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ACS chemical biology v.12 no.1, 2017년, pp.63 - 72   SCIE
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An Effective Bacterial Fucosidase for Glycoprotein Remodeling

Tsai, Tsung-I (Genomics Research Center, Academia Sinica, No. 128, Section 2, Academia Road, Taipei 115, ); Li, Shiou-Ting (Genomics Research Center, Academia Sinica, No. 128, Section 2, Academia Road, Taipei 115, ); Liu, Chiu-Ping (Genomics Research Center, Academia Sinica, No. 128, Section 2, Academia Road, Taipei 115, ); Chen, Karen Y. (Genomics Research Center, Academia Sinica, No. 128, Section 2, Academia Road, Taipei 115, ); Shivatare, Sachin S. (Genomics Research Center, Academia Sinica, No. 128, Section 2, Academia Road, Taipei 115, ); Lin, Chin-Wei (Genomics Research Center, Academia Sinica, No. 128, Section 2, Academia Road, Taipei 115, ); Liao, Shih-Fen (Genomics Research Center, Academia Sinica, No. 128, Section 2, Academia Road, Taipei 115, ); Lin, Chih-Wei (Genomics Research Center, Academia Sinica, No. 128, Section 2, Academia Road, Taipei 115, ); Hsu, Tsui-Ling (Genomics Research Center, Academia Sinica, No. 128, Section 2, Academia Road, Taipei 115, ); Wu, Ying-Ta (Genomics Research Center, Academia Sinica, No. 128, Section 2, Academia Road, Taipei 115, ); Tsai, Ming-Hung (CHO Pharma Inc., Taipei 11503, ); Lai, Meng-Yu (CHO Pharma Inc., Taipei 11503, ); Lin, Nan-Horng (CHO Pharma Inc ); Wu, Chung-Yi ( ); Wong, Chi-Huey ( );
  • 초록  

    Fucose is an important component of many oligo- and polysaccharide structures as well as glycoproteins and glycolipids, which are often associated with a variety of physiological processes ranging from fertilization, embryogenesis, signal transduction, and disease progression, such as rheumatoid arthritis, inflammation, and cancer. The enzyme α- l -fucosidase is involved in the cleavage of the fucosidic bond in glycans and glycoconjugates, particularly the Fuc-α-1,2-Gal, Fuc-α-1,3/4-GlcNAc, and Fuc-α-1,6-GlcNAc linkages. Here, we report a highly efficient fucosidase, designated as BfFucH identified from a library of bacterial glycosidases expressed in E. coli from the CAZy database, which is capable of hydrolyzing the aforementioned fucosidic linkages, especially the α-1,6-linkage from the N-linked Fuc-α-1,6-GlcNAc residue on glycoproteins. Using BfFucH coupled with endoglycosidases and the emerging glycosynthases allows glycoengineering of IgG antibodies to provide homogeneous glycoforms with well-defined glycan structures and optimal effector functions. Graphic Abstract ACS Electronic Supporting Info


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