Abstract
Prostaglandin F(2α) (PGF(2α)) is one of the most important bioactive lipids in mammals. Developing a bioproduction system for PGF(2α) could enable low-cost production with minimal environmental impact. Screening for efficient production of PGF(2α) from PGE(2) resulted in the isolation of Rhodotorula kratochvilovae NBRC 0389, a yeast that reduces PGE(2) to PGF(2α) using NADPH as a cofactor. Prostaglandin F(2α) 9-dehydrogenase (PDH) of the strain was identified, and a recombinant expression system was established in Escherichia coli for the protein. Further characterization of the recombinant PDH revealed that the enzyme catalyzes the reversible dehydrogenation of various prostaglandins. The PDH represents the first identified microbial PDH (also known as PGE(2) 9-reductase). PDH is a promising candidate for biotechnological applications in PGF(2α) production. Future research will be expected to enhance PGF(2α) yields through the implementation of PDH-based biosynthetic strategies. KEY POINTS: • Rhodotorula kratochvilovae reduced PGE(2) to PGF(2α) efficiently and stereoselectively. • Prostaglandin F(2α) 9-dehydrogenase was identified from R. kratochvilovae. • This is the first reported microbial prostaglandin F(2α) 9-dehydrogenase.