Prostaglandin F2α (PGF2α) is one of the most important bioactive lipids in mammals. Developing a bioproduction system for PGF2α could enable low-cost production with minimal environmental impact. Screening for efficient production of PGF2α from PGE2 resulted in the isolation of Rhodotorula kratochvilovae NBRC 0389, a yeast that reduces PGE2 to PGF2α using NADPH as a cofactor. Prostaglandin F2α 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 PGE2 9-reductase). PDH is a promising candidate for biotechnological applications in PGF2α production. Future research will be expected to enhance PGF2α yields through the implementation of PDH-based biosynthetic strategies. KEY POINTS: • Rhodotorula kratochvilovae reduced PGE2 to PGF2α efficiently and stereoselectively. • Prostaglandin F2α 9-dehydrogenase was identified from R. kratochvilovae. • This is the first reported microbial prostaglandin F2α 9-dehydrogenase.
Shino et al. (Mon,) studied this question.