The Biosynthetic Control in Aromatic Amino Acid Producing Mutants of Corynebacterium glutamicum

Abstract

Regulatory properties of the enzymes involved in aromatic amino acid biosynthesis in the mutant of Corynebacterium glutamicum which produces a large amount of aromatic amino acids were examined. A phenylalanine auxotrophic L-tyrosine producer, pr-20, had a 3-deoxy-D-arabinoheptulosonate-7-phosphate (DAHP) synthetase released from the feedback inhibition by L-phenylalanine, L-tyrosine and L-tryptophan and had a two-fold derepressed chorismate mutase. A pair of L-phenylalanine and L-tyrosine still strongly inhibited the chorismate mutase activity, though the enzyme was partially released from the inhibition by L-phenylalanine alone. A tyrosine auxotrophic L-phenylalanine producer, PFP-19-31, had a DAHP synthetase sensitive to the feedback inhibition by L-phenylalanine, L-tyrosine and L-tryptophan and had a prephenate dehydratase and a chorismate mutase both partially released from the feedback inhibition by L-phenylalanine. The mutant produced a large amount of prephenate as well as L-phenylalanine. A phenylalanine and tyrosine double auxotrophic L-tryptophan producer, Px-115-97, had an anthranilate synthetase partially released from the feedback inhibition by L-tryptophan and had a DAHP synthetase sensitive to the feedback inhibition. These data explained the mechanism of the production of aromatic amino acids by these mutants and supported the in vivo functioning of the control mechanisms of aromatic amino acid biosynthesis in C. glutamicum previously elucidated in vitro experiments.