Concept explainers
(a)
Interpretation:
The amino acid alternation in the upper panel of graph A must be determined.
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 affect of mutation in colipase enzyme should be determined.
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 amino acid substitution in the lower panel of graph A must be determined.
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 effect of above substitution on the ability of colipase to bind the lipase to the lipid particle must be determined.
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 effect of the L16A mutation on lipase activity should be determined by analyzing the graph B.
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 lipase-binding and activation properties of the colipase enzyme must be determined.
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.
(g)
Interpretation:
The effect of the Y55A mutation on lipase activity must be determined.
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 solutionChapter 22 Solutions
BIOCHEMISTRY W/1 TERM ACHEIVE ACCESS
- Explain well. Asaparrow_forwardC, D correct answer. I need explanation. Asaparrow_forwardInducers and Inhibitors of AEP. Short peptides such as legumain stabilization and activity modulation (LSAM) domain and αvβ3 integrin could enhance the activity of AEP. LSAM domain known as the prodomain of AEP blocks substrate binding before activation. This prodomain has a helical structure and two independent peptides. One is an activation peptide (AP, K287 to N323), and the other is a LSAM domain. LSAM domain remains even after AP is cleaved and released from protease at neutral pH via electrostatic interaction. AEP without LSAM domain has a lower melting temperature than AEP with LSAM domain [77, 117]. Another short peptide, αvβ3 integrin, can directly interact with AEP, and after forming a complex, the optimal pH for AEP activity is increased from 5.5 to 6.0. It indicates that αvβ3 binding could induce conformational stabilization of AEP accompanied by deprotonated C189. αvβ3 does not directly interact with the AEP active site; however, AEP docks to the αvβ3 RGD-binding site…arrow_forward
- Please help me with this question. More than one answer may be correct. THe graph relating to the information is included below. The figure shows the number of cells that have clusters of IRE1 molecules after those cells are treated with various levels of thapsigargin (Tg), a chemical that can induce ER stress. IRE1 can form these clusters when ER stress is induced and this clustering can cause activation of RNAse activity in IRE1. In this experiment, normal IRE1 was used (IRE1α) that can bind to Sec61, along with a modified version of IRE1 that binds to Sec61 more weakly than normal IRE1 (wIRE1α), and another modified version that binds to Sec61 more strongly than normal IRE1 (sIRE1α). From this figure you can conclude that: Question 18 options: IRE1 binding to Sec61 promotes the formation of IRE1 clumps IRE1 binding to Sec61 prevents the formation of IRE1 clumps co-translational translocation is a key process the golgi aparatus is heavily involved in the unfolded protein response The…arrow_forward1G. Please help me in detail. For Molecular Mechanism of ATP versus GTP selectivity of adenylate kinase, Write an expression for the reaction velocity.arrow_forwardproteins. Which of the following will tell you whether a protein would be found in the lumen of the ER? A. You run a hydropathy plot an look for hydrophobic peaks that span 20-30 amino acids B. You isolate microsomes and see whether the proteins are inserted into the membrane of the microsome C. You run a hydropathy plot an look for a lack of hydrophobic peaks that span 20-30 amino acids O D. You do in vitro translation of each protein in the presence or absence of microsomes and look to see whether there is a size change in the presence of microsomes.arrow_forward
- Briefly describe the induced-fit conformational change when hexokinase binds its substrate.arrow_forward. CTP synthetase catalyzes the glutamine-dependent conversion of UTP to CTP. The enzyme is allosterically inhibited by the product, CTP. Mammalian cells defective in this allosteric inhibition are found to have a complex phenotype: They require thymidine in the growth medium, they have unbalanced nucleotide pools, and they have a mutator phenotype. Explain the basis for these observations.arrow_forward. Propose a chemical mechanism for the reaction catalyzed by the PLP-dependent glatamate 1-semialdehyde aminomutase.arrow_forward
- Activated carriers participate in carbohydrate, peptidoglycan, lipid, and LPS synthesis. Briefly describe these carriers and their roles. Are there any features common to all the carriers? Explain your answerarrow_forward. The allosterically regulated enzyme ATCase binds aspartic acid as a substrate and acylates the a-amino group. Succinate acts as a competitive inhibitor of ATCase because it binds the active site but can't be acylated. The dependence of vo on [aspartic acid] for ATCase is shown in panel (a) of the accompanying figure. Panel (b) shows the effect of increasing [succinate] on v, when [Asp] is held at a low concentration (see thick vertical arrow in panel (a)). Note that in panel (b), vo is not zero when [succinate] =0 (see thin horizontal arrow). Explain the shape of the curve in panel (b). Why does v, increase initially, before decreasing at higher [succinate]? Co0- COO CH2 CH, HC -NH, CH, COO COO Asp Succinate [Asp) [Succinate] [Asp] in experiment b (a) (b)arrow_forwardNot hand written please.arrow_forward
- Biology: The Dynamic Science (MindTap Course List)BiologyISBN:9781305389892Author:Peter J. Russell, Paul E. Hertz, Beverly McMillanPublisher:Cengage Learning