| Abstract: |
Anhydroretinol and 14-hydroxy-4,14-retro-retinol, retro-retinoids endogenous to both mammals and insects, act as agonist and antagonist, respectively, in controlling proliferation in lymphoblasts and other retinol- dependent cells. We describe here the identification, purification, cloning, and bacterial expression of the enzyme retinol dehydratase, which converts retinol to anhydroretinol in Spodoptera frugiperda. Retinol dehydratase has nanomolar affinity for its substrate and is, therefore, the first enzyme characterized able to utilize free retinol at physiological intracellular concentrations. The enzyme shows sequence homology to the sulfotransferases and requires 3'-phosphoadenosine 5'-phosphosulfate for activity. |
| Keywords: |
nonhuman; mammalia; animals; gene expression; cell line; enzyme activity; enzyme substrate; bacteria (microorganisms); molecular cloning; cloning, molecular; lymphocyte differentiation; lymphocyte activation; amino acid sequence; molecular sequence data; sequence homology, amino acid; kinetics; recombinant proteins; substrate specificity; base sequence; spodoptera; sequence homology; retinol; mammals; enzyme purification; subcellular fractions; complementary dna; electrophoresis, polyacrylamide gel; dna, complementary; hexapoda; lepidoptera; chromatography, ion exchange; priority journal; article; hydro-lyases; adenosine 3' phosphate 5' phosphosulfate; hydrolyase; spodoptera frugiperda
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