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Merck

Tyramine biosynthesis in Enterococcus durans is transcriptionally regulated by the extracellular pH and tyrosine concentration.

Microbial biotechnology (2009-11-01)
Daniel M Linares, María Fernández, M Cruz Martín, Miguel A Alvarez
RESUMEN

The microbial decarboxylation of some amino acids leads to the undesirable presence of biogenic amines in foods. One of the most abundant and frequent biogenic amines found in fermented foods is tyramine, which is produced by the decarboxylation of tyrosine. In the present work, transcriptional analysis of tyramine biosynthesis in Enterococcus durans IPLA655, a strain isolated from cheese, was studied. The gene coding for the tyrosine decarboxylase (tdcA) and that coding for the tyrosine-tyramine antiporter (tyrP) form an operon transcribed from the promoter P(tdcA), the expression of which is regulated by the extracellular pH and tyrosine concentration. Quantification of gene expression during the log phase of growth showed high concentrations of tyrosine and acidic pH conditions to induce tdcA-tyrP polycistronic messenger transcription.

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Sigma-Aldrich
L-Tyrosine Decarboxylase from Streptococcus faecalis, ≥0.1 unit/mg solid
Sigma-Aldrich
L-Tyrosine Decarboxylase Apoenzyme from Streptococcus faecalis, <0.005 unit/mg solid (without pyridoxal 5-phosphate), ≥0.05 unit/mg solid (with excess pyridoxal 5-phosphate)