Biochemical characterization of a prokaryotic phenylalanine ammonia lyase

Citation:
Xiang, LK, Moore BS.  2005.  Biochemical characterization of a prokaryotic phenylalanine ammonia lyase. Journal of Bacteriology. 187:4286-4289.

Date Published:

Jun

Keywords:

2-aminoindan-2-phosphonic acid, 4-methylideneimidazole-5-one-containing tyrosine aminomutase, a biosynthesis, antibiotic c-1027 biosynthesis, bacterium, enterocin, gene-cluster, kinetic-analysis, methylidene-imidazolone, polyketide, streptomyces-maritimus, synthase

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 200 amino acid residues.

Notes:

n/a

Website

DOI:

10.1128/jb.187.12.4286-4289.2005