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Title 

Molecular characterization of acidic peptide:N-glycanase from the dimorphic yeast Yarrowia lipolytica

Authors 

Kyung Jin LeeJin Young GilSang Yoon KimOh Suk KwonK KoD I KimD K KimH H KimDoo-Byoung Oh

Publisher 

Oxford University Press

Issue Date 

2015

Citation 

Journal of Biochemistry, vol. 157, no. 1, pp. 35-43

Keywords 

acidic peptide:N-glycanseglycan analysisglycopeptideglycoproteinYarrowia lipolytica

Abstract 

Peptide:N-glycanase (PNGase) A is used preferentially to cleave the glycans from plant and insect glycopeptides. Although many putative PNGase A homologous genes have been found in the plant and fungus kingdoms through sequence similarity analyses, only several PNGases from plants and one from a filamentous fungus have been characterized. In this study, we identified and characterized a PNGase A-like enzyme, PNGase Yl, in the dimorphic yeast Yarrowia lipolytica. The corresponding gene was cloned and recombinantly expressed in Pichia pastoris. The purified enzyme cleaved glycans from glycopeptides with the maximum activity at pH 5. No metal ions were required for full activity, and rather it was repressed by three metal ions (Fe3+, Cu2+ and Zn2+). Using glycopeptide substrates, PNGase Yl was shown to release various types of N-glycans including high-mannose and complex-type glycans as well as glycans containing core-linked α(1,3)-fucose that are frequently found in plants and insects. Moreover, in comparison with PNGase A, PNGase Yl was able to cleave with higher efficiency the glycans from some denatured glycoproteins. Taken together, our results suggest that PNGase Yl, the first biochemically characterized yeast PNGase A homologue, can be developed through protein engineering as a useful deglycosylation tool for N-glycosylation study.

ISSN 

0021-924X

Link 

http://dx.doi.org/10.1093/jb/mvu051

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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