Article
Molecular and biochemical evidence for the involvement of the Asp-333-His-523 pair in the catalytic mechanism of soluble epoxide hydrolase.
The Journal of biological chemistry - 7 Apr 1995
Pinot F, Grant D F, Beetham J K, Parker A G, Borhan B, Landt S, Jones A D, Hammock B D
Abstract excerpt
In order to investigate the involvement of amino acids in the catalytic mechanism of the soluble epoxide hydrolase, different mutants of the murine enzyme were produced using the baculovirus expression system. Our results are consistent with the involvement of Asp-333 and His-523 in a catalytic mechanism similar to that of other alpha/beta hydrolase fold enzymes. Mutation of His-263 to asparagine led to the loss...
Topics
- Amino Acid Sequence
- Animals
- Aspartic Acid
- Base Sequence
- Catalysis
- Cloning, Molecular
- Epoxide Hydrolases
- Histidine
- Mice
- Molecular Sequence Data
- Mutation