| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 6531103 | Journal of Molecular Catalysis B: Enzymatic | 2014 | 9 Pages |
Abstract
- We theoretically analyzed l-2-haloacid dehalogenase from Pseudomonas sp. YL.
- The energy profile of the ester intermediate formation step was elucidated.
- Arg41 could accept the chloride ion released from the substrate.
- We compared eight mutant enzymes at Arg41 by mutagenesis simulations.
- Simulations suggested R41homK mutant could be as active as the wild-type enzyme.
Related Topics
Physical Sciences and Engineering
Chemical Engineering
Catalysis
Authors
Hirotaka Kondo, Takashi Nakamura, Shigenori Tanaka,