Fully Describe with the four reaction step the required enzymes and co-factors, for each step of the; B-oxidation for a saturated fatty acid. Use the template for your answer: product Enzyme and cofactor breakdown.
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Fully Describe with the four reaction step the required enzymes and co-factors, for each step of the; B-oxidation for a saturated fatty acid. Use the template for your answer: product Enzyme and cofactor breakdown.
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- Consider the hypothetical biochemical pathway shown below. Assume that each letter (A, B, C, etc) represents a molecule and each number (1, 2, 3, etc) represents an enzyme. Draw arrows indicating all the probable feedback inhibition interactions that would be expected to regulate the activity of enzymes in this pathway.An example of an enzyme-catalyzed reaction proceeding via a transition-state stabilization mechanism is the hydrolysis of peptides by chymotrypsin while, Lysozyme is often cited as an example of an enzyme which operates by strain mechanism. Discuss both mechanisms in the context of each enzyme.A multi-enzyme complex Is made up of three polypeptide chains, A, B and C. A is associated with decarboxylase activity; B is a transacetylase, while C is a dehydrogenase. When the protein was placed in a nonpolar solvent, then run in PAGE, two protein bands were observed. Enzyme assays showed that one protein band exhibited decarboxylase activity while the other has both transacetylase and dehydrogenase activities. When the protein was also placed in an aqueous solvent at pH 5.0, then run in electrophoresis, two protein bands were also detected. Further enzyme assays also showed that one protein band exhibits transacetytase activity while the other has both decarboxylase and dehydrogenase activities. a. What types of non-covalent interactions are possible between A, B and C? b. Addition of urea, a reducing agent gave 4 bands in the PAGE profile with a subsequent loss of decarboxylase activity. What could be the reason for the observed result? Explain briefly in terms of the structure…
- The enzyme chymotrypsin, catalyses the hydrolysis of nitrophenyl acetate and pther acyl esters. Name the amino acid residue, the side chain of the residue, and the type of bond/linkage involved in the formation of the acyl-emzyme complex during catalysis.A generalized enzyme active site is shaped like a hemisphere with a radius of 45Å. The active site holds the following amino acids in a homeostatic solution (pH = 7.38): -HAVARILKHAVARILKHAVARILK- Assuming the charge is distributed uniformly along the hemisphere, determine the force at which this active site acts upon a single ATP molecule at the center of the hemisphere.Only a few amino acid residues are actually involved in catalysis in enzymes, yet enzymes are constructed of at least 100 amino acids, and often many more. Suggest some functions for the noncatalytic amino acids.
- Consider the complete oxidation of one mole of simple TAG containing behenic acid residues (22:0). I. For one mole of the fatty acid residue, determine the following: d. What is the number of net ATP yield of ATP in the complete oxidation of the fatty acid residueConsider the complete oxidation of one mole of simple TAG containing behenic acid residues (22:0). I. For one mole of the fatty acid residue, determine the following: c. What is the number of ATP yield obtained from FADH2 coming from the complete β-oxidation of the fatty acid residueThe metabolic process in all living organisms are relative function of the molecular basic of the cell. Give a concise explanation.
- the following is a coenzyme or cofactor involved in enzymatic reaction. identify the biochemical role that S-adenosylmethionine plays within a biochemical tranformation.B-lactamase is an enzyme found in many antibiotic-resistant bacteria that hydrolyzes and inactivates antibiotics like penicillin and cephalosporin. The amount of antibiotic hydrolyzed in 1 minute in a 10-ml solution containing purified ß-lactamase was measured as a function of antibiotic concentration. The kinetics of hydrolysis was performed for two antibiotic substrates (A and B). Assume that the concentration of ß-lactamase was kept constant during the assay. 12 Initial Velocity (nanomole/min) 10 8 2 0 10 20 | 30 [Antibiotic] (µm) 40 50 Antibiotic A Antibiotic B a) Based on the enzyme description, what type of enzyme is ß-lactamase? Lyase Isomerase Ligase Hydrolase Oxidoreductase Transferase b) Based on your answer in (a), what other reactant, in addition to the antibiotic substrate, needs to be in the active site of ß-lactamase for the hydrolysis reaction to proceed? c) From the reaction curves above, what is the approximate value of Vmax for the enzyme reaction? (Do not forget the…Complete the following table by providing the reactants/substrates, enzymes and their functions as well as the products in each step of the Fatty Acid Degradation. Please provide the structure of the reactants and products
