|
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 |
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 |
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