The primary prostaglandin-inactivating enzyme of human placenta is a dimeric short-chain dehydrogenase.
The native form of NAD-dependent 15-hydroxyprostaglandin dehydrogenase of human placenta has a mol. wt. of about 50 000, while the subunit mol. wt. is around 28 000, suggesting a dimeric quaternary structure. These properties, the amino acid composition, insensitivity to EDTA, and inhibition patterns show general similarities to other short-chain dehydrogenases. Several hormones tested did not influence the activity of 15-hydroxyprostaglandin dehydrogenase, but an unusual activation by two anti-depressant drugs was found and may relate to the existence of a natural regulatory factor.
D000596:Amino Acids / Q000032:analysis; D005260:Female; D006801:Humans; D006911:Hydroxyprostaglandin Dehydrogenases / Q000037:antagonists & inhibitors / Q000302:isolation & purification*; D046911:Macromolecular Substances; D008970:Molecular Weight; D010920:Placenta / Q000201:enzymology*; D011247:Pregnancy; D011453:Prostaglandins / Q000378:metabolism*
D000596:Amino Acids; D046911:Macromolecular Substances; D011453:Prostaglandins; D006911:Hydroxyprostaglandin Dehydrogenases