ArticleBiochimica et biophysica acta2009
Functional characterization of a Na(+)-coupled dicarboxylate transporter from Bacillus licheniformis.
Article in Biochimica et biophysica acta, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 16 citations in OpenAlex.
- Membrane-anchored substrate binding proteins are deployed in secondary TAXI transporters.Biological chemistry · 2023Article
- Development and characterization of efficient xylose utilization strains of Zymomonas mobilis.Biotechnology for biofuels · 2021Article
- Thermostability-based binding assays reveal complex interplay of cation, substrate and lipid binding in the bacterial DASS transporter, VcINDY.The Biochemical journal · 2021Article
- A Sodium-Translocating Module Linking Succinate Production to Formation of Membrane Potential in Prevotella bryantii.Applied and environmental microbiology · 2021Article
- Structure and Mechanism of the Divalent Anion/Na⁺ Symporter.International journal of molecular sciences · 2019Review
- Structure and function of the divalent anion/NaNature communications · 2017Article
- Importance of Glutamate Dehydrogenase (GDH) in Clostridium difficile Colonization In Vivo.PloS one · 2016Article
- Functional characterization of a Na+-dependent dicarboxylate transporter from Vibrio cholerae.The Journal of general physiology · 2014Article
- Sodium-coupled dicarboxylate and citrate transporters from the SLC13 family.Pflugers Archiv : European journal of physiology · 2014Review
- Functional characterization of SdcF from Bacillus licheniformis, a homolog of the SLC13 Na⁺/dicarboxylate transporters.The Journal of membrane biology · 2013Article
- Article
- Mechanism of citrate metabolism by an oxaloacetate decarboxylase-deficient mutant of Lactococcus lactis IL1403.Journal of bacteriology · 2011Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The Na(+)-coupled dicarboxylate transporter, SdcL, from Bacillus licheniformis is a member of the divalent anion/Na(+) symporter (DASS) family that includes the bacterial Na(+)/dicarboxylate cotransporter SdcS (from Staphyloccocus aureus) and the mammalian Na(+)/dicarboxylate cotransporters, NaDC1 and NaDC3. The transport properties of SdcL produced in Escherichia coli are similar to those of its prokaryotic and eukaryotic counterparts, involving the Na(+)-dependent transport of dicarboxylates such as succinate or malate across the cytoplasmic membrane with a K(m) of approximately 6 microM. SdcL may also transport aspartate, alpha-ketoglutarate and oxaloacetate with low affinity. The cotransport of Na(+) and dicarboxylate by SdcL has an apparent stoichiometry of 2:1, and a K(0.5) for Na(+) of 0.9 mM. Our findings represent the characterization of another prokaryotic protein of the DASS family with transport properties similar to its eukaryotic counterparts, but with a broader substrate specificity than other prokaryotic DASS family members. The broader range of substrates carried by SdcL may provide insight into domains of the protein that allow a more flexible or larger substrate binding pocket.
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