Prostaglandin‐E2 9‐ketoreductase from human uterine decidua vera

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Abstract
Prostaglandin‐E2 9‐ketoreductase, the enzyme which catalyzes the reaction from prostaglandin F2α(PGF2α to prostaglandin F2α (PGF2α), has been purified 232‐fold from human uterine decidua vera.The molecular mass of the enzyme, as estimated by fast protein liquid chromatography, was 29 kDa. Sodium dodecyl sulfate disc gel electrophoresis of the denatured enzyme revealed a molecular mass of 31 kDa. These data suggest that the enzyme consists of a single polypeptide chain.The rate equation of the enzyme reaction for two substrates was used for the determination of five kinetic constants. The equilibrium constant with respect to PGE2 was 83 μM, the Michaelis constant, Km, for PGE2 was 93 μM. For NADPH, the equilibrium constant was 1.0 μM and Km was 1.6 μM. The maximal velocity for the forward reaction was V1= 217 pmol/min. The inhibition constants for the analgesic agents indomethacin and fentiazac were Ki= 850 μM and Ki= 450 μM and for the steroid progesterone Ki= 1.5 mM, respectively.Prostaglandin‐E2 9‐ketoreductase might be responsible for the control of the PGE2/PGF2α ratio in human decidua vera. The enzyme, therefore, might be an important factor in the cascade of events leading to uterine contractions and parturition.

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