Concept explainers
(a)
To propose:
The strong inhibitory property of the peptide pepstatin
Introduction:
Aspartic proteases include the protease enzymes which uses two very active aspartic acid complexes for the cleavage reaction of the peptide substrates. Pepstatin is a naturally present in the cell which has hexa-peptide structure with amino acid Statine and thus generally inhibits aspartyl proteases.
(b)
To explain:
Whether the pepstatin exhibit inhibits the HIV-1 protease or not.
Introduction:
Aspartic proteases include the protease enzymes which uses two very active aspartic acid complexes for the cleavage reaction of the peptide substrates. Pepstatin is a naturally present in the cell which has hexa-peptide structure with amino acid Statine and thus generally inhibits aspartyl proteases.
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Biochemistry
- Answers to all problems are at the end οΓthis book. Detailed solutions are available in the Student Solutions Manual. Study Guide, and Problems Book. Characterizing a Covalent Enzyme Inhibitor Tosyl-L-phenylalanme cfaloromethyl ketone (TPCK) specifically inhibits chymotrypsin by covalently labeling His57 Propose a mechanism for the inactivation reaction, indicating the structure of the produce(s). State why this inhibitor is specific tor cJiymotrypsin. Propose a reagent based on the structure of TPCK that might be an effective inhibitor of trypsin.arrow_forwardAnswers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. Examine the ActiveModle for N-myristoylt ranjsferase and explain the mechanism of N-myristolation.arrow_forwardAnswers to all problems are at the end οΓthis book. Detailed solutions are available in the Student Solutions Manual. Study Guide, and Problems Book. Review the mechanisms of the .serine and aspartic proteases, and compare these two mechanisms carefully. Are there steps m die mechanisms that are similar? How are they similar? How are they different? Suggest experiments that could support or refute your hypotheses.arrow_forward
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- Answers to all problems are at the end οΓthis book. Detailed solutions are available in the Student Solutions Manual. Study Guide, and Problems Book. Using Site-Direcled Muta.nts to Understand an Enzyme Mechanism In this chapter, the exponent in which Craik and Rutter replaced Asp102 with Asn in trypsin (reducing activity 10,000 -fold) was discussed. On the basis of your knowledge of the catalytic triad structure in trypsin, suggest a structure for the “uncatalytic triad of Asn-His-Ser in this mutant enzyme. Explain why the structure you have proposed explains the reduced activity of the mutant trypsin. See the original journal articles (Sprang, et al., 1987. Science 237:905-913) to Craik, et al., 1987. Scieence 237:909-913) to see Craik and Rutter's answer to this question.arrow_forwardAnswers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. (Research Problem) The Nature and Roles of Linear Motifs in Proteins In addition to domains and modules, there are other significant sequence patterns in proteins—known as linear motifs—that are associated with a particular function. Consult the biochemical literature to answer the following questions: 1. What are linear motifs? 2. How are they different from domains?. 3. What are their functions? 4. How can they be characterized? 5. There are several papers that are good starting points for this problem. Neduva, V., and Russell, R., 2005. Linear motifs: evolutionary interaction switches. FEBS Letters 579:3342-3345. Gibson, T., 2009. Cell regulation: determined to signal discrete cooperation. Trends in Biochemical Sciences 34:471-482. Diella, K. Haslam, N., Chica., C. et aL, 2009. Understanding eukaryotic linear motifs and their role in cell signaling and regulation. Frontiers of Bioscience 13:6580-6603.arrow_forwardAnswers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. Why zymogens Are Advantageous Why do you suppose proteolytic enzymes are- often synthesized as inactive zymogens?arrow_forward
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- BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage Learning