• Amphomycin: A tool to study protein N-glycosylation

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      https://www.ias.ac.in/article/fulltext/jbsc/011/01-04/0311-0319

    • Keywords

       

      Glycosylation inhibitor; protein N-glycosylation; dolichylmonophosphate; lipid-linked pathway

    • 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.

    • Author Affiliations

       

      Dipak Kumar Banerjee1

      1. Department of Biochemistry and Nutrition, School of Medicine, University of Puerto Rico, San Juan, Puerto Rico - 00936-5067, USA
    • Dates

       
  • Journal of Biosciences | News

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