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Biochemical characterization of a prokaryotic phenylalanine ammonia lyase.


ABSTRACT: The committed biosynthetic reaction to benzoyl-coenzyme A in the marine bacterium "Streptomyces maritimus" is carried out by the novel prokaryotic phenylalanine ammonia lyase (PAL) EncP, which converts the primary amino acid L-phenylalanine to trans-cinnamic acid. Recombinant EncP is specific for L-phenylalanine and shares many biochemical features with eukaryotic PALs, which are substantially larger proteins by approximately 200 amino acid residues.

SUBMITTER: Xiang L 

PROVIDER: S-EPMC1151709 | biostudies-literature | 2005 Jun

REPOSITORIES: biostudies-literature

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Biochemical characterization of a prokaryotic phenylalanine ammonia lyase.

Xiang Longkuan L   Moore Bradley S BS  

Journal of bacteriology 20050601 12


The committed biosynthetic reaction to benzoyl-coenzyme A in the marine bacterium "Streptomyces maritimus" is carried out by the novel prokaryotic phenylalanine ammonia lyase (PAL) EncP, which converts the primary amino acid L-phenylalanine to trans-cinnamic acid. Recombinant EncP is specific for L-phenylalanine and shares many biochemical features with eukaryotic PALs, which are substantially larger proteins by approximately 200 amino acid residues. ...[more]

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