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Journal of Biochemistry Advance Access published online on October 22, 2007
Journal of Biochemistry, doi:10.1093/jb/mvm186
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© 2007 The Japanese Biochemical Society

A Novel {alpha}1,2-L-Fucosidase Acting on Xyloglucan Oligosaccharides Is Associated with Endo-ß-Mannosidase

Takeshi Ishimizu, Chikako Hashimoto, Ryo Takeda, Kenta Fujii and Sumihiro Hase

Department of Chemistry, Graduate School of Science, Osaka University, Osaka 560-0043, Japan

To whom correspondence should be sent: Dr. Takeshi Ishimizu, Department of Chemistry, Graduate School of Science, Osaka University, 1-1 Machikaneyamacho, Toyonaka, Osaka 560-0043, Japan, Tel: +81-6-6850-5381; Fax: +81-6-6850-5382; E-mail: txi{at}chem.sci.osaka-u.ac.jp

Received August 29, 2007; Accepted September 19, 2007


  Abstract

SUMMARY

Endo-ß-mannosidase, which hydrolyzes the Manß1-4GlcNAc linkage of N-glycans in an endo-manner, was discovered in plants [Ishimizu, T. Sasaki, A., Okutani, S., Maeda, M., Yamagishi, M., Hase, S. J. Biol. Chem. 279, 38555-38562 (2004)]. During the course of the purification of the enzyme from lily flowers, we found a higher molecular mass form of the enzyme (designated as EBM II). EBM II was purified by column chromatgraphy to homogeneity and its molecular composition revealed EBM II to be comprised of endo-ß-mannosidase and an associated protein. The cDNA of this associated protein encodes a protein with slight homology to the fucosidase domain of bifidus AfcA. EBM II has {alpha}1,2-L-fucosidase activity and acts on a fucosylated xyloglucan nonasaccharide. The amino acid sequence of this associated protein has no similarity to known plant {alpha}-L-fucosidases. These results show that EBM II is a novel {alpha}1,2-L-fucosidase and a protein complex containing endo-ß-mannosidase.

Key Words: endo-ß-mannosidase, fucosidase, plant, protein complex, xyloglucan


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