l. Some Studies in Enzyme Kinetics. II. The Oxidation of 3-Indoleacetic Acid by Plant Enzymes. III. The Synthesis of Some α-Alkyl α-Amino Acids and Their Derivatives

Author: Manning, David Treadway

Year: 1955

Degree: Dissertation (Ph.D.)

Advisor: Niemann, Carl G.

Committee Member: Unknown, Unknown

Option: Chemistry; Biology

DOI: 10.7907/PC3Z-A208

Abstract

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The kinetics of the alpha-chymotrypsin catalyzed hydrolysis of N-carboethoxy-L-tyrosinamide have been determined in aqueous solution at 25[degrees]C and at both pH 7.9 and pH 8.2. The enzyme-inhibitor dissociation constants of N-carboethoxy-D-tyrosinamide, N-carboethoxy-D-tyrosinmethylamide, and N-carboethoxy-L-tyrosinmethylemide have been evaluated in aqueous solution at 25[degrees]C, the former at pH 7.9 and the latter two at pH 7.6. The L isomers of each enantiomorphic pair appear to have a greater affinity for the enzyme than do their respective D-isomers.

An investigation into the nature of the enzymatic oxidation products of 3-Indoleacetic acid (IAA) has been made. 3-Indolealdehyde, o-formamidoacetophenone, o-aminoacetophenone, and 4-hydroxyquinoline have been eliminated as possible major products of the reaction.

A study of synthetic routes to the alpha-alkyl alpha-amino acids has been made. DL-alpha-Methlphenylalanine and DL-alpha-methyltyrosine have been synthesized. All attempts to resolve these compounds by enzymatic means have failed.

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