| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 8296178 | Biochemical and Biophysical Research Communications | 2017 | 6 Pages |
Abstract
The X-ray structure of Clostridium perfringens class B sortase demonstrated that the unique position of the catalytic Cys232 is preferable for catalytic reaction, and that the movement of Cys232 may help His136 deprotonate Cys232 to be activated as a thiolate.282
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Biochemistry
Authors
Eiji Tamai, Hiroshi Sekiya, Jun Maki, Hirofumi Nariya, Hiromi Yoshida, Shigehiro Kamitori,