Specificity of polyprenyl phosphates in the in vitro formation of lipid-linked sugars
| Autor: | T. Mańkowski, Tadeusz Chojnacki, Ewa Janczura, W. Sasak |
|---|---|
| Rok vydání: | 1977 |
| Předmět: |
Guanosine Diphosphate Mannose
Uridine Diphosphate Glucose Stereochemistry Biophysics Biochemistry Structure-Activity Relationship chemistry.chemical_compound Residue (chemistry) Organophosphorus Compounds Glycosyltransferase Animals Glycosyl Molecular Biology Membranes Uridine Diphosphate N-Acetylglucosamine Bacteria biology Terpenes Phosphate Rats Uridine diphosphate N-acetylglucosamine chemistry Galactose Microsomes Liver Uridine diphosphate glucose biology.protein bacteria Glycolipids Guanosine diphosphate mannose |
| Zdroj: | Archives of Biochemistry and Biophysics. 181:393-401 |
| ISSN: | 0003-9861 |
| DOI: | 10.1016/0003-9861(77)90244-2 |
| Popis: | Various polyprenyl phosphates were prepared by chemical phosphorylation of native and partially hydrogenated polyprenols. They were tested as lipid acceptors of sugars from nucleoside diphosphate sugars using a microsomal preparation from rat liver and membrane preparations from B. stearothermophilus, S. typhimurium, and Sh. flexneri. With the microsomal glycosyl transferase system, a demand for saturation of the α-isoprene residue of polyprenyl phosphate was observed; the chain length and cis/trans configuration of polyprenyl radical were less important. With bacterial glycosyl transferases, a demand for the unsaturated α-isoprene residue was observed. In B. stearothermophilus, the rate of synthesis of polyprenyl monophosphate glucose did not depend on the chain length of fully unsaturated polyprenyl phosphate. In S. typhimurium, C55-polyprenyl phosphate was the most effective precursor of polyprenyl diphosphate galactose. |
| Databáze: | OpenAIRE |
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