title: Subcellular localization and substrate specificity of dolichol kinase from rat liver.
abstract: When purified subcellular fractions were prepared from rat liver and assayed for dolichol kinase activity using pig liver dolichol as a substrate, the microsomes were found to contain the highest specific activity and greater than 75% of the total activity. With regard to substrate specificity, the microsomal enzyme showed a marked preference for saturation of the alpha-isoprene: dolichol-16 and -19 were 2.5-fold more active than the corresponding polyprenols. For a given class of prenol, the 16 and 19 isoprenologs exhibited similar activity, whereas the 11 isoprenolog appeared less active. The enzyme was twice as active against the naturally occurring polyprenol-16 (alpha-cis-isoprene) compared to synthetic alpha-trans-polyprenol-16. Taken together, the data indicate that the alpha-isoprene specificity follows the order: saturated greater than cis greater than trans. In addition, all-trans-2,3-dihydrosolanesol was not a substrate, suggesting that at least one cis isoprene residue is required.
mesh_terms: D000818:Animals; D008099:Liver / Q000201:enzymology*; D008297:Male; D010770:Phosphotransferases / Q000378:metabolism*; D017853:Phosphotransferases (Alcohol Group Acceptor); D051381:Rats; D011919:Rats, Inbred Strains; D013347:Subcellular Fractions / Q000201:enzymology; D013379:Substrate Specificity; D013997:Time Factors; D014018:Tissue Distribution
chemical_list: D010770:Phosphotransferases; D017853:Phosphotransferases (Alcohol Group Acceptor); C020087:dolichol kinase