Biochemistry
9th Edition
ISBN: 9781305961135
Author: Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher: Cengage Learning
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Chapter 23, Problem 48RE
RECALL Compare the fates of the products of purine and pyrimidine catabolism.
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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?
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Chapter 23 Solutions
Biochemistry
Ch. 23 - RECALL What kinds of organisms can fix nitrogen?...Ch. 23 - RECALL How is nitrogen fixed (converted from...Ch. 23 - Prob. 3RECh. 23 - Prob. 4RECh. 23 - Prob. 5RECh. 23 - Prob. 6RECh. 23 - Prob. 7RECh. 23 - REFLECT AND APPLY Metabolic cycles are rather...Ch. 23 - RECALL What is the relationship between...Ch. 23 - Prob. 10RE
Ch. 23 - Prob. 11RECh. 23 - Prob. 12RECh. 23 - Prob. 13RECh. 23 - Prob. 14RECh. 23 - Prob. 15RECh. 23 - Prob. 16RECh. 23 - Prob. 17RECh. 23 - Prob. 18RECh. 23 - REFLECT AND APPLY Sulfanilamide and related sulfa...Ch. 23 - Prob. 20RECh. 23 - Prob. 21RECh. 23 - Prob. 22RECh. 23 - Prob. 23RECh. 23 - Prob. 24RECh. 23 - RECALL Describe citrulline and ornithine based on...Ch. 23 - Prob. 26RECh. 23 - Prob. 27RECh. 23 - Prob. 28RECh. 23 - Prob. 29RECh. 23 - Prob. 30RECh. 23 - Prob. 31RECh. 23 - Prob. 32RECh. 23 - Prob. 33RECh. 23 - Prob. 34RECh. 23 - Prob. 35RECh. 23 - Prob. 36RECh. 23 - REFLECT AND APPLY Why is it better, when running a...Ch. 23 - REFLECT AND APPLY Argue logically that the urea...Ch. 23 - BIOCHEMICAL CONNECTIONS How is the importance of...Ch. 23 - Prob. 40RECh. 23 - RECALL What is the structural difference between...Ch. 23 - Prob. 42RECh. 23 - RECALL Does the conversion of IMP to GMP use or...Ch. 23 - RECALL Discuss the role of feedback inhibition in...Ch. 23 - RECALL How many high-energy phosphate bonds must...Ch. 23 - REFLECT AND APPLY Why do most mammals, other than...Ch. 23 - Prob. 47RECh. 23 - RECALL Compare the fates of the products of purine...Ch. 23 - Prob. 49RECh. 23 - Prob. 50RECh. 23 - REFLECT AND APPLY Chemotherapy patients receiving...
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- 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!arrow_forwardThree 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_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. 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_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. 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_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. 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_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. 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_forwardWhich 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_forward
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