N-Terminal Deletion of Peptide:N-Glycanase Results in Enhanced Deglycosylation Activity
作者： Shengjun Wang , Fengxue Xin , Xiaoyue Liu , Yuxiao Wang , Zhenyi An
DOI: 10.1371/JOURNAL.PONE.0008335
关键词:
摘要: Peptide:N-glycanase catalyzes the detachment of N-linked glycan chains from glycopeptides or glycoproteins by hydrolyzing β-aspartylglucosaminyl bond. in yeast binds to Rad23p through its N-terminus. In this study, complex formed between and was found exhibit enhanced deglycosylation activity, which suggests an important role for enzyme misfolded glycoprotein degradation pathway vivo. To investigate pathway, we made stepwise deletions N-terminal helices peptide:N-glycanase. Enzymatic analysis deletion mutants showed that H1 helix (Png1p-ΔH1) activity N-glycanase towards denatured glycoproteins. addition, mutant exhibited high native Dynamic simulations wild type implied Png1p-ΔH1 is more flexible than Png1p. The efficient non-native offers a potential biotechnological application.
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