(a)
Interpretation:
The site of process of fatty acid synthesis and degradation must be compared.
Concept introduction:
The fatty acids are degraded in a sequential manner, that is two carbon units at the carboxyl end of the molecule are removed in each step. The process of beta-oxidation of fatty acids degrades the fatty acids. The process of fatty acid synthesis is a stepwise process, which occurs by the addition of two-carbon units. These carbon units are provided by the acetyl-CoA, derived from glucose oxidation.
(b)
Interpretation:
The acyl carrier of fatty acid synthesis and degradation must be compared.
Concept introduction:
The fatty acids are degraded in a sequential manner, that is two carbon units at the carboxyl end of the molecule are removed in each step. The process of beta-oxidation of fatty acids degrades the fatty acids. The process of fatty acid synthesis is a stepwise process, which occurs by the addition of two-carbon units. These carbon units are provided by the acetyl-CoA, derived from glucose oxidation.
(c)
Interpretation:
The reductants and oxidants of fatty acid synthesis and degradation must be compared.
Concept introduction:
The fatty acids are degraded in a sequential manner, that is, two carbon units at the carboxyl end of the molecule are removed in each step. The process of beta-oxidation of fatty acids degrades the fatty acids. The process of fatty acid synthesis is a stepwise process, which occurs by the addition of two-carbon units. These carbon units are provided by the acetyl-CoA, derived from glucose oxidation.
(d)
Interpretation:
The stereochemistry of intermediates of fatty acid synthesis and degradation must be compared.
Concept introduction:
The fatty acids are degraded in a sequential manner, that is, two carbon units at the carboxyl end of the molecule are removed in each step. The process of beta-oxidation of fatty acids degrades the fatty acids. The process of fatty acid synthesis is a stepwise process, which occurs by the addition of two-carbon units. These carbon units are provided by the acetyl-CoA, derived from glucose oxidation.
(e)
Interpretation:
The direction of fatty acid synthesis and degradation must be compared.
Concept introduction:
The fatty acids are degraded in a sequential manner, that is, two carbon units at the carboxyl end of the molecule are removed in each step. The process of beta-oxidation of fatty acids degrades the fatty acids. The process of fatty acid synthesis is a stepwise process, which occurs by the addition of two-carbon units. These carbon units are provided by the acetyl-CoA, derived from glucose oxidation.
(f)
Interpretation:
The organization of the enzyme system of fatty acid synthesis and degradation must be compared.
Concept introduction:
The fatty acids are degraded in a sequential manner, that is, two carbon units at the carboxyl end of the molecule are removed in each step. The process of beta-oxidation of fatty acids degrades the fatty acids. The process of fatty acid synthesis is a stepwise process, which occurs by the addition of two-carbon units. These carbon units are provided by the acetyl-CoA, derived from glucose oxidation.
Want to see the full answer?
Check out a sample textbook solution
Chapter 22 Solutions
Biochemistry
- 5. You discover a new cysteine protease similar to papain. Cysteine proteases are proteolytic enzymes that utilize a cysteine residue in the active site for the nucleophilic attack of a peptide bond, while a second residue acts as a base for proton abstraction in the reaction (acid base catalysis). In this novel enzyme the pKa of the cysteine residue is significantly lowered by the active site environment to pKa=4. a. Knowing that the protease shows highest activity between pH 4-6, what could be the identity of the base residue acting as a in the reaction? Explain and write the expected mechanism for the reaction. SH онarrow_forwardX INCORRECT; see section 13.1 Enzymes occasionally display weak "“side" activities. Draw the structure of the product (other than ADP) of the reaction that results when pyruvate kinase, operating in reverse, uses lactate as a substrate. For your structure: 1. Do not include primary or secondary hydrogens. CH2 HO OH Edit Drawingarrow_forward. Explain what is meant by the term, “high energy compound”. Name a thioester molecule that is commonly found in biochemical reactions. Explain why thioesters are “high energy” compounds. Describe the molecular structure of cellulose. How does this structure explain why cellulose forms strong fibers? Explain why digestion of cellulose takes a long time even when catalyzed by an enzyme. The enzyme phosphofructokinase transfers a phosphate from ATP to the hydroxyl group a C1 of fructose. Similar to fructose, water also has a hydroxyl group and the concentration of water is much higher than that of fructose. Explain why the phosphate is transferred to fructose and not to water.arrow_forward
