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:
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
Kallikrein-1 (preferred)
PDBe Complex ID:
PDB-CPX-529855 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Kallikrein-1
Molecule details ›
Chain: A
Length: 238 amino acids
Theoretical weight: 26.43 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Length: 238 amino acids
Theoretical weight: 26.43 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
- Canonical:
P06870 (Residues: 25-262; Coverage: 98%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
