Misfolding of glycoproteins is a prerequisite for peptide:: N-glycanase mediated deglycosylation

被引：30

作者：

Joshi, S ^{[1
]}

Katiyar, S ^{[1
]}

Lennarz, WJ ^{[1
]}

机构：

[1] SUNY Stony Brook, Dept Biochem & Cell Biol, Stony Brook, NY 11794 USA

来源：

FEBS LETTERS | 2005年 / 579卷 / 03期

关键词：

peptide : N-glycanase; glycoprotein; misfolding; deglycosylation; circular dichroism;

D O I：

10.1016/j.febslet.2004.12.060

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Peptide:N-glycanase (PNGase) is a deglycosylating enzyme that catalyzes the hydrolysis of the beta-aspartylglycosylamine bond of aspargine-linked glycopeptides and glycoproteins. Earlier studies from our laboratory indicated that PNGase catalyzed de-N-glycosylation was limited to glycopeptide substrates, but recent reports have demonstrated that it also acts upon full-length misfolded glycoproteins. In this study, we utilized two glycoprotein substrates, yeast carboxypeptidase and chicken egg albumin (ovalbumin), to study the deglycosylation activity of yeast PNGase and its mutants. Our results provide further evidence that PNGase acts upon full-length glycoprotein substrates and clearly establish that PNGase acts only on misfolded or denatured glycoproteins. (C) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：823 / 826

页数：4

共 18 条

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