Connect With Learnsmart Labs Online Access For Prescott's Microbiology
11th Edition
ISBN: 9781260408997
Author: Joanne Willey
Publisher: Mcgraw-hill Higher Education (us)
expand_more
expand_more
format_list_bulleted
Videos
Textbook Question
Chapter 10, Problem 2AL
Examine the branched pathway shown here for the synthesis of the amino acids aspartate, methionine, lysine, threonine, and isoleucine.
Scenario 1: The microbe is cultured in a medium containing aspartate and lysine but lacking methionine, threonine, and isoleucine.
Scenario 2: The microbe is cultured in a medium containing a rich supply of all five amino acids.
For each of these two scenarios, answer the following questions:
a. Which portion(s) of the pathway would need to be shut down in this situation?
b. How might allosteric control be used to accomplish this?
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solution
Students have asked these similar questions
Antibiotics that target bacterial molecules not previously exploited are desperately needed. One such target is the protein FtsZ. The small molecule 3-methoxybenzamide (3-MBA) is known to inhibit FtsZ in Bacillus subtilis but is not bacteriocidal. Nonetheless, researchers reasoned that 3-MBA offered a good starting point for the synthesis of a molecule that might be a potential drug candidate. Over 500 3-MBA analogues were synthesized and screened; one called PA190723 was extremely potent in its capacity to bind FtsZ and inhibit bacterial growth. In fact, when used in a mouse model, PA190723 was bacteriocidal against methicillinand multidrug-resistant Staphylococcus aureus.
What makes FtsZ a good drug target?
What preliminary information about 3-MBA would be helpful if you were designing the 3-MBA analogues?
As these researchers move forward with clinical (human) testing, what other parameters and outcomes must be assessed besides the bacteriocidal activity of PA190723?
Sydney Brennen isolated Salmonella typhimurium mutants that were implicated in the biosynthesis of tryptophan and would not grow on minimal medium supplemented with intermediates in tryptophan biosynthesis, some mutants were able to grow while others remained unable to grow. Review the data attached to order the biosynthetic pathway by both enzymatic step and by intermediate biomolecule. Label the step impacted by each of the mutant cell lines.
Your colleague handed you a novel strain of coli that is purifying a protein with a 6xHisTag; they claim it is superior to the TOP10 cells you have been using. But even with a larger culture size, you discover that your protein yield—using the same Ni-NTA column—is quite low. You discover that the novel strain of Escherichia coli generates an unusually high quantity of dicarboxylic acids, a byproduct of the citric acid cycle that is recognized for its ability to function as an all-purpose metal chelator. What do you think the issue is with purifying IMAC protein with this new strain of E. coli?
Chapter 10 Solutions
Connect With Learnsmart Labs Online Access For Prescott's Microbiology
Ch. 10.1 - Figure 10.2 The Relationship of G to the...Ch. 10.1 - Prob. 1CCCh. 10.1 - Prob. 2CCCh. 10.1 - Prob. 3CCCh. 10.1 - Prob. 4CCCh. 10.2 - Why is ATP called a high-energy molecule? How is...Ch. 10.2 - Describe the energy cycle and ATPs role in it....Ch. 10.3 - Prob. 1MICh. 10.3 - Prob. 2MICh. 10.4 - Figure 10.6 Electron Movement and Reduction...
Ch. 10.4 - How is the direction of electron flow between...Ch. 10.4 - When electrons flow from the NAD+/NADH conjugate...Ch. 10.4 - Which among the following would be the best...Ch. 10.4 - In general terms, how is G related to E0? What is...Ch. 10.4 - Name and briefly describe the major electron...Ch. 10.6 - Will an enzyme with a relatively high Km have a...Ch. 10.6 - Prob. 2MICh. 10.6 - Prob. 1CCCh. 10.6 - Prob. 2CCCh. 10.6 - How does enzyme activity change with substrate...Ch. 10.6 - What special properties might an enzyme isolated...Ch. 10.6 - What are competitive and noncompetitive...Ch. 10.6 - How are enzymes and ribozymes similar? How do they...Ch. 10.7 - Figure 10.19 Allosteric Regulation. The structure...Ch. 10.7 - Prob. 2MICh. 10.7 - Define the terms metabolic channeling and...Ch. 10.7 - Define allosteric enzyme and allosteric effector.Ch. 10.7 - Prob. 3CCCh. 10.7 - Prob. 4CCCh. 10.7 - Prob. 5CCCh. 10 - Prob. 1RCCh. 10 - Prob. 2RCCh. 10 - Prob. 3RCCh. 10 - Examine the structures of macromolecules in...Ch. 10 - Examine the branched pathway shown here for the...Ch. 10 - Prob. 3AL
Knowledge Booster
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biology and related others by exploring similar questions and additional content below.Similar questions
- 9) Considering the enzymatic reaction catalyzed by HIV protease: Options A) hydrolysis is the net reaction observed. B) a peptide bond is cleaved on the carboxyl side of a proline residue. C) a serine residue serves as the nucleophile during the catalytic event. D) inhibitors have been designed to covalently link to the active site just like natural substrates do. E) None of the above is true. F) All of the above are true.arrow_forwardA decapeptide which could resist burns was isolated from an endemic plant from Mt. Mayon. Deduce the amino acid sequence of the decapeptide given the following informations. Mercaptoethanol gave two pentapeptides F1 and F2. Chymotrypsin treatment of F1 releases S and a tetrapeptide (C,K,F,M) while F2 gave a dipeptide (M,S) and a tripeptide (C,F,K) F1 when treated with CNBr released a free homoserine lactone and a tetrapeptide. Trypsin treatment of F1 gave a tripeptide and a dipeptide. F2 treated with carboxypeptidase released free M while with trypsin gave free K and a tetrapeptide.arrow_forwardThe highly pathogenic anaerobic bacterium Clostridium perfringens is responsible for gas gangrene, a condition in which animal tissue structure is destroyed. This bacterium secretes an enzyme that efficiently catalyzes the hydrolysis of the peptide bond indicated in red: where X and Y are any of the 20 common amino acids. How does the secretion of this enzyme contribute to the invasiveness of this bacterium in human tissues? Why does thisenzyme not affect the bacterium itself?arrow_forward
