ArticleBioscience reports2013
Inactivation of the phosphoglucomutase gene pgm in Corynebacterium glutamicum affects cell shape and glycogen metabolism.
Article in Bioscience reports, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 18 citations in OpenAlex.
- De novo biosynthesis of β-arbutin in Corynebacterium glutamicum via pathway engineering and process optimization.Biotechnology for biofuels and bioproducts · 2024Article
- Biosynthesis of Apigenin Glucosides in EngineeredJournal of microbiology and biotechnology · 2024Article
- Recent progress in the structure of glycogen serving as a durable energy reserve in bacteria.World journal of microbiology & biotechnology · 2020Review
- Identifying the Growth Modulon ofFrontiers in microbiology · 2019Article
- Metabolic engineering of Corynebacterium glutamicum for anthocyanin production.Microbial cell factories · 2018Article
- Production of the compatible solute α-D-glucosylglycerol by metabolically engineered Corynebacterium glutamicum.Microbial cell factories · 2018Article
- The α-glucan phosphorylase MalP of Corynebacterium glutamicum is subject to transcriptional regulation and competitive inhibition by ADP-glucose.Journal of bacteriology · 2015Article
- Allosteric regulation of the partitioning of glucose-1-phosphate between glycogen and trehalose biosynthesis in Mycobacterium tuberculosis.Biochimica et biophysica acta · 2015Article
- Intracellular glycogen accumulation by human gut commensals as a niche adaptation trait.Gut microbesReview
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In Corynebacterium glutamicum formation of glc-1-P (α-glucose-1-phosphate) from glc-6-P (glucose-6-phosphate) by α-Pgm (phosphoglucomutase) is supposed to be crucial for synthesis of glycogen and the cell wall precursors trehalose and rhamnose. Furthermore, Pgm is probably necessary for glycogen degradation and maltose utilization as glucan phosphorylases of both pathways form glc-1-P. We here show that C. glutamicum possesses at least two Pgm isoenzymes, the cg2800 (pgm) encoded enzyme contributing most to total Pgm activity. By inactivation of pgm we created C. glutamicum IMpgm showing only about 12% Pgm activity when compared to the parental strain. We characterized both strains during cultivation with either glucose or maltose as substrate and observed that (i) the glc-1-P content in the WT (wild-type) and the mutant remained constant independent of the carbon source used, (ii) the glycogen levels in the pgm mutant were lower during growth on glucose and higher during growth on maltose, and (iii) the morphology of the mutant was altered with maltose as a substrate. We conclude that C. glutamicum employs glycogen as carbon capacitor to perform glc-1-P homeostasis in the exponential growth phase and is therefore able to counteract limited Pgm activity for both anabolic and catabolic metabolic pathways.
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