The biosynthetic pathways for the manufacture of the natural product cyanobacterin, which is generated in modest quantities by the cyanobacteria Scytonema hofmanni, have been discovered.
They also found a new family of enzymes for forming carbon-carbon bonds in the process.
As a result, (bio)chemists have greatly expanded the biocatalytic repertory now known from nature, allowing for novel, long-term biotechnological medical applications, and agriculture.
Biosynthesis of Cyanobacteria
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The number of compounds, so-called natural products, that nature makes biosynthetically demonstrated that it is a good chemist.
These natural compounds are also vital to our survival as humans.
They're employed in a variety of ways in our daily lives, including as active ingredients in medicine and agriculture.
Antibiotics like penicillins obtained from molds, the anti-cancer medicine Taxol derived from the Pacific yew tree, and pyrethrins derived from chrysanthemums, which are used to treat pest infestations, are just a few examples.
The discovery and manufacture of medications based on such molecules require knowledge and comprehension of the biosynthetic assembly of such chemicals by nature.
Professor of Technical Biochemistry at TU Dresden, Tobias Gulder notes, "DiPaC allows us to transfer complete natural products biosynthetic pathways into recombinant host systems extremely fast and efficiently," as per ScienceDaily.
The researchers subsequently investigated the important individual stages of cyanobacterin biosynthesis by generating all key enzymes in the host organism E.coli, isolating them, and then evaluating their activity.
They discovered a previously undiscovered family of enzymes called furanolide synthases in the process.
These have the ability to catalyze the creation of carbon-carbon bonds in an unexpected way.
Further research on these furanolide synthases revealed that they are effective in vitro biocatalysts, making them ideal for biotechnological applications.
Prof. Tanja Gulder of Leipzig University's Institute of Organic Chemistry explained, "With the furanolide synthases, we have obtained an enzymatic tool that will allow us to develop more environmentally friendly methods for the production of bioactive compounds in the future, and thus make significant contributions to a more sustainable chemistry."
The two study teams now plan to look for these unique biocatalysts in other species, in order to discover more bioactive members of this natural product class, as well as create biotechnological approaches for cyanobacterin synthesis and structural diversification.
Biosynthesis, like cellular metabolism, is the production of natural compounds through enzyme processes, as per Nature.
To produce a single physiologically active molecule, many enzymes must perform successive enzymatic reactions.
By mixing substrates with enzymes utilizing recombinant techniques, biosynthesis may be used for chemical synthesis in vitro or in organisms like Escherichia coli.
During biosynthesis, a chemical reaction is necessary to allow the simple beginning component to be transformed or turned into another substance.
Precursors are the first components.
The chemical energy for the reaction is then provided by higher energy molecules, as per Study.com.
Catalytic enzymes, which are specialized proteins, "jump-start" the process and coenzymes aid in its completion.
Plants create new chemicals using solar energy (together with carbon dioxide and water). A substance called ATP provides chemical energy to the human body for processes (or adenosine triphosphate).
Related article: Marine Cyanobacteria Releasing 'Snack Packs' : Study Finds
