ArticleJournal of bacteriology2013
Salmonella utilizes D-glucosaminate via a mannose family phosphotransferase system permease and associated enzymes.
Article in Journal of bacteriology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 34 citations in OpenAlex.
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- OftenFrontiers in microbiology · 2025Article
- His-163 is a stereospecific proton donor in the mechanism of d-glucosaminate-6-phosphate ammonia-lyase.FEBS letters · 2022Article
- Transcriptional effects of melatonin on the gut commensal bacterium Klebsiella aerogenes.Genomics · 2022Article
- N-Acetylglucosamine Sensing and Metabolic Engineering for Attenuating Human and Plant Pathogens.Bioengineering (Basel, Switzerland) · 2022Review
- Genome-wide association study ofFrontiers in microbiology · 2022Article
- Streptozotocin-induced hyperglycemia alters the cecal metabolome and exacerbates antibiotic-induced dysbiosis.Cell reports · 2021Article
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- Comparative Genomic Analysis ofGenes · 2021Article
- Gene Duplications in the Genomes of Staphylococci and Enterococci.Frontiers in molecular biosciences · 2020Article
- Novel DNA Binding and Regulatory Activities for σJournal of bacteriology · 2017Article
- Contribution of the Salmonella enterica KdgR Regulon to Persistence of the Pathogen in Vegetable Soft Rots.Applied and environmental microbiology · 2016Article
- Modulating Salmonella Typhimurium's Response to a Changing Environment through Bacterial Enhancer-Binding Proteins and the RpoN Regulon.Frontiers in molecular biosciences · 2016Review
- A Mannose Family Phosphotransferase System Permease and Associated Enzymes Are Required for Utilization of Fructoselysine and Glucoselysine in Salmonella enterica Serovar Typhimurium.Journal of bacteriology · 2015Article
- Interaction with enzyme IIBMpo (EIIBMpo) and phosphorylation by phosphorylated EIIBMpo exert antagonistic effects on the transcriptional activator ManR of Listeria monocytogenes.Journal of bacteriology · 2015Article
- Salmonella-how a metabolic generalist adopts an intracellular lifestyle during infection.Frontiers in cellular and infection microbiology · 2014Review
- Use of a promiscuous, constitutively-active bacterial enhancer-binding protein to define the σ⁵⁴ (RpoN) regulon of Salmonella Typhimurium LT2.BMC genomics · 2013Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Salmonella enterica is a globally significant bacterial food-borne pathogen that utilizes a variety of carbon sources. We report here that Salmonella enterica subsp. enterica serovar Typhimurium (S. Typhimurium) uses d-glucosaminate (2-amino-2-deoxy-d-gluconic acid) as a carbon and nitrogen source via a previously uncharacterized mannose family phosphotransferase system (PTS) permease, and we designate the genes encoding the permease dgaABCD (d-glucosaminate PTS permease components EIIA, EIIB, EIIC, and EIID). Two other genes in the dga operon (dgaE and dgaF) were required for wild-type growth of S. Typhimurium with d-glucosaminate. Transcription of dgaABCDEF was dependent on RpoN (σ(54)) and an RpoN-dependent activator gene we designate dgaR. Introduction of a plasmid bearing dgaABCDEF under the control of the lac promoter into Escherichia coli strains DH5α, BL21, and JM101 allowed these strains to grow on minimal medium containing d-glucosaminate as the sole carbon and nitrogen source. Biochemical and genetic data support a catabolic pathway in which d-glucosaminate, as it is transported across the cell membrane, is phosphorylated at the C-6 position by DgaABCD. DgaE converts the resulting d-glucosaminate-6-phosphate to 2-keto-3-deoxygluconate 6-phosphate (KDGP), which is subsequently cleaved by the aldolase DgaF to form glyceraldehyde-3-phosphate and pyruvate. DgaF catalyzes the same reaction as that catalyzed by Eda, a KDGP aldolase in the Entner-Doudoroff pathway, and the two enzymes can substitute for each other in their respective pathways. Examination of the Integrated Microbial Genomes database revealed that orthologs of the dga genes are largely restricted to certain enteric bacteria and a few species in the phylum Firmicutes.
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