Cyanobacteria are known to be producers of terpene secondary metabolites. However, there has only been a limited number of characterized terpene synthases from cyanobacteria, relative to bacteria in general and specifically from group V filamentous cyanobacteria. Here, we have identified a terpene synthase gene (FmTPS1) from Fischerella muscicola PCC 9339, using conserved domain homology. The translated amino-acid (aa) sequence analysis indicated that the N-terminal domain of FmTPS1 contains a (D/N)DXX(D/E) metal-binding domain 82 aa downstream, meeting the bacterial and fungal defined form of the domain DDXXXE, specifically DDLCDE. FmTPS1 also contains an Asn/Ser/Glu triad (NxxxSxxxE) at 222 aa downstream. The presence of these two conserved domains confirms this is a class I terpene synthase. To further characterize FmTPS1, the gene was PCR amplified from purified PCC 9339 genomic DNA and cloned into pQE expression plasmid for heterologous expression in DE3 E. coli and subsequent protein purification. Reported, are substrate preference and product outcome from FmTPS1 incubated with diphosphate substrates including geranyl diphosphate, farnesyl diphosphate, and geranyl geranyl diphosphate.

Characterization of a terpene synthase from Fischerella muscicola PCC 9339

253rd National Meeting (2017)

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