- Help mearrow_forwardThe macrolide below is a bacteria produced toxin. The primer was acetyl-Co-A. Three possible extenders are also shown A) malonate-Co-A B) methylmalonate-Co-A and C) ethylmalonate-Co-A. Indicate which extenders were used using this format: XA yB zC Meaning x molecules of A, y molecules of B and z molecules of C A COA но CH3 но, CH3 COA H3C CH3 B но HO CH3 CH3 HO CH3 C COA но CH3 Enter Your Answer:arrow_forwardDescribe which enzymes are required for lactose and tryptophan metabolism in bacteria when lactose and tryptophan, respectively, are (a) present and (b) absent.arrow_forward
- The ribosome is the target for many important antibiotics. These drugs must discriminate between bacterial and eukaryotic ribosomes to achieve drug specificity and toxicity. For the two common antibiotics below, what is their mechanism of action and why are they more toxic to bacteria than eukaryotes? a) Tetracycline b) Erythromycinarrow_forwardYou have isolated a new endoglucanase enzyme. Through various enzymes assays, you are trying to determine the optimal conditions for this enzyme's activity. You make the following observations: i. when performing the assay at 40°C using buffers with different possibilities, you observe that the enzyme has no activity below pH 3 or above pH 11. You observe high activity at pH 6 and about 50% of this activity level at pH 5 and pH 7. ii. When performing the assay using a buffer at pH 6, you measure almost no activity at a temperature of 10°C. However, the activity steadily rises when tested at 20°C, 30°C, 40°C and 50°C, where the highest activity was measured, before declining at 60°C. At 70°C there is no measurable activity. Explain the meaning of these observations and identify the optimal pH and temperature conditions for the endoglucanase enzyme. Further more, explain why these observations occur based on your knowledge of the effects of pH and temperature on enzymes.arrow_forwardWhich of the following amino acids can act as nucleophiles in a protease active site (choose all that apply): a) Cysteine b) Alanine c) Leucine d) Serine e) Threoninearrow_forward
- You perform Michaelis-Menten kenetics on i) trypsin and ii) a mutant form of the same enzyme (a single amino acid has been changed). The specificity constant for the mutant was 10 times larger than for trypsin. a) Define the specificity constant and explain using this definition how a larger value might occur. b) Explain how, if at all, a non-competitive inhibitor of trypsin would affect the specificity constant.arrow_forwardD) What are the different substrate specificities of elastase, trypsin, and chymotrypsin? And, why, from a structural standpoint, do elastase, trypsin, and chymotrypsin have different substrate specificities?arrow_forwardWhy is a strong reducing agent, such as NaBH4, not suitable for use in the conjugation of an oligosaccharide to a protein?arrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
Human Anatomy & Physiology (11th Edition)BiologyISBN:9780134580999Author:Elaine N. Marieb, Katja N. HoehnPublisher:PEARSON
Biology 2eBiologyISBN:9781947172517Author:Matthew Douglas, Jung Choi, Mary Ann ClarkPublisher:OpenStax
Anatomy & PhysiologyBiologyISBN:9781259398629Author:McKinley, Michael P., O'loughlin, Valerie Dean, Bidle, Theresa StouterPublisher:Mcgraw Hill Education,
Molecular Biology of the Cell (Sixth Edition)BiologyISBN:9780815344322Author:Bruce Alberts, Alexander D. Johnson, Julian Lewis, David Morgan, Martin Raff, Keith Roberts, Peter WalterPublisher:W. W. Norton & Company
Laboratory Manual For Human Anatomy & PhysiologyBiologyISBN:9781260159363Author:Martin, Terry R., Prentice-craver, CynthiaPublisher:McGraw-Hill Publishing Co.
Inquiry Into Life (16th Edition)BiologyISBN:9781260231700Author:Sylvia S. Mader, Michael WindelspechtPublisher:McGraw Hill Education
Human Anatomy & Physiology (11th Edition)
Biology
ISBN:9780134580999
Author:Elaine N. Marieb, Katja N. Hoehn
Publisher:PEARSON
Biology 2e
Biology
ISBN:9781947172517
Author:Matthew Douglas, Jung Choi, Mary Ann Clark
Publisher:OpenStax
Anatomy & Physiology
Biology
ISBN:9781259398629
Author:McKinley, Michael P., O'loughlin, Valerie Dean, Bidle, Theresa Stouter
Publisher:Mcgraw Hill Education,
Molecular Biology of the Cell (Sixth Edition)
Biology
ISBN:9780815344322
Author:Bruce Alberts, Alexander D. Johnson, Julian Lewis, David Morgan, Martin Raff, Keith Roberts, Peter Walter
Publisher:W. W. Norton & Company
Laboratory Manual For Human Anatomy & Physiology
Biology
ISBN:9781260159363
Author:Martin, Terry R., Prentice-craver, Cynthia
Publisher:McGraw-Hill Publishing Co.
Inquiry Into Life (16th Edition)
Biology
ISBN:9781260231700
Author:Sylvia S. Mader, Michael Windelspecht
Publisher:McGraw Hill Education
Biochemical Tests-Part 1; Author: Southern Stacker;https://www.youtube.com/watch?v=a-i9vANfQWQ;License: Standard Youtube License