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Biochemical characterization of a prokaryotic phenylalanine ammonia lyase
Longkuan Xiang1, Bradley S Moore
1College of Pharmacy, University of Arizona, Tucson, Arizona 85721-0207, USA.
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.
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