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N-Glycosylation patterns in two α-l-arabinofuranosidases fromPenicillium canescensbelonging to the glycoside hydrolase families 51 and 54

Authors
Journal
Carbohydrate Research
0008-6215
Publisher
Elsevier
Publication Date
Volume
382
Identifiers
DOI: 10.1016/j.carres.2013.08.026
Keywords
  • Glycoproteins
  • Maldi-Tof Mass Spectrometry
  • N-Glycosylation
  • High-Mannose Glycans
  • α-L-Arabinofuranosidase
  • Penicillium Canescens

Abstract

Abstract Using MALDI-TOF mass spectrometry (MS) peptide fingerprinting procedure followed by the analysis of MS data with the GlycoMod tool from the ExPASy proteomic site, N-glycosylation of two GH51 and GH54 family α-l-arabinofuranosidases (Abf51A and Abf54A) from Penicillium canescens was studied. Variable N-linked glycans were identified at five out of eight potential N-glycosylation sites in the Abf51A and one out of three potential N-glycosylation sites in the Abf54A. The discriminated glycans represented high-mannose oligosaccharides (Man)x(GlcNAc)2 with a number of Man residues up to 7 or the products of sequential enzymatic trimming of a high-mannose glycan with α-mannosidases and β-N-acetylhexosaminidases. The Abf54A peptide, containing the Asn254 glycosylation site, and one peptide from the Abf51A, containing the Asn163 glycosylation site, were found to exist not only in glycosylated, but also in a native non-modified form.

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