Remnants of an ancient pathway to L-phenylalanine and L-tyrosine in enteric bacteria: evolutionary implications and biotechnological impact.

AUTOR(ES)

Bonner, C A

RESUMO

The pathway construction for biosynthesis of aromatic amino acids in Escherichia coli is atypical of the phylogenetic subdivision of gram-negative bacteria to which it belongs (R. A. Jensen, Mol. Biol. Evol. 2:92-108, 1985). Related organisms possess second pathways to phenylalanine and tyrosine which depend upon the expression of a monofunctional chorismate mutase (CM-F) and cyclohexadienyl dehydratase (CDT). Some enteric bacteria, unlike E. coli, possess either CM-F or CDT. These essentially cryptic remnants of an ancestral pathway can be a latent source of biochemical potential under certain conditions. As one example of advantageous biochemical potential, the presence of CM-F in Salmonella typhimurium increases the capacity for prephenate accumulation in a tyrA auxotroph. We report the finding that a significant fraction of the latter prephenate is transaminated to L-arogenate. The tyrA19 mutant is now the organism of choice for isolation of L-arogenate, uncomplicated by the presence of other cyclohexadienyl products coaccumulated by a Neurospora crassa mutant that had previously served as the prime biological source of L-arogenate. Prephenate aminotransferase activity was not conferred by a discrete enzyme, but rather was found to be synonymous with the combined activities of aspartate aminotransferase (aspC), aromatic aminotransferase (tyrB), and branched-chain aminotransferase (ilvE). This conclusion was confirmed by results obtained with combinations of aspC-, tyrB-, and ilvE-deficient mutations in E. coli. An example of disadvantageous biochemical potential is the presence of a cryptic CDT in Klebsiella pneumoniae, where a mutant carrying multiple enzyme blocks is the standard organism used for accumulation and isolation of chorismate.(ABSTRACT TRUNCATED AT 250 WORDS)

Documentos Relacionados

• L-Phenylalanine and L-tyrosine catabolism by selected Streptomyces species.
• l-Phenylalanine Ammonia-Lyase (Maize): Evidence for a Common Catalytic Site for l-Phenylalanine and l-Tyrosine 1
• l-Phenylalanine Ammonia-lyase (Maize): Partial Purification and Response to Gibberellic Acid and Cycloheximide of l-Phenylalanine and l-Tyrosine Ammonia-lyase Activities 1
• Hidden overflow pathway to L-phenylalanine in Pseudomonas aeruginosa.
• Regulation of L-phenylalanine ammonia-lyase by L-phenylalanine and nitrogen in Neurospora crassa.