Molecular and kinetic properties of 15-hydroxyprostaglandin dehydrogenase (PG-15-HDH) from human placenta.
Some molecular properties of PG-15-HDH from human term placenta were investigated. Using a computer-based weighted linear regression analysis, intersecting initial rate patterns were received for the forward reaction with the prostaglandins (PG) E1, E2, and F2alpha, respectively, and NAD as substrates. NADH exerted a linear competitive inhibition with respect to NAD. The 15-ketoprostaglandins (15-keto-PG) E1 and F2alpha showed a linear noncompetitive inhibition with respect to their corresponding PG. The kinetic patterns suggest an ordered Bi Bi mechanism of PG-15-HDH reaction. The results are discussed with respect to their possible biological significance.
D000429:Alcohol Oxidoreductases / Q000378:metabolism; D005260:Female; D006801:Humans; D006911:Hydroxyprostaglandin Dehydrogenases / Q000378:metabolism; D007700:Kinetics; D007743:Labor, Obstetric; D009243:NAD / Q000378:metabolism; D010920:Placenta / Q000201:enzymology*; D011247:Pregnancy; D011458:Prostaglandins E / Q000378:metabolism; D011460:Prostaglandins F / Q000378:metabolism
D011458:Prostaglandins E; D011460:Prostaglandins F; D009243:NAD; D000429:Alcohol Oxidoreductases; D006911:Hydroxyprostaglandin Dehydrogenases