ArticleMicrobial biotechnology2016
Tyrosine decarboxylase activity of Enterococcus mundtii: new insights into phenotypic and genetic aspects.
Article in Microbial biotechnology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 12 citations in OpenAlex.
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- Time-Resolved Evaluation of L-Dopa Metabolism in Bacteria-Host Symbiotic System and the Effect on Parkinson's Molecular Pathology.Small methods · 2025Article
- Diversity of Neurotransmitter-Producing Human Skin Commensals.International journal of molecular sciences · 2024Article
- Microbial Spoilage of Traditional Goose Sausages Produced in a Northern Region of Italy.Microorganisms · 2023Article
- Survival, growth, and biogenic amine production ofFrontiers in nutrition · 2022Article
- Biogenic Amine Production by Lactic Acid Bacteria: A Review.Foods (Basel, Switzerland) · 2019Review
- Lactobacillus rossiae strain isolated from sourdough produces putrescine from arginine.Scientific reports · 2018Article
- Tyrosine decarboxylase activity of Enterococcus mundtii: new insights into phenotypic and genetic aspects.Microbial biotechnology · 2016Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Few information is available about the tyraminogenic potential of the species Enterococcus mundtii. In this study, two plant-derived strains of E. mundtii were selected and investigated to better understand the phenotypic behaviour and the genetic mechanisms involved in tyramine accumulation. Both the strains accumulated tyramine from the beginning of exponential phase of growth, independently on the addition of tyrosine to the medium. The strains accumulated also 2-phenylethylamine, although with lower efficiency and in greater extent when tyrosine was not added. Accordingly, the tyrosine decarboxylase (tyrDC) gene expression level increased during the exponential phase with tyrosine added, while it remained constant and high without precursor. The genetic organization as well as sequence identity levels of tyrDC and tyrosine permease (tyrP) genes indicated a correlation with those of phylogenetically closer enterococcal species, such as E. faecium, E. hirae and E. durans; however, the gene Na+/H+ antiporter (nhaC) that usually follow tyrP is missing. In addition, BLAST analysis revealed the presence of additional genes encoding for decarboxylase and permease in the genome of several E. mundtii strains. It is speculated the occurrence of a duplication event and the acquisition of different specificity for these enzymes that deserves further investigations.
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