ArticleApplied and environmental microbiology2013
Biochemical and genetic characterization of the Enterococcus faecalis oxaloacetate decarboxylase complex.
Article in Applied and environmental microbiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 25 citations in OpenAlex.
- Spatial ecology ofMicrobiology spectrum · 2024Article
- Potential of Cheese-Associated Lactic Acid Bacteria to Metabolize Citrate and Produce Organic Acids and Acetoin.Metabolites · 2023Article
- Citrate metabolism in lactic acid bacteria: is there a beneficial effect forFrontiers in microbiology · 2023Review
- Identification of Potential Citrate Metabolism Pathways inMicroorganisms · 2021Article
- The PEP-pyruvate-oxaloacetate node: variation at the heart of metabolism.FEMS microbiology reviews · 2021Article
- Implications of the expression of Enterococcus faecalis citrate fermentation genes during infection.PloS one · 2018Article
- Expression and purification of toxic anti-breast cancer p28-NRC chimeric protein.Advanced biomedical research · 2016Article
- Functional Analysis of the Citrate Activator CitO from Enterococcus faecalis Implicates a Divalent Metal in Ligand Binding.Frontiers in microbiology · 2016Article
- Global Regulation of Gene Expression by the MafR Protein of Enterococcus faecalis.Frontiers in microbiology · 2015Article
- Genomic comparative analysis of the environmental Enterococcus mundtii against enterococcal representative species.BMC genomics · 2014Article
- Ca2+-citrate uptake and metabolism in Lactobacillus casei ATCC 334.Applied and environmental microbiology · 2013Article
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Authors and funding
5 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Enterococcus faecalis encodes a biotin-dependent oxaloacetate decarboxylase (OAD), which is constituted by four subunits: E. faecalis carboxyltransferase subunit OadA (termed Ef-A), membrane pump Ef-B, biotin acceptor protein Ef-D, and the novel subunit Ef-H. Our results show that in E. faecalis, subunits Ef-A, Ef-D, and Ef-H form a cytoplasmic soluble complex (termed Ef-AHD) which is also associated with the membrane. In order to characterize the role of the novel Ef-H subunit, coexpression of oad genes was performed in Escherichia coli, showing that this subunit is vital for Ef-A and Ef-D interaction. Diminished growth of the oadA and oadD single deletion mutants in citrate-supplemented medium indicated that the activity of the complex is essential for citrate utilization. Remarkably, the oadB-deficient strain was still capable of growing to wild-type levels but with a delay during the citrate-consuming phase, suggesting that the soluble Ef-AHD complex is functional in E. faecalis. These results suggest that the Ef-AHD complex is active in its soluble form, and that it is capable of interacting in a dynamic way with the membrane-bound Ef-B subunit to achieve its maximal alkalinization capacity during citrate fermentation.
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