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Journal of Biochemistry Advance Access originally published online on May 23, 2007
Journal of Biochemistry 2007 142(2):175-181; doi:10.1093/jb/mvm117
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© 2007 The Japanese Biochemical Society.

Unique Peptide:N-glycanase of Caenorhabditis elegans has Activity of Protein Disulphide Reductase as well as of Deglycosylation

Toshihiko Kato, Akihito Kawahara, Hisashi Ashida* and Kenji Yamamoto

Division of Integrated Life Science, Graduate School of Biostudies, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan

*To whom correspondence should be addressed. Tel: +81-75-753-4298, Fax: +81-75-753-9228, E-mail: ashida{at}lif.kyoto-u.ac.jp

Received March 28, 2007; Accepted May 8, 2007


  Abstract

Peptide:N-glycanase (PNGase) is the enzyme responsible for de-N-glycosylation of misfolded glycoproteins in the cytosol. Here, we report the molecular identification and characterization of PNGase (png-1, F56G4.5) from Caenorhabditis elegans. This enzyme released both high mannose- and complex-type N-glycans from glycopeptides and denatured glycoproteins. Deglycosylation activity was inhibited by Zn2+ and z-VAD-fmk, but not by EDTA. PNG-1 has a thioredoxin-like domain in addition to a transglutaminase domain, the core domain of PNGases, and exhibited protein disulphide reductase activity in vitro. Our biochemical studies revealed that PNG-1 is a unique bifunctional protein possessing two enzyme activities.

Key Words: Caenorhabditis elegans, deglycosylation, peptide:N-glycanase, protein disulphide reductase, thioredoxin

Abbreviations: ER, endoplasmic reticulum; ERAD, ER-associated degradation; MBP, maltose-binding protein; PNGase, peptide:N-glycanase; SGP, sialylglycopeptide; z-VAD-fmk, carbobenzyloxy-Val-Ala-Asp-{alpha}-fluoromethylketone


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