Open AccessFirst genetic characterization of a bacterial β‐phenylethylamine biosynthetic enzyme in Enterococcus faecium RM58
Author(s) -
Marcobal Angela,
De Las Rivas Blanca,
Muñoz Rosario
Publication year - 2006
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2006.00206.x
Subject(s) - enterococcus faecium , enterococcus faecalis , tyramine , tyrosine , biochemistry , biology , escherichia coli , enterococcus , amino acid , microbiology and biotechnology , enzyme , phenylalanine , gene , antibiotics
Enterococcus faecium RM58 produces β‐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.