- G. ENZYME CLASSIFICATION. Identify the main class of enzymes used to catalyzed the following reactions: 1. Lactate dehydrogenase: NADH+H NAD HC-OH CH3 CH Pynnte Lactate 2. Methylmalonyl-CoA mutase: CH CH SCOA CH,CH, SCOA coenzyme B12 COO COO methylmalonyl-CoA succinyl-CoA 3. Enolase: 0. H–Ċ–0–P–0- C-0–P-0- + H,0 HO–CH, CH 6 Phosphoenolpyruvate 2-Phosphoglycerate 4. Chymotrypsin: -0–CH,CH3 + H2O - RCOOH + HOCH,CH3 5. Pyruvate carboxylase: coo • co, • ATP + H,0 H-C-H . ADP + P, + 2H čoo CH, Pyruvate Oxaleacetatearrow_forwardA7. Consider what can be concluded about the catalytic site (substrate binding site) of phosphatase and the binding site of NaF from the type of inhibition shown by NaF for phosphatase and illustrate it schematically. The inhibition typre is pure noncompetitive inhibition.arrow_forwardMatch each enzyme to its function. Hint: You may be unfamiliar with some of the enzymes below but you can still use what you have learned about how enzymes are named ("enzyme nomenclature") in chapter 4 to answer this question correctly. glutamate dehydrogenase an enzyme that reduces bi v lactate dehydrogenase oxidizes the molecule crea v creatine kinase an enzyme that reduces bi v glucokinase oxidizes the molecule glut v pancreatic lipase oxidizes the molecule lact: v salivary lipase an enzyme that reduces bi varrow_forward
- Explain as brief and simple as possible. Answers must not be more than 30 WORDS each. a. All coenzymes are cofactors, but not all cofactors are coenzymes. Explain this statement. b. How does the induced-fit model of enzyme action explain the broad specificities of some enzymes? c. In competitive inhibition, can both the inhibitor and the substrate bind to an enzyme at the same time? Explain your answer d. Why is penicillin toxic to bacteria but not to higher organisms? e. What is the metabolic basis for the observation that many adults cannot ingest large quantities of milk without developing gastric difficulties?arrow_forwardDraw Gluconeogenesis. Please make sure to state all the enzymes and co-factors for each step of the pathway. note you are responsible for all the enzymes for each step, even though it is not stated on the slide.arrow_forwarda. Use the values in Problem 23.31 to calculate the energy change in the following reaction. fructose 1,6-bisphosphate + ADP--------> fructose 6-phosphate + ATP b. Is this reaction energetically favorable or unfavorable? c. Write this reaction using curved arrow symbolism. d. Can this reaction be used to synthesize ATP from ADP? Explain.arrow_forward
- Compare and contrast biochemical pathways. Describe the chemistry of the last three steps of the TCA. Describe the chemistry of the first three steps of β-oxidation. Explain how these pathways are similar and how they differ in terms of their chemistry, the involvement of coenzymes and the fate of the electrons. Describe the two connections between the urea cycle and the citric acid cyclearrow_forwardCompare between the Kreb cycle and fatty acid synthesis pathways in term of: 1. The type of metabolic pathway (catabolic or anabolic). 2. The reducing or oxidizing coenzymes needed for these pathways 3. Location of these pathways inside the cell. 4. Fate of acetyl CoA in both pathwaysarrow_forwarda. Protein X can be phosphorylated. Why would the phosphorylated form of protein X elute AFTER the unphosphorylated form from an ANION exchange column? Please describe in terms of: The chemical properties of phosphorylation modification b. The chemical properties of an anion exchange column and how it works c. Why is an inhibitor that mimics the transition state more effective at enzyme inhibition than an inhibitor that mimics the substrate? d. Protein X can be covalently modified with many methyl groups. What two general properties would be different between the unmethylated protein versus the methylated protein?arrow_forward
- BiochemistryBiochemistryISBN:9781319114671Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.Publisher:W. H. Freeman
Lehninger Principles of BiochemistryBiochemistryISBN:9781464126116Author:David L. Nelson, Michael M. CoxPublisher:W. H. Freeman
Fundamentals of Biochemistry: Life at the Molecul...BiochemistryISBN:9781118918401Author:Donald Voet, Judith G. Voet, Charlotte W. PrattPublisher:WILEY 
BiochemistryBiochemistryISBN:9781305961135Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougalPublisher:Cengage Learning
BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage Learning
Fundamentals of General, Organic, and Biological ...BiochemistryISBN:9780134015187Author:John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. PetersonPublisher:PEARSON