FUNDAMENTALS OF BIOCHEM.-NEXTGEN ACCESS
5th Edition
ISBN: 9781119661450
Author: Voet
Publisher: WILEY
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Question
Chapter 12, Problem 4E
Summary Introduction
To calculate: The half-life in years for the reaction 2 X à Y.
Concept introduction: Half-life period is defined as the time required for a substance to reduce to half of its initial concentration. Half life is independent of the initial concentration of the reaction. The reactions where there are two molecules of reactant are called as second-order reactions and are also called as bimolecular reactions.
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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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