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Human hepatic 3 alpha-hydroxysteroid dehydrogenase: possible identity with human hepatic chlordecone reductase.
- Source :
-
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 1992 Sep 16; Vol. 187 (2), pp. 760-6. - Publication Year :
- 1992
-
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.
- Subjects :
- 3-Hydroxysteroid Dehydrogenases chemistry
3-Hydroxysteroid Dehydrogenases immunology
3-alpha-Hydroxysteroid Dehydrogenase (B-Specific)
Alcohol Oxidoreductases chemistry
Alcohol Oxidoreductases immunology
Amino Acid Sequence
Electrophoresis, Polyacrylamide Gel
Humans
Immunoblotting
Molecular Sequence Data
Molecular Weight
NAD (+) and NADP (+) Dependent Alcohol Oxidoreductases
Peptide Fragments chemistry
Substrate Specificity
Trypsin
3-Hydroxysteroid Dehydrogenases metabolism
Alcohol Oxidoreductases metabolism
Liver enzymology
Subjects
Details
- Language :
- English
- ISSN :
- 0006-291X
- Volume :
- 187
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- Biochemical and biophysical research communications
- Publication Type :
- Academic Journal
- Accession number :
- 1530633
- Full Text :
- https://doi.org/10.1016/0006-291x(92)91260-w