EC Number   |
Reaction |
Reference |
|---|
   3.4.23.49 | Has a virtual requirement for Arg in the P1 position and a slightly less stringent preference for this residue in the P1' position, which can also contain Lys, Gly or Val. |
- |
- |
| 3.4.23.49 | Has a virtual requirement for Arg in the P1 position and a slightly less stringent preference for this residue in the P1' position, which can also contain Lys, Gly or Val. |
active site structure, catalytic residues are Asp210 an His212, molecular dynamic simulations reveal substrate binding structure and structural requirements for the catalytic mechanism |
661351 |
| 3.4.23.49 | Has a virtual requirement for Arg in the P1 position and a slightly less stringent preference for this residue in the P1' position, which can also contain Lys, Gly or Val. |
the consensus sequence of OmpT is R/K-A, the enzyme is highly selective for a basic amino acid residue at position P1, but less exclusive at P1', where several non-basic amino acids are tolerated, enzyme residue Asp97 is responsible for interaction with P1' position substrate residue |
660757 |
| 3.4.23.49 | Has a virtual requirement for Arg in the P1 position and a slightly less stringent preference for this residue in the P1' position, which can also contain Lys, Gly or Val. |
the enzyme contains a Ser-Asp-His catalytic triad, active site, the consensus sequence of OmpT is R/K*-R/K, the enzyme is highly selective for a basic amino acid residue at position P1, but less exclusive at P1', where several amino acids are tolerated e,g, Lys, Val, and Gly, at P2' common residues are Ala or Val, at P3 and P4 the enzyme prefers Trp or Arg |
662017 |
| 3.4.23.49 | Has a virtual requirement for Arg in the P1 position and a slightly less stringent preference for this residue in the P1' position, which can also contain Lys, Gly or Val. |
the enzyme contains a Ser-Asp-His catalytic triad, active site, the consensus sequence of OmpT is R/K-R/K-A, the enzyme is highly selective for a basic amino acid residue at position P1, but less exclusive at P1', where several amino acids are tolerated, OmpP shows similar specificity, minor sequence variations in the surface loops near the catalytic residue have profound effects on the target specificity of the enzyme |
661904 |
| 3.4.23.49 | Has a virtual requirement for Arg in the P1 position and a slightly less stringent preference for this residue in the P1' position, which can also contain Lys, Gly or Val. |
the enzyme contains a Ser-Asp-His catalytic triad, active site, the enzyme prefers a basic amino acid residue at position P1, but is less exclusive at P1', where several amino acids are tolerated, minor sequence variations in the surface loops near the catalytic residue have profound effects on the target specificity of the enzyme |
661904 |
