Dehalogenation and Deamination of L-2-Amino-4-chloro-4-pentenoic Acid by Proteus mirabilis

Abstract

Eighty-one strains of bacteria were tested for their ability to catalyze the release of chloride ion from DL-2-amino-4-chloro-4-pentenoic acid. A dehalogenating enzyme was obtained from the cells of Proteus mirabilis IFO 3849, which can use the L-isomer. The enzyme was constitutively produced. The conversion of L-2-amino-4-chloro-4-pentenoic acid to 2-keto-4-pentenoic acid, ammonia, and chloride ion was demonstrated. The reaction product, 2-keto-4-pentenoic acid, was isolated as its 2, 4-dinitrophenylhydrazone and identified by catalytic hydrogenolysis of the hydrazone to the corresponding amino acid, norvaline.