Concept explainers
Vitamin E is the name for a set of chemically related tocopherols, which are lipid
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Chapter 15 Solutions
Genetic Analysis: An Integrated Approach (3rd Edition)
- The “keto diet” is a dietary regimen in which carbohydrates are severely restricted, protein intake is low, and fat comprises 70–90% of daily calories. The diet causes “nutritional ketosis,” which is a different metabolic state than the ketosis that occurs in an untreated diabetic. The normal ketone body concentration is less than 0.6 mM. Explain why an individual on the keto diet may have a blood ketone body concentration of up to 3 mM. What biochemical pathways are active in an individual adhering to the keto diet? What pathways are largely inactive? Protein intake is kept low because a high-protein diet would inhibit ketosis. Explain why. Why might the keto diet lead to weight loss?arrow_forwardA glycolytic intermediate may be used to make the glycerol 3-phosphate necessary for the production of glycerophospholipids. For this conversion, provide a reaction sequence.arrow_forwardAn enzyme that catalyzes disulfide– sulfhydryl exchange reactions, called protein disulfide isomerase (PDI), has been isolated. PDI rapidly converts inactive scrambled ribonuclease into enzymatically active ribonuclease. In contrast, insulin is rapidly inactivated by PDI. What does this important observation imply about the relation between the amino acid sequence of insulin and its threedimensional structure?arrow_forward
- Provide an illustration showing the broken down of C7 fatty acid into its corresponding end products. What are the products being generated and how much of these products are generated from C7 fatty acids? Briefly explain it.arrow_forwardMucins found on adenocarcinoma cells carry O-glycans terminated with sialic acids (such as the Sialyl Tn antigen) that are smaller and less branched than O-glycans found in healthy epithelial cells. Based on what you know about the biosynthetic pathway for O-glycans, explain this observation.arrow_forwardThe effect of ATP on the allosteric enzyme PFK-1 is shown below. For a given concentration of fructose 6-phosphate, the PFK-1 activity increases with increasing concentrations of ATP, but a point is reached beyond which increasing the concentration of ATP inhibits the enzyme. (a) Explain how ATP can be both a substrate and an inhibitor of PFK-1. How is the enzyme regulated by ATP? (b) In what ways is glycolysis regulated by ATP levels? (c) The inhibition of PFK-1 by ATP is diminished when the ADP concentration is high, as shown in the illustration. How can this observation be explained? *A graph is included for this question*arrow_forward
- Which of the following statements are descriptions of metal ion catalysis or examples of metal ion catalysis? Choose all correct answers a Zn²+ cofactor may properly orient the substrate in the active site through ionic interactions. a covalent bond forms between enzyme and substrate lowers the energy or stabilizes the transition state or intermediate catalyst retains its original form after reaction occurs catalysts may participate in oxidation-reduction reactions by changes in the oxidation statearrow_forwardUDP-glucuronosyltransferase enzymes bind the organic compound UDP-glucuronic acid (UDP-GA) in order to catalyse the transfer of a glucuronic acid group from UDP-GA to a drug molecule, releasing UDP from the active site as a product. UDP is then regenerated by the activity of another enzyme. What terms could be used to describe UDP-GA?arrow_forwardGlutathione is an important intracellular thiol. List fivefunctions of glutathione in the bodyarrow_forward
- Fish living in environments such as the Arctic Ocean, wherewater temperatures are below the freezing point of theirblood, are able to survive because of so-called antifreezeglycoproteins. Suggest how these glycoproteins work.arrow_forwardThe cells that line the mammalian intestine produce glycoproteins with O-linked oligosaccharides. Some of the glycoproteins remain anchored to the cell surface and some are released into the intestinal space. In a healthy animal, numerous microbial species (the microbiome) live in the intestine. These organisms produce fucosidase, an enzyme that hydrolyzes glycosidic bonds involving fucose. (a) Why is this enzyme useful to the micro organisms? (b) Pathogenic (disease-causing) bacteria typically lack fucosidase. How does this help prevent the growth of pathogens in the intestine, particularly during an illness when the human host stops eating?arrow_forwardA carboxypeptidase is a metalloenyme (its active site contains one or more metal ions essential for the function) that catalyzes the hydrolysis of the peptide bond of the terminal amino acid of a polypeptide chain (where the free carboxyl group occurs). The binding of an L-alanyl-L-tyrosine peptide substrate in the active site of the enzyme is represented in the scheme below: Glu Zn++ COO™ OH H3C CH₂ HC NH IO C H H Poche apolaire -H H O+N: C N H H H NH₂ Arg 145 Туг 248 NB: This scheme gives a planar representation of the spatial structure of the active site where indicated contacts (hatched lines) are supposed to occur in the 3D structure of the enzyme. 1- Describe the interactions that occur between the ligand and amino acid residues of the active site. 2- What would be the impact on the Km value if we replace L-alanyl-L-tyrosine by the following substrates: L-alanyl-L-phenylalanine; L-alanyl-L-aspartate; L-aspartyl-L- tyrosine.arrow_forward
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