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B6db references: 16630269

type Journal Article
authors Marcobal A, de las Rivas B, Muņoz R.
title First genetic characterization of a bacterial beta-phenylethylamine biosynthetic enzyme in Enterococcus faecium RM58
journal FEMS Microbiol Lett
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

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