A MAMMALIAN 3α-HYDROXYSTEROID DEHYDROGENASE
نویسندگان
چکیده
منابع مشابه
Activation of human liver 3α-hydroxysteroid dehydrogenase by sulphobromophthalein
Human liver contains at least two isoenzymes (DD2 and DD4) of 3α-hydroxysteroid}dihydrodiol dehydrogenase. The NADP(H)-linked oxidoreductase activities of DD4 were activated more than 4-fold by sulphobromophthalein at concentrations above 20 μM and under physiological pH conditions. Sulphobromophthalein did not stimulate the activities of DD2 and human liver aldehyde reductase, which are functi...
متن کاملConversion of mammalian 3alpha-hydroxysteroid dehydrogenase to 20alpha-hydroxysteroid dehydrogenase using loop chimeras: changing specificity from androgens to progestins.
Hydroxysteroid dehydrogenases (HSDs) regulate the occupancy and activation of steroid hormone receptors by converting potent steroid hormones into their cognate inactive metabolites. 3alpha-HSD catalyzes the inactivation of androgens in the prostate by converting 5alpha-dihydrotestosterone to 3alpha-androstanediol, where excess 5alpha-dihydrotestosterone is implicated in prostate disease. By co...
متن کاملCharacterization of a human 20 -hydroxysteroid dehydrogenase
It has been suggested that 20 -hydroxysteroid dehydrogenase (20 -HSD) is a T-cell differentiation marker in mice. In the human, this enzyme has generally been associated with types 1 and 2 17 -HSDs, which belong to the short-chain alcohol dehydrogenase family, whereas the rat, rabbit, pig and bovine 20 -HSDs are members of the aldoketo reductase superfamily, which also includes the 3 -HSD famil...
متن کاملThe Del1 deposition domain can immobilize 3α-hydroxysteroid dehydrogenase in the extracellular matrix without interfering with enzymatic activity
Developing methods that result in targeting of therapeutic molecules in gene therapies to target tissues has importance, as targeting can increase efficacy and decrease off target-side-effects. Work from my laboratory previously showed that the extracellular matrix protein Del1 is organized in the extracellular matrix (ECM) via the Del1 deposition domain (DDD). In this work, a fusion protein wi...
متن کاملAPO AND HOLO STRUCTURES OF 3α-HYDROXYSTEROID DEHYDROGENASE FROM Pseudomonas sp. B-0831: LOOP-HELIX TRANSITION INDUCED BY COENZYME BINDING
Takuya Yoshida, Yuji Kobayashi, and Tadayasu Ohkubo From the Graduate School of Pharmaceutical Sciences, Osaka University, 1-6 Yamadaoka, Suita, Osaka 565-0871, Japan, the Graduate School of Agriculture, Kyoto Prefectural University, 1-5 Hangi-cho, Shimogamo, Sakyo-ku, Kyoto 606-8522, Japan, the Diagnostics Department, Asahi Kasei Pharma Corporation, 632-1 Mifuku, Izunokuni, Shizuoka 410-2321, ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1956
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)65907-1