Organic Chemistry (8th Edition)
8th Edition
ISBN: 9780134042282
Author: Paula Yurkanis Bruice
Publisher: PEARSON
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Textbook Question
Chapter 22.13, Problem 25P
What advantage does the enzyme gain by forming an imine?
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The hydrolysis of an ester can be sped up by both acidic and basic conditions. Aminolysis of an ester can be sped up by acidic conditions, but not by basic conditions. Explain why.
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COO
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CH₂
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Succinate
COO
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CH₂
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COO
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both a noncompetitive and an
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O an irreversible inhibitor
O a competitive inhibitor
Chapter 22 Solutions
Organic Chemistry (8th Edition)
Ch. 22.2 - Compare each of the mechanisms listed here with...Ch. 22.2 - Prob. 3PCh. 22.2 - Prob. 4PCh. 22.3 - a. Draw the mechanism for the following reaction...Ch. 22.5 - Prob. 7PCh. 22.5 - Propose a mechanism for the Co2+ catalyzed...Ch. 22.6 - Prob. 9PCh. 22.7 - Prob. 10PCh. 22.7 - Prob. 12PCh. 22.7 - Prob. 13P
Ch. 22.9 - Which of the following amino acid side chains can...Ch. 22.9 - Which of the following C-terminal peptide bonds is...Ch. 22.9 - Carboxypeptidase A has esterase activity as well...Ch. 22.10 - Arginine and lysine side chains fit into trypsins...Ch. 22.10 - Explain why serine proteases do not catalyze...Ch. 22.11 - If H2 18O is used in the hydrolysis reaction...Ch. 22.11 - Draw the pH-activity profile for an enzyme that...Ch. 22.12 - The pHactivity profile for glucose-6-phosphate...Ch. 22.12 - Prob. 23PCh. 22.13 - Draw the mechanism for the hydroxide ion-catalyzed...Ch. 22.13 - What advantage does the enzyme gain by forming an...Ch. 22.13 - Prob. 26PCh. 22.13 - Prob. 27PCh. 22.13 - Aldolase shows no activity if it is incubated with...Ch. 22 - Which of the following parameters would be...Ch. 22 - Prob. 29PCh. 22 - Prob. 30PCh. 22 - Prob. 31PCh. 22 - Indicate the type of catalysis that is occurring...Ch. 22 - The deuterium kinetic isotope effect (KH2O/KD2O)...Ch. 22 - Prob. 34PCh. 22 - Co2+ catalyzes the hydrolysis of the lactam shown...Ch. 22 - there are two kinds of aldolases. Class I...Ch. 22 - Prob. 37PCh. 22 - The hydrolysis of the ester shown here is...Ch. 22 - Prob. 39PCh. 22 - At pH = 12, the rate of hydrolysis of ester A is...Ch. 22 - 2-Acetoxycyclohexyl tosylate reacts with acetate...Ch. 22 - Proof that an imine was formed between aldolase...Ch. 22 - Prob. 43PCh. 22 - a. Explain why the alkyl halide shown here reacts...Ch. 22 - Triosephosphate isomerase (TIM) catalyzes the...
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- The substance where the enzyme reacts with? A. Substrate B. Inhibitor C. A & B D. Activator E. Productarrow_forwardWhat is an antioxidant enzyme? Why is catalase considered to be an antioxidant enzyme?arrow_forwardThe reactant in an enzyme-catalyzed reaction is called a cofactor. True or False True Falsearrow_forward
- Based on data attached please help with the following: -How does temperature affect the rate of the reaction? -How does the inhibitor affect the rate of the reaction?arrow_forwardActivation of a zymogen is by covalent modification. How might phosphorylation or dephosphorylation (also covalent modification) modify an enzyme to make it more active (or more inactive)?arrow_forward1. What reaction is catalyzed by the enzyme carbonic anhydrase? Which metal ion serves as a cofactor for carbonic anhydrase? Explain how this metal ion is able to assist in catalyzing the reaction. 2. In relation to enzymes, what is the difference between a cosubstrate and a prosthetic group? Give one example of each.arrow_forward
- Draw the structures of the substrate (pNPP) and of the inhibitors (Pi and Phe). Consider them in the fully deprotonated states. What similarities can you detect between each inhibitor and the substrate?arrow_forwardCompared to an uncatalyzed reaction, an enzyme-catalyzed reaction O produces different products. O requires a higher temperature. occurs at a faster rate. O uses less substrate. requires more energy.arrow_forward1. What is the role of initiator and inhibitor? 2. What are short stops?arrow_forward
- What is the mechanism of action of the antibiotic drug Sulfanilamide in terms of enzyme inhibition?arrow_forwardIdentify the modes of catalysis and when / why they occur• Acid-base • Covalent• Transition state stabilization• Catalysis by proximity • Catalysis by strain• Lock & key is better seen as describing substrate binding to active sitearrow_forwardNeostigmine is an inhibitor of acetylcholinesterase. The enzyme attempts to catalyse the same reaction on neostigmine as it does with acetylcholine. However, a stable intermediate is formed which prevents completion of the process and which results in a molecule being covalently linked to the active site. Identify (draw) the stable intermediate and explain why it is stable.arrow_forward
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