Biosynthesis of prostaglandins.
Highly purified cyclooxygenase from sheep vesicular glands is stimulated by the presence of protoporphyrin IX compounds. This stimulation may be due to the conversion of an apoenzyme to the holoenzyme, and full activity is achieved when half of the enzyme subunits (70,000 daltons) bind heme. Also, one-half of the subunits appear to contain non-heme iron. The apparent molecular weight of the holoenzyme is approximately 300,000 daltons and is compatible with a complex of four 70,000 dalton subunits. Thus, we suggest that heme and non-heme iron may be attached to different 70,000 daltons subunits that make up an A2B2-type of peptide chain arrangement.
D000818:Animals; D006418:Heme / Q000494:pharmacology; D007501:Iron / Q000494:pharmacology; D007525:Isoelectric Focusing; D008297:Male; D006899:Mixed Function Oxygenases / Q000302:isolation & purification*; D008970:Molecular Weight; D011451:Prostaglandin-Endoperoxide Synthases / Q000302:isolation & purification* / Q000378:metabolism; D011453:Prostaglandins / Q000096:biosynthesis*; D012669:Seminal Vesicles / Q000201:enzymology*
D011453:Prostaglandins; D006418:Heme; D007501:Iron; D006899:Mixed Function Oxygenases; D011451:Prostaglandin-Endoperoxide Synthases