ArticleBioengineered2017
FabG can function as PhaB for poly-3-hydroxybutyrate biosynthesis in photosynthetic cyanobacteria Synechocystis sp. PCC 6803.
Article in Bioengineered, 2017. 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, 20 citations in OpenAlex.
- Draft genome sequence ofMicrobiology resource announcements · 2026Article
- Gut Microbiota-Derived 3-Hydroxybutyrate Blocks GPR43-Mediated IL6 Signaling to Ameliorate Radiation Proctopathy.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Genetic characterization of a novel Salinicola salarius isolate applied for the bioconversion of agro-industrial wastes into polyhydroxybutyrate.Microbial cell factories · 2024Article
- Adaptation Strategies to High Hydrostatic Pressures inMicroorganisms · 2023Article
- Crystal structure of acetoacetyl-CoA reductase from Rickettsia felis.Acta crystallographica. Section F, Structural biology communications · 2021Article
- Modifying the Cyanobacterial Metabolism as a Key to Efficient Biopolymer Production in Photosynthetic Microorganisms.International journal of molecular sciences · 2020Review
- Calmodulin Is the Fundamental Regulator of NADK-Mediated NAD Signaling in Plants.Frontiers in plant science · 2019Article
- Glucose Uncouples Nitrogen Sensing From Chlorosis via a Photosynthetic Checkpoint in Synechocystis sp. PCC 6803.Physiologia plantarumArticle
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The production of poly-3-hydroxybutyrate (PHB) by photosynthetic cyanobacteria is a potentially sustainable production method for the biodegradable plastics industry. β-Ketoacyl-ACP reductase (FabG), from the photosynthetic cyanobacterium Synechocystis sp. PCC 6803 (SpFabG), is the first NADPH-dependent reductase in the fatty acid biosynthesis pathway. Its structure is similar to that of acetoacetyl-CoA reductase (SpPhaB), which is critical for PHB synthesis and can replace SpPhaB for acetoacetyl-CoA reduction in vitro. However, the specific function of SpFabG in fatty acid synthesis and whether SpFabG could participate in PHB synthesis in vivo were not yet clear. In this study, the role of SpFabG in fatty acid synthesis was first verified in vivo by knocking down and overexpressing of fabG. It was shown that SpFabG was essential yet not rate-limiting for fatty acid biosynthesis. The biochemical characterization of SpFabG using acetoacetyl-CoA as the substrate showed that the optimum temperature, optimum pH, K
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