is, for solutions consisting of a mixture of β- and α-D-glucose. Explain how this is possible. Aside from allowing the detection of smaller quantities of glucose, what advantage does glucose oxidase offer over Fehling’s reagent for the determination of blood glucose? 2. Consider only the oxygen levels present in the cytoplasm and ECF as shown in the drawing above (no new oxygen is entering…(a) What are the Vmax and Km (including units) for Tigerzyme? b) What are the Vmax and Km (including units) for Tigerzyme in the presenceof the inhibitor Tar Heel? (c) What are the Vmax and Km (including units) for Tigerzyme in the presenceof the inhibitor Blue Devil?1. Please identify the substrate and type of reaction, and explain how these reactions work for the following two enzymes Two enzymes: succinate dehydrogenase and L-amino acid reductase
