Journal of Bioprocessing & Biotechniques

Yu-Ning Huang

Publications

• Research Article
  Structure and Catalytic Mechanism of a Glycoside Hydrolase Family-127 β-L-Arabinofuranosidase (HypBA1)
  Author(s): Chun-Hsiang Huang, Zhen Zhu, Ya-Shan Cheng, Hsiu-Chien Chan, Tzu-Ping Ko, Chun-Chi Chen, Iren Wang, Meng-RuHo, Shang-Te Danny Hsu, Yi-Fang Zeng, Yu-Ning Huang, Je-Ruei Liu and Rey-Ting GuoChun-Hsiang Huang, Zhen Zhu, Ya-Shan Cheng, Hsiu-Chien Chan, Tzu-Ping Ko, Chun-Chi Chen, Iren Wang, Meng-RuHo, Shang-Te Danny Hsu, Yi-Fang Zeng, Yu-Ning Huang, Je-Ruei Liu and Rey-Ting Guo
  
  The β-L-arabinofuranosidase from Bifidobacterium longum JCM 1217 (HypBA1), a DUF1680 family member, was recently characterized and classified to the glycoside hydrolase family 127 (GH127) by CAZy. The HypBA1 exerts exo-glycosidase activity to hydrolyze β-1,2-linked arabinofuranose disaccharides from non-reducing end into individual L-arabinoses. In this study, the crystal structures of HypBA1 and its complex with L-arabinose and Zn2+ ion were determined at 2.23-2.78 Å resolution. HypBA1 consists of three domains, denoted N-, S- and C-domain. The N-domain (residues 1-5 and 434-538) and C-domain (residues 539-658) adopt β-jellyroll architectures, and the S-domain (residues 6-433) adopts an (α/α)6-barrel fold. HypBA1 utilizes the S- and C-domain to form a functional dimer. The complex structure suggests that the catalytic core lies in the S-domain.. Read More»
  DOI: 10.4172/2155-9821.1000171

  Abstract PDF