Biochemistry: Concepts and Connections (2nd Edition)
2nd Edition
ISBN: 9780134641621
Author: Dean R. Appling, Spencer J. Anthony-Cahill, Christopher K. Mathews
Publisher: PEARSON
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Textbook Question
Chapter 16, Problem 28P
cis-Vaccenate is an 18-carbon unsaturated fatty acid abundant in E. coli membrane lipids. Propose a
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Which fatty acid(s) out of the following four: palmitoleate, oleate, linoleate, and linolenate, can be a biosynthetic precursor in mammals for the polyunsaturated fatty acid 20:4 all-cis-D5 ,D8 ,D11 ,D14 ? Briefly sketch the steps of the possible synthesis from the chosen precursor using symbols only for the fatty acids. (Hint: mammalian systems contain four terminal desaturases of broad chainlength specificities designated as D9 -, D6 -, D5 -, and D4 -fatty acyl desaturases.)
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Chapter 16 Solutions
Biochemistry: Concepts and Connections (2nd Edition)
Ch. 16 - Prob. 1PCh. 16 - If palmitic acid is subjected to complete...Ch. 16 - Calculate the number of ATPs generated by the...Ch. 16 - Prob. 4PCh. 16 - Prob. 5PCh. 16 - Under conditions where ketone bodies are being...Ch. 16 - Prob. 7PCh. 16 - 2-Bromopalmitoyl-CoA inhibits the oxidation of...Ch. 16 - When the identical subunits of chicken liver fatty...Ch. 16 - Prob. 10P
Ch. 16 - Prob. 11PCh. 16 - Prob. 12PCh. 16 - Prob. 13PCh. 16 - Prob. 14PCh. 16 - Prob. 15PCh. 16 - What would be the effect on fatty acid synthesis...Ch. 16 - Prob. 17PCh. 16 - Identify and briefly discuss each mechanism...Ch. 16 - Prob. 19PCh. 16 - Prob. 20PCh. 16 - Prob. 21PCh. 16 - Prob. 22PCh. 16 - Prob. 23PCh. 16 - 24. If mevalonate labeled with 14C in the carboxyl...Ch. 16 - Prob. 25PCh. 16 - Identify a pathway for utilization of the four...Ch. 16 - Prob. 27PCh. 16 - cis-Vaccenate is an 18-carbon unsaturated fatty...Ch. 16 - 29. Briefly describe how cyclic AMP controls...Ch. 16 - Prob. 30PCh. 16 - Prob. 31PCh. 16 - In addition to the pathway described in Figure...Ch. 16 - Prob. 33P
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- Lysine degradation requires removal of two amino groups. Removal of itsε-amino group gives a-aminoadipic semialdehyde. This product is thendegraded to acetoacetate by the same chemical strategy used to degrade thebranched-chain amino acids. Draw the proposed intermediates in this pathway (Hint: see Figure 18.14).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_forwardThe surface of E. coli ACP has a patch of Glu side chains. What can you conclude about the side chains likely to be located on the surface of the E. coli β-hydoxyacyl-ACP dehydrase?arrow_forward
- Mucins 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_forwardGlobular proteins with multiple disulfide bonds must be heated longer and at higher temperature to denature them. Bovinepancreatic trypsin inhibitor (BPTI), having 58 amino acids in a single chain and 3 disulfide linkages, loses its catalytic activity whenheated at nearly 90°C for 5-10 minutes. Explain the molecular basis of this observed thermal property of BPTI relative to the nativestructure and function of the protein.arrow_forwardSome of the following four amino acids : alanine, arginine, histidine, aspartic acid would provide a side chain for acid-base catalysis at physiological pH (assume pK of each amino acid is equal to pK value for the free amino acid in solution). Explain for each amino acid how and why each would or would not provide the side chain residue to support acid-base catalysis at physiological pH.arrow_forward
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- Bovine pancreatic trypsin inhibitor (BPTI; as shown) contains six cysteine residues that form three disulfide bonds in the native structure of BPTI. Suppose BPTI is reduced and unfolded in urea (as illustrated for RNase A as shown). If the reduced unfolded protein were oxidized prior to the removal of the urea, what fraction of the resulting mixture would you expect to possess native disulfide bonds?arrow_forwardGlobular proteins with multiple disulfide bonds must be heated longer and at higher temperature to denature them. Bovinepancreatic trypsin inhibitor (BPTI), having 58 amino acids in a single chain and 3 disulfide linkages, loses its catalytic activity whenheated at nearly 90°C for 5-10 minutes. Explain the molecular basis of this observed thermal property of BPTI relative to the nativestructure and function of the protein. do not coy from other answers herearrow_forwardIs the statement during fatty acid biosynthesis, the product detaches from fatty acid synthase complex when the chain length is 16 carbons, wrong or right?arrow_forward
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