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• W1982991566 abstract "The enzyme PGC is produced by the fungus Aspergillus niger during invasion of plant cell walls. The enzyme has been homologously overexpressed to provide sufficient quantities of purified enzyme for biological studies. We have characterized this enzyme in terms of its posttranslational modifications (PTMs) and found it to be both N- and O-glycosylated. The glycosyl moieties have also been characterized. This has involved a combination of matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF), liquid chromatography (LC)–ion trap, and LC–electrospray ionization (ESI) mass spectrometries in conjunction with trypsin degradation and β-elimination, followed by Michael addition with dithiothreitol (BEMAD). This is the first demonstration of the ability of BEMAD to map glycosylation sites other than O-GlcNAc sites. The complete characterization of all PTMs on PGC allows us to model them on the peptide backbone, revealing potential roles played by the glycans in modulating the interaction of the enzyme with other macromolecules." @default.
• W1982991566 created "2016-06-24" @default.
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• W1982991566 date "2006-07-01" @default.
• W1982991566 modified "2023-09-27" @default.
• W1982991566 title "Comprehensive glycan analysis of recombinant Aspergillus niger endo-polygalacturonase C" @default.
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• W1982991566 doi "https://doi.org/10.1016/j.ab.2006.02.002" @default.
• W1982991566 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/16697346" @default.
• W1982991566 hasPublicationYear "2006" @default.
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