FUNDAMENTALS OF BIOCHEM.-NEXTGEN ACCESS
5th Edition
ISBN: 9781119661450
Author: Voet
Publisher: WILEY
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Chapter 19, Problem 7E
Summary Introduction
To determine: The common names of the given enzymes and in which order do they act.
Concept introduction:
The process of conversion of light energy to chemical energy occurs in two phases of reactions, that is, light-dependent reaction and light-independent reaction. Photosynthesis process begins when energy is absorbed by the photosystem. Photosystem is the very large complex of molecules that contain pigments, proteins, and cofactors which are embedded in the thylakoid membrane. There are two types of photosystems namely PS I and PSII.
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You have isolated a protein and determined that the native molecular weight of the holoenzyme is 160 kD using size exclusion chromatography. Analysis of this protein using SDS-PAGE revealed 2 bands, one at 100 kD and one at 30 kD.
Describe the architecture of the polypeptide component of this enzyme.
In a cell free preparation of beta-lactamase, penicillin is hydrolyzed in a D2O enriched assay. After one round of catalysis, where would you anticipate finding Deuterium?
please help thank you
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.
question: the b-lactamase hydrolyzes the lactam-ring in antibiotics like penicillin. Describe the mechanism, of hydrolysis, insuring to include the involvement of S, D, and K in the reaction sequence. Please help!
Chapter 19 Solutions
FUNDAMENTALS OF BIOCHEM.-NEXTGEN ACCESS
Ch. 19 - Prob. 1ECh. 19 - 2. Green sulfur bacteria use H2S as an electron...Ch. 19 - 3. The “red tide” is a massive proliferation of...Ch. 19 - 4. Explain why the chlorophylls in...Ch. 19 - Prob. 5ECh. 19 - Prob. 6ECh. 19 - Prob. 7ECh. 19 - 8. H218O is added to a suspension of chloroplasts...Ch. 19 - 9 Describe the functional similarities between the...Ch. 19 - Prob. 10E
Ch. 19 - Prob. 11ECh. 19 - Prob. 12ECh. 19 - 13. Although tile net equation for photosynthesis...Ch. 19 - 14. Why is it possible for chloroplasts to absorb...Ch. 19 - 15. Predict the effect of witling myxothiazol, an...Ch. 19 - Prob. 16ECh. 19 - Prob. 17ECh. 19 - 18. Chloroplast ATP synthase contains 14 c...Ch. 19 - 19. Predict the effect of an uncoupler such as...Ch. 19 - Prob. 20ECh. 19 - Prob. 21ECh. 19 - 22. Would the activity of the A, thaliana K+...Ch. 19 - Prob. 23ECh. 19 - Prob. 24ECh. 19 - Prob. 25ECh. 19 - 26. The shell of the cyanobacterial carboxysome...Ch. 19 - 27. In an effort to increase the efficiency of...Ch. 19 - 28. Describe the effects of an increase in oxygen...Ch. 19 - 29. The leaves of some species of desert plants...Ch. 19 - 30. Plants must obtain CO2 but avoid the loss of...Ch. 19 - 31. How might the increase in atmospheric [CO2]...Ch. 19 - Prob. 32ECh. 19 - 33. Chlorophyll f, which occurs in some species of...Ch. 19 - 34. The cyanobacterium Oscillatoria sancta appears...Ch. 19 - Prob. 35CQCh. 19 - Prob. 36CQCh. 19 - 37. Under conditions of very high light intensity,...Ch. 19 - 38. Which of the mechanisms for dissipating light...Ch. 19 - 39. Calculate the energy cost of the Calvin cycle...Ch. 19 - 40. Oil is a major energy-storage molecule in most...Ch. 19 - 41. One aspect of climate change is that average...Ch. 19 - 42. Experiments to address the day-night...Ch. 19 - 43. If a C3 plant and a C4 plant are placed...
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- Three of these amino acids participate in the proteolytic hydrolysis of polypeptides. Show the charge-relay network generated by the serine proteases and identify the nucleophilic species that initiates the hydrolysis. please help!arrow_forwardYou have isolated a protein and determined that the native molecular weight of the holoenzyme is 160 kD using size exclusion chromatography. Analysis of this protein using SDS-PAGE revealed 2 bands, one at 100 kD and one at 30 kD. 1. Describe the architecture of the polypeptide component of this enzyme. 2. The enzyme was found to be 0.829% NAD (by weight). What further can be said regarding the architecture? can you please help me with question number 2arrow_forwardTo 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. Question: although S, K, and D are involved in the catalysis, the E in this hexapeptide does not participate in the hydrolysis of the b-lactam ring. Why is that?arrow_forward
- 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. a) Using the experimental results described below deduce the primary sequence of the active site hexapeptide. 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. please help!arrow_forwardThe 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 helparrow_forwardTo 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?arrow_forward
- 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!arrow_forwardWhich type of enzyme catalyses the following reaction? oxidoreductase, transferase, hydrolase, lyase, isomerase, or ligase.arrow_forward+NH+ CO₂ +P H₂N + ATP H₂N NH₂ +ADParrow_forward
- Which type of enzyme catalyses the following reaction? oxidoreductase, transferase, hydrolase, lyase, isomerase, or ligase.arrow_forwardWhich features of the curves in Figure 30-2 indicates that the enzyme is not consumed in the overall reaction? ES is lower in energy that E + S and EP is lower in energy than E + P. What does this tell you about the stability of ES versus E + S and EP versus E + P.arrow_forwardLooking at the figure 30-5 what intermolecular forces are present between the substrate and the enzyme and the substrate and cofactors.arrow_forward
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