ArticleScientific reports2017
Cyanobacterial Sfp-type phosphopantetheinyl transferases functionalize carrier proteins of diverse biosynthetic pathways.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Heterologous expression of NRPS and PKS pathways in Escherichia coli: from bottlenecks to biosynthetic platforms.Essays in biochemistry · 2026Review
- Mangrove cyanobacterial diversity as a source of bioactive natural products.Current research in microbial sciences · 2026Article
- Multichassis Expression of Cyanobacterial and Other Bacterial Biosynthetic Gene Clusters.ACS synthetic biology · 2025Article
- Escherichia coli Nissle 1917 secondary metabolism: aryl polyene biosynthesis and phosphopantetheinyl transferase crosstalk.Applied microbiology and biotechnology · 2021Article
- Heterologous production of cyanobacterial compounds.Journal of industrial microbiology & biotechnology · 2021Review
- Mining of Cyanobacterial Genomes Indicates Natural Product Biosynthetic Gene Clusters Located in Conjugative Plasmids.Frontiers in microbiology · 2021Article
- Heterologous Expression of Cryptomaldamide in a Cyanobacterial Host.ACS synthetic biology · 2020Article
- Recent advances in synthetic biology of cyanobacteria for improved chemicals production.Bioengineered · 2020Review
- Genetic platforms for heterologous expression of microbial natural products.Natural product reports · 2019Review
- Leveraging synthetic biology for producing bioactive polyketides and non-ribosomal peptides in bacterial heterologous hosts.MedChemComm · 2019Review
- Development of a cyanobacterial heterologous polyketide production platform.Metabolic engineering · 2018Article
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Authors and funding
7 authors.
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Abstract
Cyanobacteria produce structurally and functionally diverse polyketides, nonribosomal peptides and their hybrids. Sfp-type phosphopantetheinyl transferases (PPTases) are essential to the production of these compounds via functionalizing carrier proteins (CPs) of biosynthetic megaenzymes. However, cyanobacterial Sfp-type PPTases remain poorly characterized, posing a significant barrier to the exploitation of cyanobacteria for biotechnological and biomedical applications. Herein, we describe the detailed characterization of multiple cyanobacterial Sfp-type PPTases that were rationally selected. Biochemical characterization of these enzymes along with the prototypic enzyme Sfp from Bacillus subtilis demonstrated their varying specificities toward 11 recombinant CPs of different types of biosynthetic pathways from cyanobacterial and Streptomyces strains. Kinetic analysis further indicated that PPTases possess the higher binding affinity and catalytic efficiency toward their cognate CPs in comparison with noncognate substrates. Moreover, when chromosomally replacing the native PPTase gene of Synechocystis sp. PCC6803, two selected cyanobacterial PPTases and Sfp supported the growth of resulted mutants. Cell lysates of the cyanobacterial mutants further functionalized recombinant CP substrates. Collectively, these studies reveal the versatile catalysis of selected cyanobacterial PPTases and provide new tools to synthesize cyanobacterial natural products using in vitro and in vivo synthetic biology approaches.
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