Function and Biology Details
Reaction catalysed:
Preferential cleavage of Arg-|- bonds in small molecule substrates. Highly selective action to release kallidin (lysyl-bradykinin) from kininogen involves hydrolysis of Met-|- or Leu-|-. The rat enzyme is unusual in liberating bradykinin directly from autologous kininogens by cleavage at two Arg-|- bonds (5).
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:
Structure analysis Details
Assemblies composition:
Assembly name:
Tonin (preferred)
PDBe Complex ID:
PDB-CPX-133317 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tonin
Molecule details ›
Chain: A
Length: 235 amino acids
Theoretical weight: 25.69 KDa
Source organism: Rattus rattus
Expression system: Not provided
UniProt:
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Length: 235 amino acids
Theoretical weight: 25.69 KDa
Source organism: Rattus rattus
Expression system: Not provided
UniProt:
- Canonical:
P00759 (Residues: 25-259; Coverage: 98%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
