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Chapter 24: Q14P (page 1272)

Question: Propose a mechanism for the acid-catalyzed hydrolysis of phenylalanine ethyl ester.

Short Answer

Expert verified

Esters of amino acids can be used as protected derivatives in order to prevent the carboxyl group from reacting in an unusual manner. The most common protecting groups are methyl, ethyl and benzyl estersA

Step by step solution

01

Step-by-Step solutionStep 1: Esterification of carboxyl group

Esters of amino acids can be used as protected derivatives in order to prevent the carboxyl group from reacting in an unusual manner. The most common protecting groups are methyl, ethyl and benzyl estersA

02

Mechanism

Ester is hydrolyzed by the aqueous acid which regenerates the free amino acid.

Mechanism for acid-catalyzed hydrolysis of phenylalanine ethyl ester to phenylalanine

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Most popular questions from this chapter

Histidine is an important catalytic residue found at the active sites of many enzymes. In many cases, histidine appears to remove protons or to transfer protons from one location to another.

(a) Show which nitrogen atom of the histidine heterocycle is basic and which is not.

(b) Use resonance forms to show why the protonated form of histidine is a particularly stable cation.

(c) Show the structure that results when histidine accepts a proton on the basic nitrogen of the heterocycle and then is deprotonated on the other heterocyclic nitrogen. Explain how histidine might function as a pipeline to transfer protons between sites within an enzyme and its substrate.

Draw the structure of the predominant form of

(a)Isoleucine at pH 11 (b) Proline at pH 2

(c)Arginine at pH 7 (d) Glutamic acid at pH 7

A mixture of alanine, lysine, and aspartic acid at 1). pH 6 ; 2). pH 11; 3). pH 2

Daw the structure of the predominant form of

Isoleucine at pH 11 (b) Proline at pH 2

Arginine at pH 7 (d) Glutamic acid at pH 7

A mixture of alanine, lysine, and aspartic acid at 1). pH 6 ; 2). pH 11; 3). pH

Complete hydrolysis of an unknown basic decapeptide gives Gly, Ala, Leu, Ile, Phe, Tyr, Glu, Arg, Lys, and Ser. Terminal residue analysis shows that the N terminus is Ala, and the C terminus is Ile. Incubation of the decapeptide with chymotrypsin gives two tripeptides, A and B, and a tetrapeptide, C. Amino acid analysis shows that peptide A contains Gly, Glu, Tyr, and; peptide B contains Ala, Phe, and Lys; and peptide C contains Leu, Ile, Ser, and Arg.Terminal residue analysis gives the following results.

Incubation of the decapeptide with trypsin gives a dipeptide D, a pentapeptide E, and a tripeptide F. Terminal residue analysis of F shows that the N terminus is Ser and the C terminus is Ile. Propose a structure for the decapeptide and for fragments A through F.

Draw the electrophoretic separation of Ala, Lys, and Asp at pH 9.7.

See all solutions

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