Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
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Question
Chapter 20, Problem 11P
Interpretation Introduction
Interpretation:
The reason for the decrease in activity of Rubisco in an atmosphere devoid of CO2 but rich in O2, should be determined.
Concept introduction:
Ribulose 1, 5-bisphosphate carboxylase/ oxygenase is a key enzyme in Calvin cycle as well as photosynthesis. During the process of carbon fixation, rubisco converts inorganic carbon dioxide into an organic molecule in the first stage of the Calvin cycle.
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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 20 Solutions
Biochemistry
Ch. 20 - Prob. 1PCh. 20 - Prob. 2PCh. 20 - Prob. 3PCh. 20 - Prob. 4PCh. 20 - Prob. 5PCh. 20 - Prob. 6PCh. 20 - Prob. 7PCh. 20 - Prob. 8PCh. 20 - Prob. 9PCh. 20 - Prob. 10P
Ch. 20 - Prob. 11PCh. 20 - Prob. 12PCh. 20 - Prob. 13PCh. 20 - Prob. 14PCh. 20 - Prob. 15PCh. 20 - Prob. 16PCh. 20 - Prob. 17PCh. 20 - Prob. 18PCh. 20 - Prob. 19PCh. 20 - Prob. 20PCh. 20 - Prob. 21PCh. 20 - Prob. 22PCh. 20 - Prob. 23PCh. 20 - Prob. 24PCh. 20 - Prob. 25PCh. 20 - Prob. 26PCh. 20 - Prob. 27PCh. 20 - Prob. 28PCh. 20 - Prob. 29PCh. 20 - Prob. 30PCh. 20 - Prob. 31PCh. 20 - Prob. 32PCh. 20 - Prob. 33PCh. 20 - Prob. 34PCh. 20 - Prob. 35PCh. 20 - Prob. 36PCh. 20 - Prob. 37PCh. 20 - Prob. 38PCh. 20 - Prob. 39PCh. 20 - Prob. 40PCh. 20 - Prob. 41PCh. 20 - Prob. 42PCh. 20 - Prob. 43PCh. 20 - Prob. 44PCh. 20 - Prob. 45PCh. 20 - Prob. 46PCh. 20 - Prob. 47PCh. 20 - Prob. 48P
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- Which 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_forwardprovide short answers to the followings Urgent!arrow_forward
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