Biochemistry
6th Edition
ISBN: 9781305577206
Author: Reginald H. Garrett, Charles M. Grisham
Publisher: Cengage Learning
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Chapter 19, Problem 20P
Interpretation Introduction
To write:
Post translational modification via Michael addition.
Introduction:
The tricarboxylic acid (TCA) cycle consist of a series of various
The Krebs cycle is called as the citric acid cycle as the
The Michael reaction also known as Michael addition in which there is addition of a nucleophile of a carbanion takes place to the a, ß unsaturated carbonyl compound.
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Trypsin uses a nearly identical mechanism as chymotrypsin (including the catalytic triad his57-ser195-asp102. beginning with the enzyme substrate complex draw the complete steps in the trypsin mechanism that occur to release the first product and create the acyl enzyme intermediate in the trypsin active site. The substrate for trypsin to be used is gly-lys-gly-ala
(i)
Describe the mechanism of chymotrypsin in cleaving a peptide bond, highlighting the
roles of the catalytice triad for the two phases of the catalytic reactions. Explain the
significance of the oxyanion hole for the catalysis.
(ii)
All serine proteases contain the catalytic triad and these amino acids are positioned in
the exact same conformation. Since this is true, why do trypsin and chymotrypsin
have such different substrate specificity? What features of the enzyme allow for this
situation?
In serine protease catalytic triad mechanism, the first and second products that leaves the active site are
Carboxylic acid and amide respectively
Amide and carboxylic acid respectively
Ester and amide respectively
Carboxylic acid and ester respectively
Chapter 19 Solutions
Biochemistry
Ch. 19 - Radiolabeling with 14C-Glutamate Describe the...Ch. 19 - Prob. 2PCh. 19 - Assessing the Effect of Active-Site...Ch. 19 - Understanding the Mechanism of the -Ketoglutarate...Ch. 19 - Understanding the Action of Fluoroacetate on the...Ch. 19 - Prob. 6PCh. 19 - Prob. 7PCh. 19 - Prob. 8PCh. 19 - Prob. 9PCh. 19 - Prob. 10P
Ch. 19 - Prob. 11PCh. 19 - Prob. 12PCh. 19 - Prob. 13PCh. 19 - Prob. 14PCh. 19 - Prob. 15PCh. 19 - Prob. 16PCh. 19 - Understanding the Oxidation of Glucose and Its...Ch. 19 - Prob. 18PCh. 19 - Prob. 19PCh. 19 - Prob. 20PCh. 19 - Complete oxidation of a 16-carbon fatty acid can...Ch. 19 - Study Figure 19.18 and decide which of the...Ch. 19 - Prob. 23P
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- Consider the role of Histidine in the Serine protease mechanism and sketch a plot showing the predicted pH profile of chymotrypsin which has a pH optimum of approximately ~8. The pk, for the His in the catalytic triad is 7.3 in free chymotrypsin which increases to greater than 8 with a bound peptide. Be sure to label the plot axes and indicate the pka of His on the plot,arrow_forwardUsing the ActiveModel for phosphofructokinase (Trypanosoma), describe the difference between the APO1, AP02, and holoenzyme conformations.arrow_forwardb. Compounds A, B, C, and D are known to be intermediates in the pathway for production of protein E. To determine where the block in protein-E production occurred in each individual, the various intermediates were given to each individuals cel Is in culture. After a few weeks of growth with the intermediate, the cells were assayed for the production of protein E. The results for each individuals cells are given in the following table. A plus sign means that protein E was produced after the cells were given the intermediate listed at the top of the column. A minus sign means that the cells still could not produce protein E even after being exposed to the intermediate at the top of the column. Denote the point in the pathway in which each individual is blocked.arrow_forward
