First genetic characterization of a bacterial β-phenylethylamine biosynthetic enzyme in Enterococcus faecium RM58
A Marcobal, B De Las Rivas…�- FEMS microbiology�…, 2006 - academic.oup.com
A Marcobal, B De Las Rivas, R Mu�oz
FEMS microbiology letters, 2006•academic.oup.comEnterococcus 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�…
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�…
Abstract
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.
Oxford University Press