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• W2031976951 startingPage "1309" @default.
• W2031976951 abstract "ABSTRACT The ability to produce diacetyl from pyruvate and l -serine was studied in various strains of Pediococcus pentosaceus and Pediococcus acidilactici isolated from cheese. After being incubated on both substrates, only P. pentosaceus produced significant amounts of diacetyl. This property correlated with measurable serine dehydratase activity in cell extracts. A gene encoding the serine dehydratase ( dsdA ) was identified in P. pentosaceus , and strains that showed no serine dehydratase activity carried mutations that rendered the gene product inactive. A functional dsdA was cloned from P. pentosaceus FAM19132 and expressed in Escherichia coli . The purified recombinant enzyme catalyzed the formation of pyruvate from l - and d -serine and was active at low pH and elevated NaCl concentrations, environmental conditions usually present in cheese. Analysis of the amino acid profiles of culture supernatants from dsdA wild-type and dsdA mutant strains of P. pentosaceus did not show differences in serine levels. In contrast, P. acidilactici degraded serine. Moreover, this species also catabolized threonine and produced alanine and α-aminobutyrate." @default.
• W2031976951 created "2016-06-24" @default.
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• W2031976951 date "2013-02-15" @default.
• W2031976951 modified "2023-10-16" @default.
• W2031976951 title "Catabolism of Serine by Pediococcus acidilactici and Pediococcus pentosaceus" @default.
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• W2031976951 doi "https://doi.org/10.1128/aem.03085-12" @default.
• W2031976951 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3568594" @default.
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