Ling Wu

TL;DR: Four substitution and two splice junction mutations were identified in the 17βHSD3 genes of five unrelated male pseudohermaphrodites that severely compromised the activity of the 17 β–HSD type 3 isozyme.

TL;DR: The data suggest that the 17 beta-HSD type 2 cDNA encodes the microsomal 17 beta -HSD of human placenta, described by several laboratories.

TL;DR: It is suggested that the common mechanism for testosterone formation in postpubertal subjects with this disorder is the conversion of circulating androstenedione to testosterone by one or more of the unaffected 17 beta-hydroxysteroid dehydrogenase isoenzymes.

TL;DR: The 17β-HSD3 gene is mutated in male pseudohermaphrodites with the genetic disease 17β,HSD deficiency, and the enzyme possesses 20α- HSD activity demonstrated by its ability to convert 20α,dihydro-progesterone to progesterone.

TL;DR: To qualitatively assess the role arginine 80 plays in both selecting and stabilizing NADPH binding, it was replaced with each amino acid and the mutant enzymes subjected to enzymatic analysis and in no case was NADH found to substitute for NADPH.