Human hepatic 3 alpha-hydroxysteroid dehydrogenase: possible identity with human hepatic chlordecone reductase

Biochem Biophys Res Commun. 1992 Sep 16;187(2):760-6. doi: 10.1016/0006-291x(92)91260-w.

Abstract

3 alpha-Hydroxysteroid dehydrogenase is a cytosolic, monomeric, NADPH-dependent oxidoreductase which reduces 3-keto-5-dihydrosteroids to their tetrahydro products. We present here the first partial amino acid sequence data for the human liver enzyme and show these sequences to be identical to the deduced amino acid sequence for human hepatic chlordecone reductase. In addition, these two enzymes exhibit similar substrate and cofactor specificities and immunological reactivity. The results suggest that the natural substrates for chlordecone reductase are 3-keto-5-dihydrosteroids and that these two proteins may be identical.

Publication types

  • Comparative Study
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • 3-Hydroxysteroid Dehydrogenases / chemistry
  • 3-Hydroxysteroid Dehydrogenases / immunology
  • 3-Hydroxysteroid Dehydrogenases / metabolism*
  • 3-alpha-Hydroxysteroid Dehydrogenase (B-Specific)
  • Alcohol Oxidoreductases / chemistry
  • Alcohol Oxidoreductases / immunology
  • Alcohol Oxidoreductases / metabolism*
  • Amino Acid Sequence
  • Electrophoresis, Polyacrylamide Gel
  • Humans
  • Immunoblotting
  • Liver / enzymology*
  • Molecular Sequence Data
  • Molecular Weight
  • NAD (+) and NADP (+) Dependent Alcohol Oxidoreductases
  • Peptide Fragments / chemistry
  • Substrate Specificity
  • Trypsin

Substances

  • Peptide Fragments
  • 3-Hydroxysteroid Dehydrogenases
  • Alcohol Oxidoreductases
  • NAD (+) and NADP (+) Dependent Alcohol Oxidoreductases
  • chlordecone reductase
  • 3-alpha-Hydroxysteroid Dehydrogenase (B-Specific)
  • Trypsin