This work was made possible by combining modern tools from bioinformatics, synthetic biology, enzymology and (bio)chemical analytics. The focus was on how the central part of the cyanobacterin carbon skeleton is produced. The putative genes for this were first cloned by the method of "Direct Pathway Cloning" (DiPaC) and then activated in the model organism E. coli as a cell factory. DiPaC is a new synthetic biology method previously developed in the laboratory of Tobias Gulder, Professor of Technical Biochemistry at TU Dresden. "DiPaC allows us to transfer entire natural products biosynthetic pathways into recombinant host systems very quickly and efficiently," Tobias Gulder explains. In the next step, the research team analyzed the essential individual steps of cyanobacterin biosynthesis by additionally producing all key enzymes in the host organism E.coli, isolating them and then investigating the function of each enzyme. In the process, they came across a previously unknown class of enzymes called furanolide synthases. These are capable of catalyzing the formation of carbon-carbon bonds following an unusual mechanism. In further studies of these furanolide synthases, these enzymes proved to be efficient in vitro biocatalysts, making them highly attractive for biotechnological applications.

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EurekAlert, 22.05.27.
https://www.eurekalert.org/news-releases/954170