EP ESSENTIAL ORG.CHEM.-MOD.MASTERING
3rd Edition
ISBN: 9780133858501
Author: Bruice
Publisher: PEARSON CO
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Textbook Question
Chapter 18.3, Problem 3P
Which of the following amino acid side chains can aid the departure of a leaving group?
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Chapter 18 Solutions
EP ESSENTIAL ORG.CHEM.-MOD.MASTERING
Ch. 18.1 - Prob. 1PCh. 18.2 - If H218O were used to hydrolyze lysozyme, which...Ch. 18.3 - Which of the following amino acid side chains can...Ch. 18.3 - Arginine and lysine side chains fit into trypsins...Ch. 18.4 - Which of the following amino acid side chains can...Ch. 18.4 - Prob. 6PCh. 18.5 - Prob. 7PCh. 18.5 - Draw the mechanism for the hydroxide-ion-catalyzed...Ch. 18.5 - What advantage does the enzyme gain by forming an...Ch. 18.7 - Prob. 10P
Ch. 18.7 - Prob. 11PCh. 18.8 - How many conjugated double bonds are there in a....Ch. 18.8 - Instead of adding to the 4a-position and...Ch. 18.8 - In succinate dehydrogenase, FAD is covalently...Ch. 18.8 - Prob. 15PCh. 18.9 - Acetolactate synthase is another TPP-requiring...Ch. 18.9 - Acetolactate synthase can also transfer the acyl...Ch. 18.9 - Prob. 18PCh. 18.9 - Prob. 19PCh. 18.10 - Prob. 21PCh. 18.11 - Prob. 23PCh. 18.11 - Which compound is more easily decarboxylated?Ch. 18.11 - Explain why the ability of PLP to catalyze an...Ch. 18.11 - Explain why the ability of PLP to catalyze an...Ch. 18.12 - What groups are interchanged in the following...Ch. 18.13 - Why is the coenzyme called tetrahydrofolate?Ch. 18.13 - What amino acid is formed by the following...Ch. 18.13 - How do the structures of tetrahydrofolate and...Ch. 18.13 - What is the source of the methyl group in...Ch. 18 - Prob. 32PCh. 18 - Prob. 33PCh. 18 - From what vitamins are the following coenzymes...Ch. 18 - Prob. 35PCh. 18 - For each of the following reaction, name both the...Ch. 18 - Explain why serine proteases do not catalyze...Ch. 18 - Prob. 38PCh. 18 - For each of the following enzyme catalyzed...Ch. 18 - Trisephosphate isomerase (TIM) catalyzes the...Ch. 18 - Prob. 41PCh. 18 - What acyl groups have we seen transferred by...Ch. 18 - When UMP is dissolved in T2O, exchange of T for H...Ch. 18 - Prob. 44PCh. 18 - When transaminated, the three branched-chain amino...Ch. 18 - Aldolase shows no activity if it is incubated with...
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- Which of the following amino acid side chains can form an imine with a substrate?arrow_forwardExplain why the rate of aminolysis of an ester cannot be increased by H+, HO-, or RO-.arrow_forwardNet charge and isoelectric point of an amino acid with an ionizable side group.Consider the net charge and isoelectric point of an amino acid with ionizable side (R-) group.(a) Identify the acidic amino acid(s) capable of having a negatively charged carboxyl side group.(b) Identify the basic amino acid(s) capable of having a positively charged amino side group.(c) For an amino acid with a side (R-) chain that can ionize to a negative charge, derive a general expression in terms of measured pH and known pKa values of α-carboxyla-amino (pKca), α-amino(pKaa),and side group (pKRa), respectively, for the net charge of an amino acid Consider the net charge and isoelectric point of an amino acid with ionizable side (R-) group.(d) For an amino acid with a side (R-) chain that can ionize to a positive charge, derive a general expression in terms of measured pH and known pKa values ofα-carboxyl (pKca), α-amino (pKaa), and side group (pKRa), respectively, for the net charge of the amino acid.(e)…arrow_forward
- Reaction of the a-carboxyl group of an amino acid or peptide with phenylisothiocyanate allows for the determination of the amino acid residue in the N- terminus of an unknown peptide O True O Falsearrow_forwardSeveral compounds have been found to inhibit -lactamase, and drugs based on these compounds can be taken in combination with penicillins and cephalosporins to restore their effectiveness when resistance is known to be a problem. The commonly prescribed formulation called Augmentin is a combination of the -lactamase inhibitor shown below with amoxicillin (shown above). It is used to treat childhood ear infections when resistance is suspected, and many kids know it as the white liquid that tastes like bananas. Which of the statements below are true statements? 1. The stereochemistry of the fusion between the four-and five-membered rings in the inhibitor and amoxicillin are different. 2. The inhibitor possesses enol ether and allylic alcohol functional groups while the antibiotic possesses a phenol and a secondary amide functional group. 3. Neither the inhibitor nor the antibiotic contains strained rings. 4. Both 1 and 2 are true.arrow_forwardThe reaction of an ester with an amine is not as slow as the reaction of an ester with water or an alcohol. Explain with reason. Explain why the rate of aminolysis of an ester cannot be increased by H+, OH- or OR-. How can you activate the carboxylic acid? Is acid catalyzed hydrolysis of acetamide a reversible or an irreversible reaction. Explain.arrow_forward
- Serine esterase contains a catalytic triad at its active site. Which amino acid in serine esterase is responsible for mediating general acid catalysis for the breakdown of tetrahedral intermediate to the carboxyl product? Explain.arrow_forwardPyridoxal phosphate facilitates the stabilization of a carbanion by charge shielding via its positively charged amine group. True Falsearrow_forwardProvide a complete arrow push mechanism for each of the following reactions.arrow_forward
- Which of the attached amines can be used to resolve a racemic mixture of amino acids?arrow_forwardAcetylcholine esterase is an important enzyme in neural synaptic signal transmission. It breaks down the neurotransmitter acetylcholine after it binds the acetylcholine receptor. Its active site has the same features used by serine proteases. Here is the reaction catalyzed by Acetylcholine esterase: Acetylcholine Choline OH Acetate + H Acetylcholine is an ester, while peptide bonds cleaved by proteases are amides. How should acetylcholine estease's mechanism accommodate this? This cannot be determined from the information presented in class and in this question. For amides, the amide nitrogen is deprotonate to make it more like an ester. The same mechanism cleaves deprotonated amides and esters. No changes are needed. The mechanism same works for esters and amides. Prior to cleavage, a transamination converts the ester to an amide. The esterase will make a covalent intermediate to an amine to create the amide to be cleaved.arrow_forwardExplain why, when the guanidino group of arginine is protonated, the double-bonded nitrogen is the nitrogen that accepts the proton.arrow_forward
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