ArticleBMC microbiology2014
Characterization of 3-phosphoglycerate kinase from Corynebacterium glutamicum and its impact on amino acid production.
Article in BMC microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed, 25 citations in OpenAlex.
- Transcriptional analysis of genes associated with glycolysis in Streptomyces coelicolor M145.International microbiology : the official journal of the Spanish Society for Microbiology · 2025Article
- Transcriptome and Metabolome Analyses Reveal High-Altitude Adaptation in the Qinghai Toad-Headed LizardBiology · 2025Article
- A GTP-driven central carbon metabolism in the cellulolytic bacterium Ruminiclostridium cellulolyticum.Communications biology · 2025Article
- Characterization of the enzyme kinetics of EMP and HMP pathway inFrontiers in bioengineering and biotechnology · 2023Article
- Control of protein activity by photoinduced spin polarized charge reorganization.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Phosphoglycerate kinase: structural aspects and functions, with special emphasis on the enzyme from Kinetoplastea.Open biology · 2020Review
- A RecET-assisted CRISPR-Cas9 genome editing in Corynebacterium glutamicum.Microbial cell factories · 2018Article
- Metabolic engineering of an ATP-neutral Embden-Meyerhof-Parnas pathway in Corynebacterium glutamicum: growth restoration by an adaptive point mutation in NADH dehydrogenase.Applied and environmental microbiology · 2015Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundCorynebacterium glutamicum cg1790/pgk encodes an enzyme active as a 3-phosphoglycerate kinase (PGK) (EC 2.7.2.3) catalyzing phosphoryl transfer from 1,3-biphosphoglycerate (bPG) to ADP to yield 3-phosphoglycerate (3-PG) and ATP in substrate chain phosphorylation.
resultsC. glutamicum 3-phosphoglycerate kinase was purified to homogeneity from the soluble fraction of recombinant E. coli. PGK(His) was found to be active as a homodimer with molecular weight of 104 kDa. The enzyme preferred conditions of pH 7.0 to 7.4 and required Mg²⁺ for its activity. PGK(His) is thermo labile and it has shown maximal activity at 50-65°C. The maximal activity of PGK(His) was estimated to be 220 and 150 U mg-1 with KM values of 0.26 and 0.11 mM for 3-phosphoglycerate and ATP, respectively. A 3-phosphoglycerate kinase negative C. glutamicum strain ∆pgk was constructed and shown to lack the ability to grow under glycolytic or gluconeogenic conditions unless PGK was expressed from a plasmid to restore growth. When pgk was overexpressed in L-arginine and L-ornithine production strains the production increased by 8% and by 17.5%, respectively.
conclusionUnlike many bacterial PGKs, C. glutamicum PGK is active as a homodimer. PGK is essential for growth of C. glutamicum with carbon sources requiring glycolysis and gluconeogenesis. Competitive inhibition by ADP reveals the critical role of PGK in gluconeogenesis by energy charge. Pgk overexpression improved the productivity in L-arginine and L-ornithine production strains.
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