5α-Reductase activity in Lycopersicon esculentum: Cloning and functional characterization of LeDET2 and evidence of the presence of two isoenzymes

@article{Rosati20055ReductaseAI,
  title={5$\alpha$-Reductase activity in Lycopersicon esculentum: Cloning and functional characterization of LeDET2 and evidence of the presence of two isoenzymes},
  author={F. Rosati and I. Bardazzi and Paola Blasi and L. Simi and D. Scarpi and A. Guarna and M. Serio and M. Racchi and G. Danza},
  journal={The Journal of Steroid Biochemistry and Molecular Biology},
  year={2005},
  volume={96},
  pages={287-299}
}
The full-length cDNA (LeDET2) encoding a 257 amino acid protein homolog of Arabidopsis DET2 (AtDET2) was isolated in tomato (Lycopersicon esculentum). LeDET2 has 76% similarity with AtDET2 and structural characteristics conserved among plant and mammalian steroid 5alpha-reductases (5alphaRs). LeDET2 is ubiquitously expressed in tomato tissues with higher levels in leaf than in stem, root, seed and callus. When expressed in mammalian cells (COS-7), recombinant LeDET2 was active on substrates… Expand
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