EC Number |
Reaction |
Reference |
---|
3.4.21.19 | Preferential cleavage: Glu-/-, Asp-/- |
- |
- |
3.4.21.19 | Preferential cleavage: Glu-/-, Asp-/- |
absolutely specific for cleavage sites Glu-/-Xaa and Asp-/-Xaa, cleavage exclusively at the carboxylic side, active site Ser169 |
649239 |
3.4.21.19 | Preferential cleavage: Glu-/-, Asp-/- |
catalytic tetrad of His213, Asp102, Ser195, and Trp214, computer modeling of S1 and S'1 sites of the enzyme's active site |
-, 653874 |
3.4.21.19 | Preferential cleavage: Glu-/-, Asp-/- |
catalytic triad of His, Asp, and Ser |
653874 |
3.4.21.19 | Preferential cleavage: Glu-/-, Asp-/- |
catalytic triad of His, Asp, and Ser, computer modeling of active site structure, S1-substrate binding site, and substrate binding mechanism |
653874 |
3.4.21.19 | Preferential cleavage: Glu-/-, Asp-/- |
catalytic triad of His, Asp, and Ser, substrate binding mechanism and structure |
653874 |
3.4.21.19 | Preferential cleavage: Glu-/-, Asp-/- |
specific for cleavage on the carboxylic site of glutamic acid, catalytic site are His47 and Ser171, the N-terminus is involved in formation of the substrate binding pocket, a direct structural relation between zymogen activation and substrate charge compensation exists |
650241 |