N-Glycosylation patterns in two 伪-l-arabinofuranosidases from Penicillium canescens belonging to the glycoside hydrolase families 51 and 54

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• 作者：Alex ; er V. Gusakov ; Olga A. Sinitsyna ; Alex ; ra M. Rozhkova ; Arkady P. Sinitsyn
• 关键词：Glycoproteins ; MALDI-TOF mass spectrometry ; N-Glycosylation ; High-mannose glycans ; 伪-l-Arabinofuranosidase ; Penicillium canescens
• 刊名：Carbohydrate Research
• 出版年：15 December, 2013
• 年：2013
• 卷：382
• 期：Complete
• 页码：71-76
• 全文大小：1247 K

文摘

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 伪-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 伪-mannosidases and 尾-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.