Studies on peroxidase-catalyzed formation of progesterone.
Subcellular fractions of pregnant rabbit ovary at day six of gestation catalysed the formation of progesterone from pregnenolone (3 beta-hydroxy-5-pregnen-20-one). The microsomal fraction was found to have maximum activity. The enzyme needed hydrogen peroxide for its activity. In vitro studies using horseradish peroxidase also showed similar conversion and this was stimulated 200% in the presence of ascorbic acid. Ascorbate thus appears to perform a catalytic role in this conversion. The importance of peroxidase in luteal steroidogenesis is indicated.
D000818:Animals; D002250:Carbon Radioisotopes; D005260:Female; D006735:Horseradish Peroxidase / Q000378:metabolism; D006861:Hydrogen Peroxide / Q000378:metabolism; D008861:Microsomes / Q000201:enzymology*; D010053:Ovary / Q000201:enzymology*; D010544:Peroxidases / Q000378:metabolism*; D011374:Progesterone / Q000096:biosynthesis*; D011817:Rabbits; D011863:Radioimmunoassay
D002250:Carbon Radioisotopes; D011374:Progesterone; D006861:Hydrogen Peroxide; D006735:Horseradish Peroxidase; D010544:Peroxidases