[Review: Prize-awarded article] Study of Substrate Specificity for Glycosidase Inhibitor Design

Author:

Hakamata Wataru1

Affiliation:

1. Department of Chemistry and Life Sciences, College of Bioresource Science, Nihon University

Publisher

The Japanese Society of Applied Glycoscience

Subject

General Medicine

Reference35 articles.

1. 1) http://www.cazy.org/ (ページ取得日:2010 年9 月30 日)

2. 2) B.L. Cantarel, P.M. Coutinho, C. Rancurel, T. Bernard, V. Lombard and B. Henrissat: The Carbohydrate-Active EnZymes database (CAZy): an expert resource for glycogenomics. Nucleic Acids Res., 37, D233-238 (2009).

3. 3) G.J. Davies, T.M. Gloster and B. Henrissat: Recent structural insights into the expanding world of carbohydrate-active enzymes. Curr. Opin. Struct. Biol., 15, 637-645 (2005).

4. 8) M.M. Palcic, C.H. Scaman, A. Otter, A. Szpacenko, A. Romaniuk, Y.X. Li and I.K. Vijay: Processing α-glucosidase I is an inverting glycosidase. Glycoconjugate J., 16, 351-355 (1999).

5. 16) W. Hakamata, M. Muroi, K. Kadokura, T. Nishio, T. Oku, A. Kimura, S. Chiba and A. Takatsuki: Aglycon specificity profiling of α-glucosidases using synthetic probes. Bioorg. Med. Chem. Lett., 15, 1489-1492 (2005).

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