cDNA cloning, tissue distribution, and substrate characteristics of a cis-Retinol/3alpha-hydroxysterol short-chain dehydrogenase isozyme.

@article{Su1998cDNACT,
  title={cDNA cloning, tissue distribution, and substrate characteristics of a cis-Retinol/3alpha-hydroxysterol short-chain dehydrogenase isozyme.},
  author={Jian Su and Xiaomei Chai and Barbara E. Kahn and Joseph L. Napoli},
  journal={The Journal of biological chemistry},
  year={1998},
  volume={273 28},
  pages={
          17910-6
        }
}
We report here a mouse cDNA that encodes a 316-amino acid short-chain dehydrogenase that prefers NAD+ as its cofactor and recognizes as substrates androgens and retinols, i.e. has steroid 3alpha- and 17beta-dehydrogenase and cis/trans-retinol catalytic activities. This cis-retinol/androgen dehydrogenase type 2 (CRAD2) shares close amino acid similarity with mouse retinol dehydrogenase isozyme types 1 and 2 and CRAD1 (86, 84, and 87%, respectively). CRAD2 exhibits cooperative kinetics with… CONTINUE READING

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