Relationship of human liver dihydrodiol dehydrogenases to hepatic bile-acid-binding protein and an oxidoreductase of human colon cells

Biochem J. 1996 Jan 15;313 ( Pt 2)(Pt 2):373-6. doi: 10.1042/bj3130373.


We previously isolated three monomeric dihydrodiol dehydrogenases, DD1, DD2 and DD4, from human liver, and cloned a cDNA (C9) thought to encode DD2, which is identical with those for human bile-acid-binding protein and an oxidoreductase of human colon carcinoma HT29 cells. In the present study we have provided evidence that the C9 cDNA clone encodes DD1, not DD2. A recombinant enzyme expressed from the cDNA in a bacterial system was purified, and its catalytic properties, bile-acid-binding ability and primary sequence were compared with those of the hepatic dihydrodiol dehydrogenases. The results show that DD1 encoded by C9 possesses prostaglandin F synthase activity but low affinity for lithocholic acid, whereas DD2, showing differences of six amino acid residues from the DD1 sequence, exhibited high-affinity binding for the bile acid. Refined relationship between dihydrodiol dehydrogenases and their related proteins of human tissues is proposed.

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Carrier Proteins / metabolism*
  • Colon / cytology
  • Colon / enzymology*
  • DNA, Complementary
  • Humans
  • Hydroxysteroid Dehydrogenases*
  • Liver / enzymology*
  • Membrane Glycoproteins*
  • Molecular Sequence Data
  • Oxidoreductases / metabolism*
  • Sequence Homology, Amino Acid
  • Substrate Specificity
  • Tumor Cells, Cultured


  • Carrier Proteins
  • DNA, Complementary
  • Membrane Glycoproteins
  • bile acid binding proteins
  • Oxidoreductases
  • Hydroxysteroid Dehydrogenases
  • AKR1C2 protein, human
  • trans-1,2-dihydrobenzene-1,2-diol dehydrogenase

Associated data

  • GENBANK/D26124
  • GENBANK/M86609
  • GENBANK/U05684