Human prostaglandin F synthase (PGFS) is a ~37 kDa monomeric protein with high sequence similarity to aldo-keto reductase family members. It exhibits two related primary activities, catalyzing the isomerization of PGH2 to PGF2α (PGH2 9,11-endoperoxide reductase activity), as well as the formation of 11β-PGF2α from PGD2 (PGD2 11-ketoreductase activity) in the presence of NADPH. The enzyme also exhibits reductase activities toward carbonyl compounds such at nitroacetophenone, nitrobenzaldehyde, and 9,10-phenanthrene quinine (PQ). Cayman’s human recombinant PGFS has been expressed and purified from an E.coli overexpression system. Enzyme activity was determined by monitoring the change in absorbance at 340 nm using PGD2 as the substrate and NADPH as the cofactor (PGD2 11-ketoreductase activity).
