Prostaglandin-endoperoxide synthase (PGHS) catalyzes the two-step conversion of arachidonic acid to prostaglandin H2 through the intermediate prostaglandin G2. The first biosynthetic step adds two oxygens to arachidonic acid to form prostaglandin G2, which is quickly reduced at the C15 hydroperoxide to an alcohol, producing prostaglandin H2. Prostaglandins are important molecules due to their role in the mediation of the inflammatory reactions. PGHS has been extensively studied in humans and mammals and has more recently been identified in coral, algae, and a variety of bacteria. A putative cyclooxygenase protein has been identified in the cyanobacterium Cyanothece. In this study, the gene encoding the Cyanothece protein was cloned into expression vectors with either an N-terminal (his)6 tag or N-terminal green fluorescent protein fusion partner and expressed in E. coli cells. Electrophoretic analysis indicates that the desired protein has been overexpressed, but the protein product is not soluble. We are currently generating Cyanothece protein with N-terminal fusion partners glutathione-S-transferase and maltose binding protein in an attempt to produce soluble protein. Once soluble protein is isolated, the function and activity of the protein will be assessed.

Expression and characterization of a putative cyclooxygenase from Cyanothece

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.