Essential Organic Chemistry (3rd Edition)
3rd Edition
ISBN: 9780321937711
Author: Paula Yurkanis Bruice
Publisher: PEARSON
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Textbook Question
Chapter 18.11, Problem 26P
Explain why the ability of PLP to catalyze an amino acid transformation is greatly reduced if the OH substituent of PLP is replaced by OCH3.
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Chapter 18 Solutions
Essential Organic Chemistry (3rd Edition)
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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- Leuprolide is a synthetic nonapeptide used to treat both endometriosis in women and prostate cancer in men. (a) Both C-terminal and N-terminal amino acids in leuprolide have been structurally modified. Identify the modifications. (b) One of the nine amino acids in leuprolide has d stereochemistry rather than the usual L. Which one? (c) Write the structure of leuprolide using both one- and three-letter abbreviations. (d) What charge would you expect leuprolide to have at neutral pH?arrow_forwardThe configuration of the chiral center in a-amino acids is most commonly specified using the d,l convention. It can also be identified using the R,S convention . Does the chiral center in l-serine have the R or S configuration?arrow_forwardGive the following1. an amino acid that has an aryl side group chain 2. an amino acid that contains a side chain with a thioether bond3. an amino acid that reacts with HCL through acid-base reaction4. an amino acid that contains a sulfhydryl side chain5. an amino acid with a side chain that can form hydrogen bonds with water6. an amino acid that contains an amide side chainarrow_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_forwardShow how valine can be prepared by a reductive amination.arrow_forwardAlthough tryptophan contains a heterocyclic amine, it is considered a neutral aminoacid. Explain why the indole nitrogen of tryptophan is more weakly basic than one ofthe imidazole nitrogens of histidine.arrow_forward
- Write out the steps needed to synthesize the following peptide using the Merrifield method.arrow_forwardHow do you account for the fact that the -NH3+ group of the conjugate acid of alanine is a stronger acid than the -NH3+ group of the conjugate acid of isopropylamine?arrow_forwardDraw the structure of the tetrapeptide Asp-Arg-Val-Tyr. Please show the appropriate stereochemistry of the natural amino acids in the resulting peptide. Please draw all ionizable groups in their neutral form.arrow_forward
- α-Amino acids can be prepared by treating an aldehyde with ammonia/trace acid, followed by hydrogen cyanide, followed by acid-catalyzed hydrolysis. What aldehyde is needed to prepare isoleucine?arrow_forwardAnother method to form a peptide bond involves a two-step process Conversion of a Boc-protected amino acid to a p-nitrophenyl ester. Why does a p-nitrophenyl ester “activate” the carboxy group of thefirst amino acid to amide formation?arrow_forwardEsterase is an enzyme that catalyzes the hydrolysis of esters. It hydrolyzes esters of L-amino acids more rapidly than esters of d-amino acids. How can this enzyme be used to separate a racemic mixture of amino acids?arrow_forward
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