Skip Navigation

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Request Permissions
Google Scholar
Right arrow Articles by Hara, A.
Right arrow Articles by Sawada, H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hara, A.
Right arrow Articles by Sawada, H.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

J. Biochem, 1988, Vol. 103, No. 6 1027-1034
© 1988 Japanese Biochemical Society

research-article

Purification and Characterization of NADP+-Dependent 3{alpha}-Hydroxysteroid Dehydrogenase from Mouse Liver Cytosol

Akira Hara, Yoshio Inoue, Makoto Nakagawa, Fumiharu Naganeo and Hideo Sawada1

Department of Biochemistry, Gifu Pharmaceutical University Gifu, Gifu 502

1To whom correspondence should be addressed.

A monomeric 3{alpha}-hydroxysteroid dehydrogenase with a molecular weight of 34,000 was purified to apparent homogeneity from mouse liver cytosol. The enzyme catalyzed the reversible oxidation of the 3{alpha}-hydroxy group of C19-, C21-, and C24-steroids, reduced a variety of carbonyl compounds, and was inhibited by SH-reagents, synthetic estrogens, anti-inflammatory drugs, prostaglandins, and {delta}4-3-ketosteroids. Although these properties are similar to those of the enzyme from rat liver cytosol, the mouse enzyme exhibited low dehydrogenase activity toward benzene dihydrodiol and some alicyclic alcohols, it showed a strict cofactor specificity for NADP(H), and high substrate inhibition was observed in the reverse reaction. In addition, dexamethasone, deoxycorticosterone, and medroxyprogesterone acetate inhibited the mouse enzyme competitively at low concentrations and noncompetitively at high concentrations, whereas hexestrol, indomethacin, and prostaglandin A, were competitive inhibitors. Steady-state kinetic measurements in both directions indicated that the reaction proceeds through an ordered bi bi mechanism with the cofactors binding to the free enzyme. The 3-ketosteroid substrates inhibited the enzyme uncompetitively at elevated concentrations, suggesting that the substrates bind to the enzyme NADPH complex and to the enzyme NADP+ complex.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Proc. Natl. Acad. Sci. USAHome page
R. C. Agis-Balboa, G. Pinna, A. Zhubi, E. Maloku, M. Veldic, E. Costa, and A. Guidotti
Characterization of brain neurons that express enzymes mediating neurosteroid biosynthesis
PNAS, September 26, 2006; 103(39): 14602 - 14607.
[Abstract] [Full Text] [PDF]

Home page
 Biol. Reprod.Home page
R.-S. Ge, D. O. Hardy, J. F. Catterall, and M. P. Hardy
Opposing Changes in 3{alpha}-Hydroxysteroid Dehydrogenase Oxidative and Reductive Activities in Rat Leydig Cells during Pubertal Development
Biol Reprod, April 1, 1999; 60(4): 855 - 860.
[Abstract] [Full Text]

Home page
 J. Pharmacol. Exp. Ther.Home page
K. Matsuura, A. Hara, M. Kato, Y. Deyashiki, Y. Miyabe, S. Ishikura, T. Sugiyama, and Y. Katagiri
Activation of Human Liver 3alpha -Hydroxysteroid Dehydrogenase by Clofibrate Derivatives
J. Pharmacol. Exp. Ther., June 1, 1998; 285(3): 1096 - 1103.
[Abstract] [Full Text]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.