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 domains:
Structure analysis Details
Assembly composition:
hetero hexamer (preferred)
PDBe Complex ID:
PDB-CPX-133316 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (4 distinct):
Kallikrein 1-related peptidase-like b4
Molecule details ›
Chains: A, X
Length: 240 amino acids
Theoretical weight: 26.78 KDa
Source organism: Mus musculus
UniProt:
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Length: 240 amino acids
Theoretical weight: 26.78 KDa
Source organism: Mus musculus
UniProt:
- Canonical:
P00757 (Residues: 17-256; Coverage: 100%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Beta-nerve growth factor
Molecule details ›
Chains: B, Y
Length: 118 amino acids
Theoretical weight: 13.28 KDa
Source organism: Mus musculus
UniProt:
Sequence domains: Nerve growth factor family
Structure domains: Cystine-knot cytokines
Length: 118 amino acids
Theoretical weight: 13.28 KDa
Source organism: Mus musculus
UniProt:
- Canonical: P01139 (Residues: 122-239; Coverage: 53%)
Sequence domains: Nerve growth factor family
Structure domains: Cystine-knot cytokines
Kallikrein 1-related peptidase b3
Molecule details ›
Chains: G, Z
Length: 237 amino acids
Theoretical weight: 26.43 KDa
Source organism: Mus musculus
UniProt:
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Length: 237 amino acids
Theoretical weight: 26.43 KDa
Source organism: Mus musculus
UniProt:
- Canonical: P00756 (Residues: 25-261; Coverage: 98%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