- a. Compounds A, B, C, and D are known to be intermediates in the pathway for production of protein E. To determine where the block in protein-E production occurred in each individual, the various intermediates were given to each individuals cel Is in culture. After a few weeks of growth with the intermediate, the cells were assayed for the production of protein E. The results for each individuals cells are given in the following table. A plus sign means that protein E was produced after the cells were given the intermediate listed at the top of the column. A minus sign means that the cells still could not produce protein E even after being exposed to the intermediate at the top of the column. Draw the pathway leading to the production of protein E.arrow_forward#1 Specify the role each of the following amino acids play within the crystal structure and/or active site for Be as specific as possible, with pictures (and mechanistic arrows) as necessary. His11 Arg140 Glu89 Trp68 #2 Provide a step-wise mechanism for the reaction Bisphosphoglycerate mutase catalyzes, using the amino acids responsible for aiding in catalysis. You do not need to add surrounding amino acids that aid in substrate specificity. (drawn out)arrow_forwardUsing the catalytic mechanism of serine proteases, draw and label a reaction coordinate diagram/graph of the chymotrypsin-catalyzed hydrolysis of a peptide bond.arrow_forward
- A diagram of the residues defining the binding site of 2,3-bis-phosphoglycerate (BPG) is 2. ( shown on the right. Given the mutation in Hb Great Lakes, Leu(B68)His, show on either O2 binding plot whether its p(O2)50% will be altered in the presence of a 10-fold excess of BPG and in which direction with respect to that of HbA. Explain. B1 B1-subunit His 143 Lys 82 His 2 BPG a-NH,* a-NH,* B2-subunit Lys 82 His 2 His 143 B2arrow_forwardLysozyme is an antibacterial enzyme found in animals. Residues Asp 101 and Arg 114 are required for efficient catalysis, although they are located at some distance from the active site Glu 35 and Asp 52. Substituting Ala for either Asp 101 or Arg 114 does not significantly alter the enzyme's tertiary structure, but significantly reduces its catalytic activity. Explain.arrow_forward(c) On the right is a diagram of the ac tive site of E. coli aspartate aminotrans- ferase illustrating the cofactor pyridoxal phosphate (labeled PLP) with the dicar- boxylic acid maleate (labeled MAL) bound in the active site. The structural formula of maleate is shown on the right. Am 194 MAL Arg292 Arg386 Ilx17 Lauf 'coo- H get H Coo- Maleate (c1) Draw the structure of L-aspartate and draw a border around the atoms in the amino acid that maleate simulates. (c2) Identify the active site residues that make hydrogen bonds and electrostatic interac- tions with the oxygen atoms of the carboxylate groups of maleate in the diagram above. Identify the carboxylate groups according to the numbering in the diagram of maleate above. Indicate the hydrogen donor groups of the active site residues. (C3) Compare and draw the structures of L-Arg and L-Lys. On the basis of the diagram why does replacement of an arginine for a lysine have an effect on substrate binding to AspAT? (c4) Of the mutant…arrow_forward
- Escherichia coli Fpg protein is responsible for removing damaged DNA base pairs such as C8-oxoguanine (8-oxoG). The catalytic mechanism is believed to involve the formation of a transient Schiff base intermediate formed between DNA base the N-terminal proline residue. Draw the structure of PTH-derivative that is formed after Fpg is subjected to one cycle of Edman degradation.arrow_forwardA chain NH3 NH3 B chain Gly Phe 2. The protein pictured below is bovine insulin. Determine the number and the size of the fragments that would be generated upon treatment with the following: İle Val Val Asn Gln Gln 5 Ġln 5 His look for the cleavage points (a) without DTT and (b) with DTT. Cys Leu Cys S-S Cys Without DTT With DTT Ala Ģly Ser Ser Trypsin 10 Val 10 His Cys Leu Chymotrypsin Ser Val Leu Glu BrCN Tyr Ala 15 Gln 15 Leu Leu Тyr Ġlu Leu Ásn Val Тyr Cys 20 Çys 20 Gly Asn Glu Arg Reagent (source) Trypsin (bovine pancrease) Chymotrypsin (bovine pancrease) Staphylococcus V8 protease Pepsin (porcine pancrease) Cyanogen bromide (chemical)(CnBr) Specificity Lys, Arg (C) Phe, Trp, Tyr (C) Glu, Asp (C) Phe, Trp, Tyr (N) Met (C) Gly Phe 25 Phe Тyr Thr Pro Lys 30 Álaarrow_forward
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