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- 7. Chalcone isomerase catalyzes the reaction illustrated below. A series of modification experiments were performed on this enzyme to identify which amino acid residues might be in the active site and which might promote the cyclization reaction. OH Ho. Но Explain the following results: A) Acetic anhydride treatment inhibited enzyme activity. B) Pyrocarbonate inhibited activity and was found to modify 7 residues. However, this enzyme only contains 6 His and modification of these did not affect activity. C) lodoacetate inhibited activity but this effect coult be decreased in the presence of substrate or product. D) Methane methanethiol sulfonate modified the enzyme but did not inhibit catalytic turnover. In addition, this modification was reversed in the presence of B-mercaptoethanol. keNyons Rengent19. Which statement is TRUE of sphingolipid synthesis? 1.All of the carbon atoms of palmitate and serine are incorporated into sphingosine. 2CDP-sphingosine is the activated intermediate. 3CO2 is produced during the synthesis of ceramide from palmitate and serine. 4Glucose 6-phosphate is the direct precursor of the glucose in cerebrosides. 5Phosphatidic acid is a key intermediate in the pathway.1 Using Haworth projections, draw the structure of an a-disaccharide of mannose B(1,2) galactose (mannose is the C-2 epimer of glucose, galactose is the C-4 epimer of glucose). Using the disaccharide that you have drawn, show one interaction that would occur between C-4 of galactose and the R-group of His at pH 7. You will need to draw the structure of His. Use a dotted line between the specific atoms to indicate the interaction. What type of interaction is this? O 2022 Arizona State University Online 2. Draw the structure of the fatty acid, 16:247,10, as it occurs at pH 7. Make sure double bonds have the correct configuration. Using the omega numbering system for fatty acids, what type of fatty acid is this? © 2022 Arizona State University Online 3. Draw a diagram that shows the formation of the sodium gradient using ATP coupled to active transport of glucose using the sodium gradient. Clearly label the sides of the membrane and transporter(s) used. Clearly show the direction of…
- 1. Acid phosphatases are an important group of enzymes that can be detected in human blood serum. Under slightly acidic conditions (pH 5.0), this group of enzymes can hydrolyze biological phosphate esters as follows: R-O-P-O, + H 20→ R-OH + HO-P-O;?. Acid phosphatases are produced and can be detected in erythrocytes, kidney, spleen, the liver, and prostrate gland. The enzyme from the prostrate gland is clinically important because an increased activity in the blood is frequently an indication of cancer of the prostrate gland. Tartrate ion can strongly inhibit the phosphatase from the prostrate gland, but not acid phosphatases from other tissues. How can you use the information above to develop a specific procedure for measuring the activity of the acid phosphatase of the prostrate gland in human blood serum?3. (a) In Bakers yeast there are two variants of cytochrome c, a heme containing protein of 108 amino acid residues that catalyzes electron transfer reactions in mitochondria. The two forms of cyto- chrome c known as iso-1 and iso-2 cytochrome c differ in 17 of the 108 amino acids. The content of proton dissociable side chains for the two cytochromes c is given in the table below: Side chain pka iso-1 cytochrome c Ziso-1 iso-2 cytochrome c 12.5 3 4.0 4 8.0 4.0 6.0 10.0 9.0 7.0 4.0 Arginine Aspartate Cysteine Glutamate Histidine Lysine Tyrosine -NH3Ⓡ -COOH 1 4 4 16 5 1 1 What is the overall electrostatic charge on each cytochrome at pH 8? (b) To the right is a diagram of the chemical groups in carboxymethyl-cellulose and DEAE-cellulose that are used for ion exchange chromatography to purify proteins. At pH 8 which chromatographic resin has to be used to separate iso-1-cytochrome c from iso-2-cytochrome c from a lysate of yeast cells? If the proteins are separated by application of a…1. Acid phosphatases are an important group of enzymes that can be detected in human blood serum.Under slightly acidic conditions (pH 5.0), this group of enzymes can hydrolyze biological phosphate esters as follows: R-O-P-O3-2 + H 2O R-OH + HO-P-O3-2. Acid phosphatases are produced and can be detected in erythrocytes, kidney, spleen, the liver, and prostate gland. The enzyme from the prostate gland is clinically important because an increased activity in the blood is frequently an indication of cancer of the prostate gland. Tartrate ion can strongly inhibit the phosphatase from the prostate gland, but not acid phosphatases from other tissues. How canyou use the information above to develop a specific procedure for measuring the activity of the acid phosphatase of the prostate gland in human blood serum?
- 5. Shown below are the first steps in the mechanism of a cysteine protease, which catalyses amide bond hydrolysis in a similar manner as serine proteases. (a) Complete this mechanisms, and (b) sketch the approximate reaction coordinate diagram for this catalyzed reaction relative to the uncatalyzed proteolysis. HN N HN cysteine protease1. To determine the sequence of amino acids in protein, partial hydrolyses at different points are made and then compared to other sets of partial hydrolyses For example: Complete hydrolysis gave: Phenylalanine-1 Histidine-2 Glutamic acid-1 Leucine - 4 Asparagine-1 Cystine -2 Glutamine-1 Glycine - 2 The Partial Hydrolyses yielded the following: 1st Hydrolysis : 4 polypeptides ● . IA: phe-val-asn-gln-his-leu IB: IC: leu-tyr-leu-val ID: val-cys-gly 2nd Hydrolysis: 3 polypeptides IIA: phe-val-asn-gIn-his-leu-cys-gly-ser-his-leu IIB: val-glu-ala-leu-tyr-leu IIC: val-cys-gly Write down the primary structure of this polypeptide by finding the overlaps of the amino acids therein: Serine-1 Valine-3 Alanine-1 tyrosine-1 cys-gly-ser-his-leu-val-glu-ala(iii) Draw a structural diagram of a hydrogen bond between β-D-glucose and the side chain of any polar residue in a protein. (iv) Name the type of bond that can occur between the axial hydrogens of glucose and the indole ring of tryptophan. Draw a structural diagram of this bond. (v) Comment on the polar / apolar nature of the bond in part (iv) and explain why this type of interaction is prevalent in protein-sugar complexes. Answer (iii) to (v) please.
- 2) Briefly explain the relationships between [AMP], [ADP], and [F 2,6-BP] and [F-6-P] in the following graph (a). Fructose 6 – phosphate (F6P) → Fructose 1,6 – bisphosphate (FBP) AG = -22.2 kJ/mol 100 +0.13 mM fructose-2,6- bisphosphate 50 No fructose-2,6- bisphosphate [Fructose-6-phosphate] (a) Activation of PFK by fructose-2,6-bisphosphate. PFK activity Reaction rate, % Vmax1. 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…Carboxypeptidase, which sequentially removes carboxyl-terminal amino acid residues from its peptide substrates, is a single polypeptide of 307 amino acids. The two essential catalytic groups in the active site arefurnished by Arg 145 and Glu 270 .(a) If the carboxypeptidase chain were a perfect α helix, how far apart (in Å) would Arg 145 and Glu 270 be? (b) Explain how the two amino acid residues can catalyze a reaction occurring in the space of a few angstroms