| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10755974 | Biochemical and Biophysical Research Communications | 2014 | 6 Pages |
Abstract
- HypBA1 β-l-arabinofuranosidase belongs to glycoside hydrolase family 127.
- Crystal structure of HypBA1 was determined.
- HypBA1 consists of a catalytic barrel and two additional β-sandwich domains.
- The active site contains a Zn2+ coordinated by glutamate and three cysteines.
- A possible reaction mechanism involving cysteine as the nucleophile is proposed.
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Biochemistry
Authors
Tasuku Ito, Kyo Saikawa, Seonah Kim, Kiyotaka Fujita, Akihiro Ishiwata, Sophon Kaeothip, Takatoshi Arakawa, Takayoshi Wakagi, Gregg T. Beckham, Yukishige Ito, Shinya Fushinobu,