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Hydroxysteroid dehydrogenase

About: Hydroxysteroid dehydrogenase is a research topic. Over the lifetime, 1087 publications have been published within this topic receiving 28468 citations. The topic is also known as: hydroxysteroid dehydrogenase.


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Journal ArticleDOI
01 Sep 2011-Steroids
TL;DR: A thermostable 7α-hydroxysteroid dehydrogenase from B. fragilis might play multiple functional roles in biosynthesis and metabolism of bile acids, and in the detoxification of xenobiotics containing carbonyl groups in the large intestine, and its broad substrate spectrum offers great potential for finding applications.

14 citations

Journal ArticleDOI
01 Jan 1992
TL;DR: Three enzyme forms of carbonyl reductase were purified from chicken liver with using 4-benzoylpyridine as a substrate and the results suggest that CR1 is a hydroxysteroid dehydrogenase, and CR2 and CR3 are similar to each other and to the kidney enzymes.
Abstract: Three enzyme forms (CR1, CR2 and CR3) of carbonyl reductase were purified from chicken liver with using 4-benzoylpyridine as a substrate. CR1 was a dimeric enzyme composed of two identical 25-kD subunits. CR2 and CR3 were monomeric enzymes whose molecular weights were both 32 kD. CR1 exhibited 17 beta-hydroxysteroid dehydrogenase activity as well as carbonyl reductase activity in the presence of both NADP(H) and NAD(H). CR2 and CR3 had similar properties with regard to substrate specificity and inhibitor sensitivity. They could exhibit the activity only with NADPH and had no hydroxysteroid dehydrogenase activity. CR2 and CR3 cross-reacted with anti-chicken kidney carbonyl reductase antibody, though CR1 did not. The results suggest that CR1 is a hydroxysteroid dehydrogenase, and CR2 and CR3 are similar to each other and to the kidney enzymes.

13 citations

Journal ArticleDOI
TL;DR: Only trace 3β-hydroxysteroid dehydrogenase activity was demonstrable in renal tissue, however liver possessed a higher level of activity and lanosterol, a precurser of cholesterol, was an especially suitable substrate possibly indicating that the liver is capable of synthesising cholesterol.
Abstract: Mouse, rat, hamster, guinea pig and sheep kidneys and foetal human, adult male and female human, mouse, rat, hamster and guinea pig livers were examined for hydroxysteroid dehydrogenase activity. 3α-Hydroxysteroids were utilised by all tissues, including neonatal mouse kidney, but the 5α-configuration was a more suitable substrate than the corresponding 5β-steroid. Both N.A.D. and N.A.D.P. were suitable cofactors. Only trace 3β-hydroxysteroid dehydrogenase activity was demonstrable in renal tissue, however liver possessed a higher level of activity and lanosterol, a precurser of cholesterol, was an especially suitable substrate possibly indicating that the liver is capable of synthesising cholesterol. 6β-Hydroxyprogesterone was poorly utilized by renal and hepatic tissue and N.A.D. was found to be the only cofactor suitable for this reaction. All the tissues, possessed 11β-hydroxysteroid dehydrogenase activity. In the kidney, this enzyme occurred in the collecting tubules. It was further noted that in mouse kidney 11β-hydroxysteroid dehydrogenase was absent at birth but appeared within the first fourteen days. Activity with 11β-hydroxysteroids was observed to be more prominent in the liver of male animals and this pattern was also found with 3α-, 3β-, 16α- and 16β-hydroxysteroids, all of which are confirmed by previous biochemical findings. Renal tissue was not capable of utilizing the 16α-hydroxysteroid in contrast to liver which could use this substrate fairly well. 16β- and 17β-hydroxysteroid dehydrogenases were demonstrable in the livers of all species and in all kidneys. The 20β-hydroxysteroid was only poorly utilized by hepatic tissue and not at all by renal tissue. Slight activity was demonstrable with 5α- and 5β-androstans as substrates in liver and the diformazan deposition was presumably due to the action of a steroid reductase.

13 citations

Journal ArticleDOI
TL;DR: Comparison of all retrieved 17beta-HSD 2 sequences indicates that this functional loss may have occurred only in zebrafish, where steroid inactivation at position C17 seems to pursue without the protein studied.

13 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
202319
202217
20218
202016
201916
20186