ArticleJournal of experimental botany2025
Fructose-1,6-bisphosphatase is involved in heterotrophic growth and glycogen metabolism in cyanobacteria.
Article in Journal of experimental botany, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed.
- Horizontal Gene Transfers Underpin Ribose Heterotrophy and Central Carbon Metabolism Remodeling in Gloeobacteraceae.Genome biology and evolution · 2026Article
- The impact of CP12 on the metabolome of cyanobacteria under fluctuating COFrontiers in plant science · 2025Article
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Authors and funding
11 authors.
Funding
Abstract
Cyanobacteria switch between photoautotrophic and heterotrophic carbon metabolism during diurnal cycles. A classical control point is characterized by two glycolytic phosphofructokinases (PFKs) and a bifunctional fructose-1,6-biphosphatase/sedoheptulose-1,7-biphosphatase (F/SBPase; slr2094), which catalyses two reactions in the Calvin-Benson-Bassham (CBB) cycle. In addition, Synechocystis possesses a fructose-1,6-bisphosphatase (FBPase; slr0952) with yet unknown physiological function and biochemical properties. Our aim was to elucidate the physiological role of FBPase, in combination with the above-mentioned enzymes. We discovered that FBPase is specific for fructose 1,6-bisphosphate (FBP), showing no SBPase activity, and unlike F/SBPase does not exhibit any biochemical regulatory properties. In contrast to F/SBPase, FBPase is not involved in the CBB cycle, but instead affects growth and glycogen metabolism under heterotrophic conditions. We hypothesize that FBPase may influence glycogen turnover by controlling cellular levels of its substrate, FBP, since FBP is involved in the formation of glucose 1,6-bisphosphate, which is a regulatory metabolite for the control point between glycogen and central carbon metabolism at the level of phosphoglucomutases. Our data indicate that PFK and FBPase act as an antagonistic enzyme couple in darkness. Furthermore, we found redox-insensitive FBPases from plant chloroplasts to be closely related to Synechocystis FBPase, indicating that they might serve a similar function.
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