FUNDAMENTALS OF BIOCHEM.-NEXTGEN ACCESS
5th Edition
ISBN: 9781119661450
Author: Voet
Publisher: WILEY
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Chapter 12, Problem 32CQ
Summary Introduction
To explain: The reason why uncompetitive and mixed inhibitors are generally considered to be more effective in vivo than competitive inhibitors.
Concept introduction: Enzyme inhibitors are those that block the enzyme activity. Enzyme inhibitors are of several types.
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Students have asked these similar questions
The beta-lactamase hydrolyzes the lactam-ring in penicillin. Describe the mechanism
of hydrolysis, insuring to include the involvement of S, D, & K in the reaction sequence. Please help
To map the active site of beta-lactamase, the enzyme was hydrolyzed with trypsin to yield a hexapeptide (P1) with the following amino acids. Glu, Lys, Leu, Phe, Met, and Ser. Treatment of P1 with phenyl isothiocyanate yielded a PTH derivative of phenylalanine and a peptide (P2). Treatment of P1 with cyanogenbromide gave an acidic tetrapeptide (P3) and a dipeptide (P4).Treatment of P2 with 1-fluoro-2,4-dinitrobenzene, followed by complete hydrolysis, yields N-2,4-dinitrophenyl-Glu. P1, P2, and P3 contain the active site serine.
Why doesn't D in this hexapeptide not participate in the hydrolysis of the beta-lactam ring even though S, K, and D are involved in the catalyst?
To map the active site of -lactamase, the enzyme was hydrolyzed with trypsin to yield a hexapeptide (P1) with the following amino acids. Glu, Lys, Leu, Phe, Met, and Ser. Treatment of P1 with phenyl isothiocyanate yielded a PTH derivative of phenylalanine and a peptide (P2). Treatment of P1 with cyanogenbromide gave an acidic tetrapeptide (P3) and a dipeptide (P4).Treatment of P2 with 1-fluoro-2,4-dinitrobenzene, followed by complete hydrolysis, yields N-2,4-dinitrophenyl-Glu. P1, P2, and P3 contain the active site serine.
Using the experimental results described above derive the primary sequence of the active site hexapeptide. Please help!
Chapter 12 Solutions
FUNDAMENTALS OF BIOCHEM.-NEXTGEN ACCESS
Ch. 12 - Prob. 1ECh. 12 - Prob. 2ECh. 12 - Prob. 3ECh. 12 - Prob. 4ECh. 12 - 5. From the reaction data below, determine whether...Ch. 12 - Prob. 6ECh. 12 - 7. For an enzymatic reaction, draw curves that...Ch. 12 - 8. Explain why it is usually easier to calculate...Ch. 12 - Prob. 9ECh. 12 - 10. Identify the enzymes in Table 12-1 whose...
Ch. 12 - 11. Calculate KM and Vmax from the following...Ch. 12 - 12. Explain why each of the following data sets...Ch. 12 - 13. The KM for the reaction of chymotrypsin with...Ch. 12 - 14. Enzyme A catalyzes the reaction S ? P and has...Ch. 12 - 15. In a bisubstrute reaction, a small amount of...Ch. 12 - 16. In a bisubstrate reaction, a small amount of...Ch. 12 - Prob. 17ECh. 12 - 18. Molecule A is the substrate for enzyme X....Ch. 12 - 19. Determine the type of inhibition of an...Ch. 12 - 20. Estimate KI for a competitive inhibitor when...Ch. 12 - Prob. 21CQCh. 12 - 22 Is it necessary to know [E]T to determine (a)...Ch. 12 - 23. You are trying to determine the KM for an...Ch. 12 - 24. You are attempting to determine KM by...Ch. 12 - Prob. 25CQCh. 12 - 26. Enzyme X and enzyme Y catalyze the same...Ch. 12 - 27. Based on some preliminary measurements, you...Ch. 12 - 28. For the same enzyme sample described in...Ch. 12 - 29. For an enzyme catalyzed reaction, the presence...Ch. 12 - 30. Sphingosine-1-phosphate (S1P) is important for...Ch. 12 - 31. Ethanol in the body is oxidized to...Ch. 12 - Prob. 32CQCh. 12 - MORE TO EXPLORE What kind of inhibitor is...
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