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Glycobiology, 2000, Vol. 10, No. 12 1283-1289
© 2000 Oxford University Press

N-linked oligosaccharide processing enzyme glucosidase II produces 1,5-anhydrofructose as a side product

Kiyoko Hirano3,4, Martin Ziak4, Keiichi Kamoshita5, Yoshikazu Sukenaga5, Shunichi Kametani1,3, Yoko Shiga3, Jürgen Roth4 and Hiroshi Akanuma2,3

3Department of Life Sciences (Chemistry), Graduate School of Arts and Sciences, The University of Tokyo, Komaba, Meguro-ku, Tokyo 153–8902, Japan, 4Division of Cell and Molecular Pathology, Department of Pathology, University of Zürich, 8091 Zürich, Switzerland, and the 5Pharmaceuticals Group, Nippon Kayaku Co., Ltd., Kita-ku Tokyo 115–0042, Japan

{alpha}-1,4-Glucan lyase cleaves {alpha}-1,4-linkages of nonreducing termini of {alpha}-1,4-glucans to produce 1,5-anhydrofructose (1,5-AnFru). The enzymes isolated from fungi and algae show high homology with glycoside hydrolase family 31. Purification of {alpha}-1,4-glucan lyase from rat liver using DEAE Cellulose chromatography resulted in separation of two enzymatic active fractions, one was bound to the column and the other was in the flow-through. Partial amino acid sequence determined from the lyase, retained on the anion exchange column, were identical with that of the N-linked oligosaccharide processing enzyme glucosidase II. The lyase showed similar enzymatic properties as the microsomal glucosidase such as inhibition by 1-deoxynojirimycin and castanospermine. On the other hand, glucosidase II purified from rat liver microsomes produced not only glucose but also a small amount of 1,5-AnFru using maltose as substrate. Furthermore, CHO cells overexpressing pig liver glucosidase II showed a 1.5- to 2-fold higher lyase activity compared to the nontransfected CHO cells. Conversely, no lyase activity was detectable either in PHAR2.7, the glucosidase II-deficient mutant from a mouse lymphoma cell line, or in Saccharomyces cerevisiae strain YG427 having the glucosidase II gene disrupted. These data demonstrate that glucosidase II possesses an additional enzymatic activity of releasing 1,5-AnFru from maltose.

1 Present address: Taisho Pharmaceutical Co., Ltd., Yoshino-cho Ohmiya, Saitama 330–8530, Japan

2 To whom correspondence should be addressed


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