ArticleApplied and environmental microbiology2009
Exopolyphosphatases PPX1 and PPX2 from Corynebacterium glutamicum.
Article in Applied and environmental microbiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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18 citing papers in PubMed, 36 citations in OpenAlex.
- Polyphosphate as a novel regulator of super-enhancer complexes: disruption of phase separation and gene expression.Nucleic acids research · 2026Article
- An Update on Polyphosphate In Vivo Activities.Biomolecules · 2024Review
- Ppx1 putative exopolyphosphatase is essential for polyphosphate accumulation inApplied and environmental microbiology · 2024Article
- Inorganic Polyphosphates As Storage for and Generator of Metabolic Energy in the Extracellular Matrix.Chemical reviews · 2019Review
- Inorganic polyphosphate accumulation suppresses the dormancy response and virulence inThe Journal of biological chemistry · 2019Article
- Marine ArchaeonFrontiers in microbiology · 2019Article
- Mutations in Escherichia coli Polyphosphate Kinase That Lead to Dramatically IncreasedJournal of bacteriology · 2018Article
- Combined genomic and structural analyses of a cultured magnetotactic bacterium reveals its niche adaptation to a dynamic environment.BMC genomics · 2016Article
- Regulation of the pstSCAB operon in Corynebacterium glutamicum by the regulator of acetate metabolism RamB.BMC microbiology · 2015Article
- Article
- Functional characterization of exopolyphosphatase/guanosine pentaphosphate phosphohydrolase (PPX/GPPA) of Campylobacter jejuni.Virulence · 2014Article
- Accumulation of polyphosphate in Lactobacillus spp. and its involvement in stress resistance.Applied and environmental microbiology · 2014Article
- Deciphering the genome of polyphosphate accumulating actinobacterium Microlunatus phosphovorus.DNA research : an international journal for rapid publication of reports on genes and genomes · 2012Article
- Two-component signal transduction in Corynebacterium glutamicum and other corynebacteria: on the way towards stimuli and targets.Applied microbiology and biotechnology · 2012Review
- The two PPX-GppA homologues from Mycobacterium tuberculosis have distinct biochemical activities.PloS one · 2012Article
- Polyphosphate deficiency affects the sliding motility and biofilm formation of Mycobacterium smegmatis.Current microbiology · 2011Article
- The role of the novel exopolyphosphatase MT0516 in Mycobacterium tuberculosis drug tolerance and persistence.PloS one · 2011Article
- Link between phosphate starvation and glycogen metabolism in Corynebacterium glutamicum, revealed by metabolomics.Applied and environmental microbiology · 2010Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Corynebacterium glutamicum accumulates up to 300 mM of inorganic polyphosphate (PolyP) in the cytosol or in granules. The gene products of cg0488 (ppx1) and cg1115 (ppx2) were shown to be active as exopolyphosphatases (PPX), as overexpression of either gene resulted in higher exopolyphosphatase activities in crude extracts and deletion of either gene with lower activities than those of the wild-type strain. PPX1 and PPX2 from C. glutamicum share only 25% identical amino acids and belong to different protein groups, which are distinct from enterobacterial, archaeal, and yeast exopolyphosphatases. In comparison to that in the wild type, more intracellular PolyP accumulated in the Deltappx1 and Deltappx2 deletion mutations but less when either ppx1 or ppx2 was overexpressed. When C. glutamicum was shifted from phosphate-rich to phosphate-limiting conditions, a growth advantage of the deletion mutants and a growth disadvantage of the overexpression strains compared to the wild type were observed. Growth experiments, exopolyphosphatase activities, and intracellular PolyP concentrations revealed PPX2 as being a major exopolyphosphatase from C. glutamicum. PPX2(His) was purified to homogeneity and shown to be active as a monomer. The enzyme required Mg2+ or Mn2+ cations but was inhibited by millimolar concentrations of Mg2+, Mn2+, and Ca2+. PPX2 from C. glutamicum was active with short-chain polyphosphates, even accepting pyrophosphate, and was inhibited by nucleoside triphosphates.
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