title: First genetic characterization of a bacterial beta-phenylethylamine biosynthetic enzyme in Enterococcus faecium RM58.
abstract: Enterococcus faecium RM58 produces beta-phenylethylamine and tyramine. A gene from Ent. faecium RM58 coding for a 625 amino-acid residues protein that shows 85% identity to Enterococcus faecalis tyrosine decarboxylase has been expressed in Escherichia coli, resulting in L-phenylalanine and L-tyrosine decarboxylase activities. Both activities were lost when a truncated protein lacking 84 amino acids at its C-terminus was expressed in E. coli. This study constitutes the first genetic characterization of a bacterial protein having L-phenylalanine decarboxylase activity and solves a long-standing question regarding the specificity of tyrosine decarboxylases in enterococci.
authors.affiliation: Departamento de Microbiología, Instituto de Fermentaciones Industriales, CSIC, Madrid, Spain.
authors.forename: Angela
authors.initials: A
authors.lastname: Marcobal
authors.forename: Blanca
authors.initials: B
authors.lastname: de las Rivas
authors.forename: Rosario
authors.initials: R
authors.lastname: Muñoz
mesh_terms: D002262:Carboxy-Lyases / Q000235:genetics*; D016984:Enterococcus faecium / Q000201:enzymology* / Q000235:genetics; D004926:Escherichia coli / Q000235:genetics; D010627:Phenethylamines / Q000378:metabolism*; D014439:Tyramine / Q000096:biosynthesis*
chemical_list: D010627:Phenethylamines; C029261:phenethylamine; D002262:Carboxy-Lyases; C019517:phenylalanine decarboxylase; D014439:Tyramine