Organic Chemistry (8th Edition)
8th Edition
ISBN: 9780134042282
Author: Paula Yurkanis Bruice
Publisher: PEARSON
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Chapter 28.6, Problem 21P
Chorismate mutase is an enzyme that promotes a pericyclic reaction by forcing the substrate to assume the conformation needed for the reaction. The product of the pericyclic reaction is prephenate that is subsequently converted into the amino acids phenylalanine and tyrosine. What kind of a pericyclic reaction does chorismate mutase catalyze?
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Chapter 28 Solutions
Organic Chemistry (8th Edition)
Ch. 28.1 - Prob. 1PCh. 28.2 - Prob. 2PCh. 28.2 - Prob. 3PCh. 28.2 - Give a molecular orbital description for each of...Ch. 28.3 - Prob. 5PCh. 28.3 - Prob. 6PCh. 28.3 - Prob. 7PCh. 28.3 - Prob. 8PCh. 28.4 - Prob. 10PCh. 28.4 - Prob. 11P
Ch. 28.5 - Prob. 12PCh. 28.5 - a. Draw the product of the following reaction: b....Ch. 28.5 - Prob. 14PCh. 28.5 - Prob. 15PCh. 28.5 - Prob. 17PCh. 28.5 - Prob. 18PCh. 28.6 - Prob. 19PCh. 28.6 - Explain why the hydrogen and the methyl...Ch. 28.6 - Chorismate mutase is an enzyme that promotes a...Ch. 28.7 - Convince yourself that the TE-AC method for...Ch. 28 - Draw the product of each of the following...Ch. 28 - Draw the product of each of the following...Ch. 28 - Prob. 25PCh. 28 - Show how norbornance can be prepared from...Ch. 28 - Prob. 27PCh. 28 - Prob. 28PCh. 28 - Draw the product of each of the following...Ch. 28 - Prob. 30PCh. 28 - Prob. 31PCh. 28 - Prob. 32PCh. 28 - Prob. 33PCh. 28 - When the following compound is heated, a product...Ch. 28 - Prob. 35PCh. 28 - Propose a mechanism for the following reaction:Ch. 28 - Prob. 37PCh. 28 - Prob. 38PCh. 28 - Prob. 39PCh. 28 - Prob. 40PCh. 28 - If isomer A is heated to about 100 C, a mixture of...Ch. 28 - Propose a mechanism for the following reaction:Ch. 28 - Prob. 43PCh. 28 - A student found that heating any one of the...Ch. 28 - Prob. 45PCh. 28 - Prob. 46PCh. 28 - Prob. 47P
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- Describe the importance of zymogens in the body. Give an example of an enzyme that has a zymogen.arrow_forwardA chemist wanted to test his hypothesis that the disulfide bridges that form in many proteins do so after the minimum energy conformation of the protein has been achieved. He treated a sample of an enzyme that contained four disulfide bridges with 2-mercaptoethanol and then added urea to denature the enzyme. He slowly removed these reagents so that the enzyme could re-fold and re-form the disulfide bridges. The enzyme he recovered had 80% of its original activity. What would be the percent activity in the recovered enzyme if disulfide bridge formation were entirely random rather than determined by the tertiary structure? Does this experiment support his hypothesis?arrow_forwardThe hydrolysis of pyrophosphate to orthophosphate drives biosynthetic reactions such as DNA synthesis. In Escherichia coli, a pyrophosphatase catalyzes this hydrolytic reaction. The pyrophosphatase has a mass of 120 kDa and consists of six identical subunits. A unit of activity for this enzyme, U, is the amount of enzyme that hydrolyzes 10 umol of pyrophosphate in 15 minutes. The purified enzyme has a Vnax of 2800 U per milligram of enzyme. When (S] >> KM, how many micromoles of substrate can 1 mg of enzyme hydrolyze per second? Vnax = umol -s. mg- If cach enzyme subunit has one active site, how many micromoles of active sites, or (E]r, are there in 1 mg of enzyme? (Er = umol - mg-arrow_forward
- The following experimental data were collected during a study of the catalytic activity of an intestinalpeptidase with the substrate glycylglycine: Glycylglycine + H2O → 2 glycine [S] (mM) Rate of product formation (mol/min) 1.5 0.21 2.0 0.24 3.0 0.28 4.0 0.33 8.0 0.40 16.0 0.45 Use the graphical analysis (Lineweaver-Burk plot and equation) to determine the Km and Vmax for this enzyme preparation and substrate.arrow_forwardThe substrate dissociation constant, Ks, is k-1/k1. What do large values of this constant mean? That the formation of product will be fast Strong binding between enzyme and substrate that the reaction is unimolecular Weak binding between enzyme and substratearrow_forwardIt is known that the amino acid at position 523 of the cyclooxygenase enzyme is part of the active site. In the isoenzyme COX-1, this amino acid is isoleucine, whereas in COX-2, it is valine. Suggest how such information could be used in the design of drugs that selectively inhibit COX-2.arrow_forward
- the conversion of the amino acid phenylalanine into non-harmful tyrosine is mutated and doesn't work as well (or at all). Phenylalanine will still break down into tyrosine by itself, ol because this is a favorable reaction. Why is the non-functional enzyme a problem? Explain in a few sentences. 3. The disease Phenylketonuria (or PKU) occurs when the enzyme that helps to catalyze O p HOo (pn) O pe oHe avl lls sew.i Snde (a)H noitas on ol woisd sidst nos stolgno ta T b e sd linw ps fertt sro.nalom ni encbeono mundiups sis novi 2noitetnono uTeeg os s oulev THI utinogmet cseo.o 8880 4. Consider the following reaction, which is exothermic: C2H4 (g) + Br2 (g) → C2H¾Br2 (g) ΔΗ< Predict the effect of each of the following perturbations (shift right/products, shift left/reactants, or no effect) using Le Chatelier's principle a. The reaction temperature is increased: b. The reaction volume is decreased: C. More bromine gas is added: d. The reaction is done in the presence of helium: e. C2H4BR2…arrow_forwardEnzymen catalysis mechanism and examplesarrow_forwardProteins are thermodynamically unstable molecules since the Delta G of hydrolysis is quite negative. However, most proteins are not degraded unless they come into contact with proteases in cells. What is the reasoning for this paradox? The reaction is endergonic and will not proceed without energy. There is very little water inside cells to react with protein molecules. The free energy change doesn't reveal anything about the rate of the reaction. The concentration of proteins are low which allows them to be more stable.arrow_forward
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