4A. Write out the chemical equations (structures are not necessary) for the two steps in the reaction catalyzed by aminoacyl tRNA transferase. Include all products and reactants. Step 1: amino acid activation Step 2: aminoacyl transfer to the tRNA 4B. Write the chemical equation for the net reaction catalyzed by aminoacyl transferase. This can be determined by taking the sum of the two reactions above.
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- Chart is Given for you: Below is a chart of values for actual enzymes. Enzyme Km (M) kcat (1/s)Chymotrypsin 1.5 × 10^−2 0.14Pepsin 3.0 × 10^−4 0.5Tyrosyl-tRNA synthetase 9.0 × 10^−4 7.6Ribonuclease 7.9 × 10^−3 7.9 × 10^2Carbonic anhydrase 2.6 × 10^−2 4.0 × 10^5Fumarase 5.0 × 10^−6 8.0 × 10^2 Assume the enzyme concentration is equal across all samples (and is equal to 1). (Answer a and b only)a. Which enzyme will have the highest V0 at very high substrate concentrations? (1 M). Why? b. Which will have the highest V0 at very low substrate concentrations (5.0 × 10^−12). Why?A. Lineweaver-Burk plot of the enzyme with increasing amounts of substrate in the absence or the presence of the inhibitor is shown below. Graph A : x-intercept Graph B : x-intercept = - 0.012, y-intercept = 0.8 Graph C : x-intercept = - 0.027, y-intercept = 0.8 Graph D : x-intercept = - 0.039, y-intercept = 0.8 - 0.007, y-intercept = 0.8 Graph A 4 Graph B Graph C Graph D 1 -0,04 -0,02 0,00 0,02 0,04 1/[Substrate] (uM) (i) Which graph indicates an enzymatic reaction without inhibitor? (ii) Which type of inhibitor is it? Briefly explain. (iii) Which graph indicates the highest concentration of inhibitor? (iv) Calculate the Vmax and Km of the graph showing an enzymatic reaction with the lowest concentration of inhibitor. Show the steps of calculation and unit in your answers. Keep 2 decimal places in your answers. 1/Rate (umol/min)E Threonine 6. You have identified some intermediates in threonine synthesis: A, B, C, D and E. You grow a few of your mutants in the presence of these different intermediates to determine the order in which the gene products act. Below are your results. A (+) means growth and a (-) means no growth. Given these data, draw the best possible pathway for the synthesis of threonine. The diagram should use arrows to indicate one intermediate being changed to another intermediate. Indicate which gene produces the product responsible for the conversion by listing the mutant in that gene above the arrow. Mt1 Mt2 Mt4 Mt7
- I. A protein, X, was Isolated from a pathogenlc mlcroorganism. The proteln Is a vlrulence factor whose path0genlclty lies In a heptapeptide of unknown sequence. After trypsin cleavage of the heptapeptide from protein X, the peptlde's compOsition and sequence was determined. The fOllowing were the results of the sequenclng process: 1. When the peptide was treated with dinitrofluorobenzene (DNFB), DNP-asp and a mixture of amino acids were produced. 2. When the same Intact peptide was treated with streptococcal protease, a pentapeptide of composition asp, asN, cys, gly and ser and 2 amlno acids were released. 3. When the heptapeptlde was also treated with hydrOxylamine HCI, a tripeptide and a tetrapeptide were obtained. The C-terminal amino acid of the tripeptide was asN. 1) What is the sequence of the heptapeptide if it is composed of cys, asp, lys, asN, gly and ser only? 2) What is the pl of the heptapeptide?Anabolism & Catabolism of Nitrogenous Bases. a. Differentiate the processes of purine nucleotide biosynthesis & pyrimidine nucleotide biosynthesis. What are the starting materials for each process? b. Differentiate the processes of purine nucleotide degradation &pyrimidine nucleotide degradation. What are the end products of each process? c. Explain how purine & pyrimidine biosynthesis is regulated to produce balanced levels ofall four nucleotides (ATP, GTP, UTP & CTP)?Which 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.
- . Radioactive uracil can be used to label all of the pyrimidine residues in DNA. Using either names or structures, present pathways for the conversion of uracil to dTTP and to dCTP. For each reaction, show the involvement of cofactors, and identify sites of allosteric regulation.Which of the following would be a good chemotherapy approach: blocking formationof the ribonucleotide GTP or blocking formation of the deoxyribonucleotide dGTP?Why? Please explain the chemical differences between each of the two nucleotides. Use the specific processes below to support your choice by explaining how either GTP or dGTPare related to these and how loss of the particular molecule would affect each process. *PEP carboxykinase in gluconeogenesis*Succinyl-CoA synthetase in the TCA Cycle*Glucagon signal transduction. (a) Explain the biochemical basis for the fact that one can synchro- nize cell populations þy treating them with deoxythymidine. (b) Explain the apparent paradox that dATP at low concentrations is an activator of ribonucleotide reductase, whereas at higher concen- trations it becomes inhibitory.
- . Explain why DNA is stable in the presence of alkali (0.3 M KOH), while RNA is quantitatively degraded to 2'- and 3'-nucleoside monophosphates under these conditions.Suggest a reasonable strategy for the specific phosphorylation of the5’ –OH group of a nucleoside.3. Solve the sequence of an oligopeptide 7 residues long which gave: Asp Leu Lys Met Phe Tyr The following facts were observed: a. Trypsin treatment had no apparent effect b. The PTH derivative from Edman degradation was c. Brief chymotrypsin treatment yielded several products including but not limited to a dipeptide and a tetrapeptide. The amino acid composition of the tetrapeptide was Leu, Lys, and Met. d. Cyanogen bromide treatment yielded a dipeptide, a tetrapeptide, and a free Lys.