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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Chapter 19 Solutions
Biochemistry
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- cis-Vaccenate is an 18-carbon unsaturated fatty acid abundant in E. coli membrane lipids. Propose a metabolic route for synthesis of this fatty acid, in light of the fact that stearic acid, the C18 saturated analogous fatty acid, is virtually absent from E. coli lipids.arrow_forward(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?arrow_forwardWhy does enzyme x catalyze the formation of the phosphodiester bond and please explain how nucleas recognizes phospjodiester bondsarrow_forward
- 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 respectivelyarrow_forwardThe S3’ pocket on PfSUB1 (attached) contains the side chains of Lys465 and Tyr427. Researchers discovered that the Km for substrates with acidic residues in the P3’ position are much lower than those with nonpolar resides at the P3’ position in PfSUB1. Explain the Km data.arrow_forwardConsider 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_forward
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- b. 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_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#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_forward
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