I. Some studies in enzyme kinetics. II. The oxidation of 3-indoleacetic acid by plant enzymes. III. The synthesis of some alpha-alkyl alpha-amino acids and their derivatives

NOTE: Text or symbols not renderable in plain ASCII are indicated by [...]. Abstract is included in .pdf document. 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