Skip Navigation


Glycobiology Advance Access originally published online on June 17, 2008
Glycobiology 2008 18(9):727-734; doi:10.1093/glycob/cwn053
This Article
Right arrow Full Text Freely available
Right arrow FREE Full Text (PDF) Freely available
Right arrow All Versions of this Article:
18/9/727    most recent
cwn053v1
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 ISI Web of Science
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 Search for citing articles in:
ISI Web of Science (4)
Right arrowRequest Permissions
Right arrow Disclaimer
Google Scholar
Right arrow Articles by Ashida, H.
Right arrow Articles by Yamamoto, K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ashida, H.
Right arrow Articles by Yamamoto, K.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© The Author 2008. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

Characterization of two different endo-{alpha}-N-acetylgalactosaminidases from probiotic and pathogenic enterobacteria, Bifidobacterium longum and Clostridium perfringens

Hisashi Ashida1,2, Riichi Maki2, Hayato Ozawa2, Yasushi Tani2, Masashi Kiyohara2, Masaya Fujita3, Akihiro Imamura4, Hideharu Ishida4, Makoto Kiso4 and Kenji Yamamoto2

2 Graduate School of Biostudies, Kyoto University, Kyoto 606-8502
3 The Noguchi Institute, Tokyo 173-0003
4 Faculty of Applied Biological Science, Gifu University, Gifu 501-1193, Japan

1 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 on April 25, 2008; revised on May 27, 2008; accepted on June 2, 2008

Endo-{alpha}-N-acetylgalactosaminidase (endo-{alpha}-GalNAc-ase) catalyzes the hydrolysis of the O-glycosidic bond between {alpha}-GalNAc at the reducing end of mucin-type sugar chains and serine/threonine of proteins to release oligosaccharides. Previously, we identified the gene engBF encoding endo-{alpha}-GalNAc-ase from Bifidobacterium longum, which specifically released the disaccharide Galβ1-3GalNAc (Fujita K, Oura F, Nagamine N, Katayama T, Hiratake J, Sakata K, Kumagai H, Yamamoto K. 2005. Identification and molecular cloning of a novel glycoside hydrolase family of core 1 type O-glycan-specific endo-{alpha}-N-acetylgalactosaminidase from Bifidobacterium longum. J Biol Chem. 280:37415–37422). Here we cloned a similar gene named engCP from Clostridium perfringens, a pathogenic enterobacterium, and characterized the gene product EngCP. Detailed analyses on substrate specificities of EngCP and EngBF using a series of p-nitrophenyl-{alpha}-glycosides chemically synthesized by the di-tert-butylsilylene-directed method revealed that both enzymes released Hex/HexNAcβ1-3GalNAc (Hex = Gal or Glc). EngCP could also release the core 2 trisaccharide Galβ1-3(GlcNAcβ1-6)GalNAc, core 8 disaccharide Gal{alpha}1-3GalNAc, and monosaccharide GalNAc. Our results suggest that EngCP possesses broader substrate specificity than EngBF. Actions of the two enzymes on native glycoproteins and cell surface glycoproteins were also investigated.

Key words: endo-{alpha}-N-acetylgalactosaminidase / endoglycosidase / GH101 / mucin / O-glycan


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


This article has been cited by other articles:


Home page
 J BiochemHome page
R. Suzuki, T. Katayama, M. Kitaoka, H. Kumagai, T. Wakagi, H. Shoun, H. Ashida, K. Yamamoto, and S. Fushinobu
Crystallographic and Mutational Analyses of Substrate Recognition of Endo-{alpha}-N-acetylgalactosaminidase from Bifidobacterium longum
J. Biochem., September 1, 2009; 146(3): 389 - 398.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. Nakajima, M. Nishimoto, and M. Kitaoka
Characterization of Three {beta}-Galactoside Phosphorylases from Clostridium phytofermentans: DISCOVERY OF D-GALACTOSYL-{beta}1->4-L-RHAMNOSE PHOSPHORYLASE
J. Biol. Chem., July 17, 2009; 284(29): 19220 - 19227.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
E. L. Stone, M. N. Ismail, S. H. Lee, Y. Luu, K. Ramirez, S. M. Haslam, S. B. Ho, A. Dell, M. Fukuda, and J. D. Marth
Glycosyltransferase Function in Core 2-Type Protein O Glycosylation
Mol. Cell. Biol., July 1, 2009; 29(13): 3770 - 3782.
[Abstract] [Full Text] [PDF]


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.