Amphomycin: A tool to study protein N-glycosylation |
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Authors: | Dipak Kumar Banerjee |
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Institution: | (1) Department of Biochemistry and Nutrition, School of Medicine, University of Puerto Rico, 00936-5067 San Juan, Puerto Rico, USA |
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Abstract: | Radio-labelled amphomycin (3H-amphomycin) forms a complex with dolichylmonophosphate in presence of Ca2+. Complex formation has also been documented with retinylmonophosphate and perhydromonoeneretinylmonophosphate. Analysis of
the space-filling model suggested both fatty acylated aspartic acid residue at the N-terminus of the lipopeptide and phosphate
head group of dolichylmonophosphate are necessary for the complex formation. The binding ability of amphomycin is then utilized
to localize dolichylmonophosphate in the microsomal membrane. Studies with microsomal membranes from hen oviduct suggested
that dolichylmonophosphate is located in the cytoplasmic side of the membrane. |
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Keywords: | Glycosylation inhibitor protein N-glycosylation dolichylmonophosphate lipid-linked pathway |
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