Biochemistry: Concepts and Connections (2nd Edition)
2nd Edition
ISBN: 9780134641621
Author: Dean R. Appling, Spencer J. Anthony-Cahill, Christopher K. Mathews
Publisher: PEARSON
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Chapter 26, Problem 16P
Interpretation Introduction
Interpretation:
The reason for histone deacetylase action to repress transcription should be explained.
Concept Introduction:
Acetylation and deacetylation of histones play essential role in regulating gene expression. Histone acetyltransferase (HAT) adds acetyl group to the conserved lysine residues whereas histone deacetylase (HDAC) has a reverse action i.e. removal of acetyl group. Both the enzymes play an important role in the regulation of gene expression and chromatin modeling.
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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 26 Solutions
Biochemistry: Concepts and Connections (2nd Edition)
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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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