A study on glycosylation of cationic peanut peroxidase.
Cationic peroxidase from a cell suspension culture has two heterogeneously glycosylated forms, based on their Concanavalin A column binding property, namely CP-and CP+. In these two forms three out of five potential glycosylation sites are used. Asn60 and Asn185 are located in hydrophilic beta-turns, while Asn144 in a hydrophobic beta-sheet. Asn209 and Asn275 lacking glycans all have a proline residue at the C-terminal of the consensus sequence. The difference between CP- and CP+ is due to the heterogeneous glycosylation at individual glycosylation sites.
Department of Plant Sciences, University of Western Ontario, London, Canada.
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van Huystee
D000595:Amino Acid Sequence; D010367:Arachis / Q000201:enzymology*; D001216:Asparagine / Q000737:chemistry; D016384:Consensus Sequence; D014644:Genetic Variation; D006020:Glycopeptides / Q000737:chemistry; D006023:Glycoproteins / Q000737:chemistry*; D006031:Glycosylation; D008969:Molecular Sequence Data; D009195:Peroxidase / Q000737:chemistry*; D011499:Protein Processing, Post-Translational; D017433:Protein Structure, Secondary
D006020:Glycopeptides; D006023:Glycoproteins; D001216:Asparagine; D009195:Peroxidase