Identification and characterization of prostaglandin F_2α 9-dehydrogenase from Rhodotorula kratochvilovae

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 PGE₂ resulted in the isolation of Rhodotorula kratochvilovae NBRC 0389, a yeast that reduces PGE₂ 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 PGE₂ 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 PGE₂ 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.