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Amphomycin: A tool to study protein N-glycosylation
Authors:Dipak Kumar Banerjee
Institution:(1) Department of Biochemistry and Nutrition, School of Medicine, University of Puerto Rico, 00936-5067 San Juan, Puerto Rico, USA
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.
Keywords:Glycosylation inhibitor  protein N-glycosylation  dolichylmonophosphate  lipid-linked pathway
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