Human Placental 17β-Estradiol Dehydrogenase. VI. Substrate Specificity of the Diphosphopyridine Nucleotide (Triphosphopyridine Nucleotide)-Linked Enzyme1
- 1 May 1971
- journal article
- other
- Published by The Endocrine Society in Endocrinology
- Vol. 88 (5) , 1165-1169
- https://doi.org/10.1210/endo-88-5-1165
Abstract
The substrate specificity of pure D(T)PN-linked 17β-estradiol dehydrogenase of human placenta was examined and shown to differ in several aspects from the results previously obtained with less pure preparations. The enzyme, in addition to having an absolute stereospecificity for the 17β-hydroxy group, appears also to have an absolute requirement for an aromatic ring A. Three non-aromatic steroids (testosterone, 19-nortestosterone and 20α-hydroxypregn- 4-en-3-one) previously reported to be substrates for 17β-estradiol dehydrogenase were not oxidized by the pure enzyme with either DPN or TPN as cofactors. Diethylstilbestrol, estriol, 17α-estradiol and 17β-hydroxy-4,4,17α-trimethyl- 3-oxoandrost-5-ene-2α-nitrile are weak inhibitors of 17β-estradiol dehydrogenase. (Endocrinology88: 1165, 1971)Keywords
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