Inhibitors of glycoprotein biosynthesis.
Altogether 30 different sugar analogues have been tested in a cell free system from rat liver or, in part, in freshly prepared hepatocytes. It is our aim to find suitable compounds which are able either to interfere with the metabolization of L-fucose, galactose and N-acetylmannosamine or, alternatively, to block the attachment of these sugars to the nascent oligosaccharide chain. 1-Methylfucoside inhibits the fucokinase by a competitive mode (Ki = 1.1 mmol/l). Both the fucokinase and fucose-1-phosphate pyrophosphorylase activity are impaired by Clobenoside, a chloro-containing glucofuranoside (Ki values between 5 to 10 mmol/l). In hepatocytes this inhibition leads to a drastic reduction of fucoprotein biosynthesis and secretion. 1-Methylenegalactose proved to be a promising competitive inhibitor of the galactokinase (Ki = 4.1 mmol/l), while the efficacy of 2-deoxy-2-fluoro-galactose and 6-deoxy-6-fluoro-galactose is less pronounced. Part of these sugar analogues could become a suitable tool in order to elucidate the biological significance of terminal and subterminal sugars.[1]References
- Inhibitors of glycoprotein biosynthesis. Reutter, W., Bauer, C. Adv. Enzyme Regul. (1985) [Pubmed]
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