type	Journal Article
authors	Marcobal A, de las Rivas B, Muñoz R.
title	First genetic characterization of a bacterial beta-phenylethylamine biosynthetic enzyme in Enterococcus faecium RM58
journal	FEMS Microbiol Lett
Activity	4.1.1.25
Family	4.1.1.25.a
sel	selected
ui	16630269
year	(2006)
volume	258
number	1
pages	144-9
keywords	Amino Acid Sequence
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.
last changed	2008/01/25 19:48