PROSITE documentation PDOC50244Steroid 5-alpha reductase C-terminal domain profile
Description
Steroid 5-α reductases (EC 1.3.99.5) are responsible for the NADPH-dependent reduction of testosterone into dihydrotestosterone, a key reaction in androgen action [1]. This enzyme is also found in plants where it is involved in brassinosteroids biosynthesis [2]. A domain of around 80 amino acids is found in the C-terminal part of the protein and contains the binding site for NADPH [3].
Last update:April 2002 / First entry.
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References
| 1 | Authors | Russell D.W. Wilson J.D. |
| Title | Steroid 5 alpha-reductase: two genes/two enzymes. | |
| Source | Annu. Rev. Biochem. 63:25-61(1994). | |
| PubMed ID | 7979239 | |
| DOI | 10.1146/annurev.bi.63.070194.000325; |
| 2 | Authors | Li J. Biswas M.G. Chao A. Russell D.W. Chory J. |
| Title | Conservation of function between mammalian and plant steroid 5alpha-reductases. | |
| Source | Proc. Natl. Acad. Sci. U.S.A. 94:3554-3559(1997). | |
| PubMed ID | 9108014 |
| 3 | Authors | Bhattacharyya A.K. Chavan A.J. Haley B.E. Taylor M.F. Collins D.C. |
| Title | Identification of the NADP(H) binding site of rat liver microsomal 5 alpha-reductase (isozyme-1): purification of a photolabeled peptide corresponding to the adenine binding domain. | |
| Source | Biochemistry 34:3663-3669(1995). | |
| PubMed ID | 7893662 |
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