title: 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.
authors.affiliation: College of Pharmacy, University of Arizona, Tucson, Arizona 85721-0207, USA.
authors.forename: Longkuan
authors.initials: L
authors.lastname: Xiang
authors.forename: Bradley S
authors.initials: BS
authors.lastname: Moore
mesh_terms: D007189:Indans; D007700:Kinetics; D008956:Models, Chemical; D015394:Molecular Structure; D016297:Mutagenesis, Site-Directed; D063065:Organophosphonates / Q000494:pharmacology; D010650:Phenylalanine Ammonia-Lyase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D010802:Phylogeny; D013302:Streptomyces / Q000201:enzymology* / Q000235:genetics; D013379:Substrate Specificity
chemical_list: C411146:2-aminoindan-2-phosphonic acid; D007189:Indans; D063065:Organophosphonates; D010650:Phenylalanine Ammonia-Lyase