ArticleJournal of bacteriology2013
Characterization of fructose 1,6-bisphosphatase and sedoheptulose 1,7-bisphosphatase from the facultative ribulose monophosphate cycle methylotroph Bacillus methanolicus.
Article in Journal of bacteriology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 52 citations in OpenAlex.
- Fructose-1,6-bisphosphatase is involved in heterotrophic growth and glycogen metabolism in cyanobacteria.Journal of experimental botany · 2025Article
- Ribose-5-phosphate metabolism protectsmBio · 2025Article
- Article
- A novel gluconeogenic route enables efficient use of erythritol in zoonoticFrontiers in veterinary science · 2024Article
- Metabolic engineering of thermophilic Bacillus methanolicus for riboflavin overproduction from methanol.Microbial biotechnology · 2023Article
- Article
- Analysis of the Plasmid-BasedApplied and environmental microbiology · 2022Article
- Unravelling Formaldehyde Metabolism in Bacteria: Road towards Synthetic Methylotrophy.Microorganisms · 2022Review
- Aerobic Utilization of Methanol for Microbial Growth and Production.Advances in biochemical engineering/biotechnology · 2022Article
- Transcriptome analysis reveals the roles of nitrogen metabolism and sedoheptulose bisphosphatase pathway in methanol-dependent growth of Corynebacterium glutamicum.Microbial biotechnology · 2021Article
- Interrogating the Role of the Two Distinct Fructose-Bisphosphate Aldolases ofFrontiers in microbiology · 2021Article
- Charting the Metabolic Landscape of the Facultative Methylotroph Bacillus methanolicus.mSystems · 2020Article
- Dual metabolomic profiling uncovers Toxoplasma manipulation of the host metabolome and the discovery of a novel parasite metabolic capability.PLoS pathogens · 2020Article
- Transaldolase in Bacillus methanolicus: biochemical characterization and biological role in ribulose monophosphate cycle.BMC microbiology · 2020Article
- Lateral Gene Transfer Shapes the Distribution of RuBisCO among Candidate Phyla Radiation Bacteria and DPANN Archaea.Molecular biology and evolution · 2019Article
- Pareto Optimality Explanation of the Glycolytic Alternatives in Nature.Scientific reports · 2019Article
- Synthetic Biology Applied to Carbon Conservative and Carbon Dioxide Recycling Pathways.Frontiers in bioengineering and biotechnology · 2019Review
- Improving formaldehyde consumption drives methanol assimilation in engineered E. coli.Nature communications · 2018Article
- Quantitative metabolomics of the thermophilic methylotroph Bacillus methanolicus.Microbial cell factories · 2016Article
- Genome-Based Genetic Tool Development forFrontiers in microbiology · 2016Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The genome of the facultative ribulose monophosphate (RuMP) cycle methylotroph Bacillus methanolicus encodes two bisphosphatases (GlpX), one on the chromosome (GlpX(C)) and one on plasmid pBM19 (GlpX(P)), which is required for methylotrophy. Both enzymes were purified from recombinant Escherichia coli and were shown to be active as fructose 1,6-bisphosphatases (FBPases). The FBPase-negative Corynebacterium glutamicum Δfbp mutant could be phenotypically complemented with glpX(C) and glpX(P) from B. methanolicus. GlpX(P) and GlpX(C) share similar functional properties, as they were found here to be active as homotetramers in vitro, activated by Mn(2+) ions and inhibited by Li(+), but differed in terms of the kinetic parameters. GlpX(C) showed a much higher catalytic efficiency and a lower Km for fructose 1,6-bisphosphate (86.3 s(-1) mM(-1) and 14 ± 0.5 μM, respectively) than GlpX(P) (8.8 s(-1) mM(-1) and 440 ± 7.6 μM, respectively), indicating that GlpX(C) is the major FBPase of B. methanolicus. Both enzymes were tested for activity as sedoheptulose 1,7-bisphosphatase (SBPase), since a SBPase variant of the ribulose monophosphate cycle has been proposed for B. methanolicus. The substrate for the SBPase reaction, sedoheptulose 1,7-bisphosphate, could be synthesized in vitro by using both fructose 1,6-bisphosphate aldolase proteins from B. methanolicus. Evidence for activity as an SBPase could be obtained for GlpX(P) but not for GlpX(C). Based on these in vitro data, GlpX(P) is a promiscuous SBPase/FBPase and might function in the RuMP cycle of B. methanolicus.
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