|
type |
Journal Article |
authors |
Lucas, P.; Lonvaud-Funel, A. |
title |
Purification and partial gene sequence of the tyrosine decarboxylase of Lactobacillus brevis IOEB 9809 |
journal |
FEMS Microbiol Lett |
Activity |
4.1.1.25 |
Family |
4.1.1.25.a |
sel |
selected |
ui |
12052555 |
year |
(2002) |
volume |
211 |
number |
1 |
pages |
85-9 |
| |
abstract |
Some lactic acid bacteria contain a tyrosine decarboxylase (TDC) which converts tyrosine to tyramine, a biogenic amine frequently encountered in fermented food and wine. Purification and microsequencing of the TDC of Lactobacillus brevis IOEB 9809 allowed us to determine a partial sequence of the TDC gene encoding 264 amino acids of the enzyme. Analysis of this protein sequence revealed typical features of pyridoxal phosphate-dependent amino acid decarboxylases while not any known decarboxylase was closely related to the TDC of L. brevis IOEB 9809. In addition, we could detect other L. brevis strains carrying a TDC gene in a rapid assay based on the polymerase chain reaction. |
last changed |
2009/06/12 11:27 |
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