First genetic characterization of a bacterial beta-phenylethylamine biosynthetic enzyme in Enterococcus faecium RM58.
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.
Marcobal
Angela
A
Departamento de Microbiología, Instituto de Fermentaciones Industriales, CSIC, Madrid, Spain.
de las Rivas
Blanca
B
Muñoz
Rosario
R
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*
D010627:Phenethylamines; C029261:phenethylamine; D002262:Carboxy-Lyases; C019517:phenylalanine decarboxylase; D014439:Tyramine