Skip Navigation



Journal of Biochemistry Advance Access published online on May 23, 2007
Journal of Biochemistry, doi:10.1093/jb/mvm117
This Article
Right arrow Advance Access manuscript (PDF)
Right arrow All Versions of this Article:
142/2/175    most recent
mvm117v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Request Permissions
Google Scholar
Right arrow Articles by Kato, T.
Right arrow Articles by Yamamoto, K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kato, T.
Right arrow Articles by Yamamoto, K.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© 2007 The Japanese Biochemical Society

Unique peptide:N-glycanase of Caenorhabditis elegans has activity of protein disulfide 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: Hisashi Ashida: 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 disulfide 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 disulfide reductase, Thioredoxin


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?




Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.