15‐Hydroxy‐Prostanoate Dehydrogenase. Prostaglandins as Substrates and Inhibitors

The Michaelis constants and maximum reaction rates were determined for a series of substrates for 15‐hydroxyprostanoate dehydrogenase (prostaglandin dehydrogenase). The results show that the enzyme is stereospecific with regard to the configuration at C‐15. The nature of the substituents of the cyclopentane ring did not markedly affect the properties as a substrate, whereas the nature of the carboxyl side chain was important. Prostaglandin B compounds and a synthetic epimer of prostaglandin E1, 15‐R‐prostaglandin E1, produced a non‐competitive inhibition.